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\n \n\n \n \n \n \n \n \n The liquid fraction from hydrothermal pretreatment of wheat straw provides lytic polysaccharide monooxygenases with both electrons and H2O2 co-substrate.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Biotechnology for Biofuels, 12(1). 2019.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"The$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n \n \n 2 downloads\n \n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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\n \n\n \n \n \n \n \n \n Erratum: Retraction for polev et al., \"Draft genome sequence of Geotrichum candidum Strain 3C\" (Microbiol Resour Announc (2019) 8:e00561-19. doi.10.1128/genomeA.00956-14).\n \n \n \n \n\n\n \n Polev, D.; Bobrov, K.; Eneyskaya, E.; and Kulminskaya, A.\n\n\n \n\n\n\n Microbiology Resource Announcements, 8(24). 2019.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Erratum:$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Polev2019,\r\nauthor={Polev, D.E. and Bobrov, K.S. and Eneyskaya, E.V. and Kulminskaya, A.A.},\r\ntitle={Erratum: Retraction for polev et al., "Draft genome sequence of Geotrichum candidum Strain 3C" (Microbiol Resour Announc (2019) 8:e00561-19. doi.10.1128/genomeA.00956-14)},\r\njournal={Microbiology Resource Announcements},\r\nyear={2019},\r\nvolume={8},\r\nnumber={24},\r\ndoi={10.1128/MRA.00561-19},\r\nart_number={e00561-19},\r\nnote={cited By 0},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-85069478479&doi=10.1128%2fMRA.00561-19&partnerID=40&md5=7b812082ec64d305fb2e108b02888af7},\r\naffiliation={Research Resource Center for Molecular and Cell Technologies, St. Petersburg State University, St. Petersburg, Russian Federation; National Research Centre, Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Orlova Roscha, Russian Federation; St. Petersburg State Polytechnical University, St. Petersburg, Russian Federation},\r\nabstract={Volume 2, no. 5, e00956-14, 2014, https://doi.org/10.1128/genomeA.00956-14. We retract this article. The Geotrichum candidum strain 3C was initially identified and classified in the early 1970s (N. A. Rodionova, N. A. Tiunova, R. V. Feniksova, T. I. Kudriashova, and L. I. Martinovich, Dokl Akad Nauk SSSR 214:1206 -1209, 1974). In 2014, we had sequenced and published its draft genome, so the genome analysis of the strain became possible (D. E. Polev, K. S. Bobrov, E. V. Eneyskaya, and A. A. Kulminskaya, Genome Announc 2:e00956-14, 2014, https://doi.org/10.1128/genomeA.00956-14). After the publication of the draft genome sequence of the G. candidum strain CLIB 918 (ATCC 204307) in 2015 (G. Morel, L. Sterck, D. Swennen, M. Marcet-Houben, et al., Sci Rep 5:11571, 2015, https://doi.org/10.1038/srep11571 [Erratum, 5:12596, https://doi .org/10.1038/srep12596]) and due to the inconsistency between these genome sequences, it became clear that G. candidum strain 3C needed to be reclassified. In further work, the yeast-like fungus previously known as G. candidum 3C was reclassified as Scytalidium candidum 3C (I. Y. Pavlov, K. S. Bobrov, A. D. Sumacheva, A. E. Masharsky, et al., J Basic Microbiol 58:883- 891, 2018, https://doi.org/10.1002/jobm.201800066). We apologize to the readers of Genome Announcements/Microbiology Resource Announcements for any inconvenience that this causes. Copyright © 2019 Polev et al.},\r\ncorrespondence_address1={Polev, D.E.; Research Resource Center for Molecular and Cell Technologies, St. Petersburg State UniversityRussian Federation; email: dmitry.polev@gmail.com},\r\npublisher={American Society for Microbiology},\r\nissn={2576098X},\r\nlanguage={English},\r\nabbrev_source_title={Micro. Res. Ann},\r\ndocument_type={Erratum},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Comprehensive Analysis of Carbohydrate-Active Enzymes from the Filamentous Fungus Scytalidium candidum 3C.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Biochemistry (Moscow), 83(11): 1399-1410. 2018.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Comprehensive$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n \n \n 1 download\n \n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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\n \n\n \n \n \n \n \n \n Scytalidium candidum 3C is a new name for the Geotrichum candidum Link 3C strain.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Journal of Basic Microbiology, 58(10): 883-891. 2018.\n cited By 2\n\n\n\n
\n\n\n\n \n \n $\"Scytalidium$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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\n \n\n \n \n \n \n \n \n Microbial Sulfatases.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Moscow University Chemistry Bulletin, 73(4): 139-151. 2018.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Microbial$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n \n \n 1 download\n \n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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\n \n 2017\n \n \n (4)\n \n \n

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\n \n\n \n \n \n \n \n \n Heterologous expression in Pichia pastoris and biochemical characterization of the unmodified sulfatase from Fusarium proliferatum LE1.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Protein Engineering, Design and Selection, 30(7): 477-488. 2017.\n cited By 2\n\n\n\n
\n\n\n\n \n \n $\"Heterologous$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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\n \n\n \n \n \n \n \n \n Corrigendum to “Characterization of a new α-L-fucosidase isolated from Fusarium proliferatum LE1 that is regioselective to α-(1 → 4)-L-fucosidic linkage in the hydrolysis of α-L-fucobiosides” [Biochimie (2017) 132C (54–65)] (S0300908416303029) (10.1016/j.biochi.2016.10.014).\n \n \n \n \n\n\n \n Shvetsova, S.; Shabalin, K.; Bobrov, K.; Ivanen, D.; Ustyuzhanina, N.; Krylov, V.; Nifantiev, N.; Naryzhny, S.; Zgoda, V.; Eneyskaya, E.; and Kulminskaya, A.\n\n\n \n\n\n\n Biochimie, 137: 198. 2017.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Corrigendum$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Shvetsova2017198,\r\nauthor={Shvetsova, S.V. and Shabalin, K.A. and Bobrov, K.S. and Ivanen, D.R. and Ustyuzhanina, N.E. and Krylov, V.B. and Nifantiev, N.E. and Naryzhny, S.N. and Zgoda, V.G. and Eneyskaya, E.V. and Kulminskaya, A.A.},\r\ntitle={Corrigendum to “Characterization of a new α-L-fucosidase isolated from Fusarium proliferatum LE1 that is regioselective to α-(1 → 4)-L-fucosidic linkage in the hydrolysis of α-L-fucobiosides” [Biochimie (2017) 132C (54–65)] (S0300908416303029) (10.1016/j.biochi.2016.10.014)},\r\njournal={Biochimie},\r\nyear={2017},\r\nvolume={137},\r\npages={198},\r\ndoi={10.1016/j.biochi.2017.04.007},\r\nnote={cited By 0},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-85018899144&doi=10.1016%2fj.biochi.2017.04.007&partnerID=40&md5=c6e162583a61b1d5dcf12b5dd03029b4},\r\naffiliation={National Research Center «Kurchatov Institute», B.P. Konstantinov Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina, 188300, Russian Federation; Department of Medical Physics, Peter the Great St. Petersburg Polytechnic University, Chlopina Str. 5, St. Petersburg, 195251, Russian Federation; Peter the Great St. Petersburg Polytechnic University, Polytechnicheskaya Str., 29, St. Petersburg, 195251, Russian Federation; N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 47, Leninsky Pr., Moscow, 119991, Russian Federation; Institute of Biomedical Chemistry, Pogodinskaya 10, Moscow, 119121, Russian Federation},\r\nabstract={The authors would like to inform readers of needed clarifications to this article: 1. page 55, the second column, line 12: pNPαGal instead of pNP αGal.2. page 59, section 3.3, references to Figure 2 should be to Figure 3. Line 6: Fig. 2A should be Fig. 3A; line 10: Fig. 2B should be Fig. 3B; line 11: Fig. 2C should be Fig. 3C; line 14: Fig. 2D should be Fig. 3D.3. page 61, section 3.5, lines 3 and 4: in the sentence starting “The highest affinity …” the numbering of fucobiosides should be corrected and should read “The highest affinity was observed for the L-Fuc-α-(1→4)-L-Fuc-α-OPr and the lowest one was for the L-Fuc-α-(1→3)-L-Fuc-α-OPr”.4. page 63, Acknowledgments: please remove Table 2S and add Fig. 3S in line 8. It should read: … syntheses of the p-nitrophenyl glycoside substrates and the experiments depicted in Figs. 4–6, 1S and 3S, Tables 1 and 5 as well as sample preparation for gene sequencing and analysis were supported by the RSF grant 16-14-00109; …The authors wish to apologise for any inconvenience caused. © 2017},\r\ncorrespondence_address1={Kulminskaya, A.A.; Laboratory of Enzymology, National Research Center «Kurchatov Institute», B.P. Konstantinov Petersburg Nuclear Physics Institute, Orlova roscha, Russian Federation; email: kulm@omrb.pnpi.spb.ru},\r\npublisher={Elsevier B.V.},\r\nissn={03009084},\r\ncoden={BICMB},\r\npubmed_id={28434920},\r\nlanguage={English},\r\nabbrev_source_title={Biochimie},\r\ndocument_type={Erratum},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n A comparison of the effect of fucoidan from alga Fucus vesiculosus and its fractions obtained by anion-exchange chromatography on HeLa G-63, Hep G2, and Chang liver cells.\n \n \n \n \n\n\n \n Zhurishkina, E.; Stepanov, S.; Shvetsova, S.; Kulminskaya, A.; and Lapina, I.\n\n\n \n\n\n\n Cell and Tissue Biology, 11(3): 242-249. 2017.\n cited By 2\n\n\n\n
\n\n\n\n \n \n $\"A$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Zhurishkina2017242,\r\nauthor={Zhurishkina, E.V. and Stepanov, S.I. and Shvetsova, S.V. and Kulminskaya, A.A. and Lapina, I.M.},\r\ntitle={A comparison of the effect of fucoidan from alga Fucus vesiculosus and its fractions obtained by anion-exchange chromatography on HeLa G-63, Hep G2, and Chang liver cells},\r\njournal={Cell and Tissue Biology},\r\nyear={2017},\r\nvolume={11},\r\nnumber={3},\r\npages={242-249},\r\ndoi={10.1134/S1990519X17030117},\r\nnote={cited By 2},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-85020387177&doi=10.1134%2fS1990519X17030117&partnerID=40&md5=d27abe92e2332552ac7f56409535a045},\r\naffiliation={Russian Research Centre Kurchatov Institute, Gatchina, Leningrad oblast  188300, Russian Federation; Department of Medical Physics, Peter the Great St. Petersburg Polytechnic University, St. Petersburg, 195251, Russian Federation},\r\nabstract={The aim of this study was to compare the effects of sulfated fucopolysaccharides isolated from Fucus vesiculosus on HeLa G-63, Hep G2, and Chang liver cells. Native fucoidan F3 and two fractions (F3-0.5 and F3-1) obtained by anion-exchange chromatography were analyzed using chemical methods and IR spectroscopy. It was demonstrated that F3 and F3-1 are characterized by a higher content of sulfates, location of sulfo groups mostly at the C4 atom of fucose residue, and low content of uronic acids inhibited cell proliferation. Human liver carcinoma Hep G2 appeared to be the most sensitive to fucoidan, whereas nonmalignant human Chang liver cells were the least sensitive. © 2017, Pleiades Publishing, Ltd.},\r\nauthor_keywords={fucoidan;  human cell lines;  sulfated polysaccharides},\r\ncorrespondence_address1={Zhurishkina, E.V.; Russian Research Centre Kurchatov InstituteRussian Federation; email: furfur@yandex.ru},\r\npublisher={Maik Nauka-Interperiodica Publishing},\r\nissn={1990519X},\r\nlanguage={English},\r\nabbrev_source_title={Cell Tissue Biol.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Characterization of a new α-L-fucosidase isolated from Fusarium proliferatum LE1 that is regioselective to α-(1 → 4)-L-fucosidic linkage in the hydrolysis of α-L-fucobiosides.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Biochimie, 132: 54-65. 2017.\n cited By 5\n\n\n\n
\n\n\n\n \n \n $\"Characterization$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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\n \n\n \n \n \n \n \n \n Biochemical and structural characterizations of two Dictyostelium cellobiohydrolases from the Amoebozoa kingdom reveal a high level of conservation between distant phylogenetic trees of life.\n \n \n \n \n\n\n \n Hobdey, S.; Knott, B.; Momeni, M.; Taylor, L.; Borisova, A.; Podkaminer, K.; VanderWall, T.; Himmel, M.; Decker, S.; Beckham, G.; and Ståhlberg, J.\n\n\n \n\n\n\n Applied and Environmental Microbiology, 82(11): 3395-3409. 2016.\n cited By 4\n\n\n\n
\n\n\n\n \n \n $\"Biochemical$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Hobdey20163395,\r\nauthor={Hobdey, S.E. and Knott, B.C. and Momeni, M.H. and Taylor, L.E., II and Borisova, A.S. and Podkaminer, K.K. and VanderWall, T.A. and Himmel, M.E. and Decker, S.R. and Beckham, G.T. and Ståhlberg, J.},\r\ntitle={Biochemical and structural characterizations of two Dictyostelium cellobiohydrolases from the Amoebozoa kingdom reveal a high level of conservation between distant phylogenetic trees of life},\r\njournal={Applied and Environmental Microbiology},\r\nyear={2016},\r\nvolume={82},\r\nnumber={11},\r\npages={3395-3409},\r\ndoi={10.1128/AEM.00163-16},\r\nnote={cited By 4},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84971320437&doi=10.1128%2fAEM.00163-16&partnerID=40&md5=3bbc140ea172a8e7c982b186fdb385a0},\r\naffiliation={Biosciences Center, National Renewable Energy Laboratory, Golden, CO, United States; National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO, United States; Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, Uppsala, Sweden; Idaho Veterans Research and Education Foundation, VA Medical Center, Boise, ID, United States; Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Kongens Lyngby, Denmark},\r\nabstract={Glycoside hydrolase family 7 (GH7) cellobiohydrolases (CBHs) are enzymes commonly employed in plant cell wall degradation across eukaryotic kingdoms of life, as they provide significant hydrolytic potential in cellulose turnover. To date, many fungal GH7 CBHs have been examined, yet many questions regarding structure-activity relationships in these important natural and commercial enzymes remain. Here, we present the crystal structures and a biochemical analysis of two GH7 CBHs from social amoeba: Dictyostelium discoideum Cel7A (DdiCel7A) and Dictyostelium purpureum Cel7A (DpuCel7A). DdiCel7A and DpuCel7A natively consist of a catalytic domain and do not exhibit a carbohydrate-binding module (CBM). The structures of DdiCel7A and DpuCel7A, resolved to 2.1 Å and 2.7 Å, respectively, are homologous to those of other GH7 CBHs with an enclosed active-site tunnel. Two primary differences between the Dictyostelium CBHs and the archetypal model GH7 CBH, Trichoderma reesei Cel7A (TreCel7A), occur near the hydrolytic active site and the product-binding sites. To compare the activities of these enzymes with the activity of TreCel7A, the family 1 TreCel7A CBM and linker were added to the C terminus of each of the Dictyostelium enzymes, creating DdiCel7ACBM and DpuCel7ACBM, which were recombinantly expressed in T. reesei. DdiCel7ACBM and DpuCel7ACBM hydrolyzed Avicel, pretreated corn stover, and phosphoric acid-swollen cellulose as efficiently as TreCel7A when hydrolysis was compared at their temperature optima. TheKi of cellobiose was significantly higher for DdiCel7ACBM and DpuCel7ACBM than for TreCel7A: 205, 130, and 29μM, respectively. Taken together, the present study highlights the remarkable degree of conservation of the activity of these key natural and industrial enzymes across quite distant phylogenetic trees of life. © 2016, American Society for Microbiology. All Rights Reserved.},\r\ncorrespondence_address1={Beckham, G.T.; National Bioenergy Center, National Renewable Energy LaboratoryUnited States; email: gregg.beckham@nrel.gov},\r\npublisher={American Society for Microbiology},\r\nissn={00992240},\r\ncoden={AEMID},\r\npubmed_id={27037126},\r\nlanguage={English},\r\nabbrev_source_title={Appl. Environ. Microbiol.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3.\n \n \n \n \n\n\n \n Zhemkov, V.; Kulminskaya, A.; Bezprozvanny, I.; and Kim, M.\n\n\n \n\n\n\n FEBS Open Bio, 6(3): 168-178. 2016.\n cited By 6\n\n\n\n
\n\n\n\n \n \n $\"The$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Zhemkov2016168,\r\nauthor={Zhemkov, V.A. and Kulminskaya, A.A. and Bezprozvanny, I.B. and Kim, M.},\r\ntitle={The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3},\r\njournal={FEBS Open Bio},\r\nyear={2016},\r\nvolume={6},\r\nnumber={3},\r\npages={168-178},\r\ndoi={10.1002/2211-5463.12029},\r\nnote={cited By 6},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84975760011&doi=10.1002%2f2211-5463.12029&partnerID=40&md5=20145a54e32e78938457758cf8de8577},\r\naffiliation={Laboratory of Molecular Neurodegeneration, St Petersburg State Polytechnical University, Russian Federation; Laboratory of Enzymology, National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Russian Federation; Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX, United States},\r\nabstract={An expansion of polyglutamine (polyQ) sequence in ataxin-3 protein causes spinocerebellar ataxia type 3, an inherited neurodegenerative disorder. The crystal structure of the polyQ-containing carboxy-terminal fragment of human ataxin-3 was solved at 2.2-Å resolution. The Atxn3 carboxy-terminal fragment including 14 glutamine residues adopts both random coil and α-helical conformations in the crystal structure. The polyQ sequence in α-helical structure is stabilized by intrahelical hydrogen bonds mediated by glutamine side chains. The intrahelical hydrogen-bond interactions between glutamine side chains along the axis of the polyQ α-helix stabilize the secondary structure. Analysis of this structure furthers our understanding of the polyQ-structural characteristics that likely underlie the pathogenesis of polyQ-expansion disorders. © 2016 Federation of European Biochemical Societies.},\r\nauthor_keywords={Ataxia;  Ataxins;  Huntington's disease;  Polyglutamine;  Triplet repeat disorder},\r\ncorrespondence_address1={Kim, M.; Department of Physiology, University of Texas Southwestern Medical CenterUnited States; email: Meewhi.Kim@UTSouthwestern.edu},\r\npublisher={Elsevier B.V.},\r\nissn={22115463},\r\nlanguage={English},\r\nabbrev_source_title={FEBS Open Bio.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Sequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3C.\n \n \n \n \n\n\n \n Borisova, A.; Eneyskaya, E.; Bobrov, K.; Jana, S.; Logachev, A.; Polev, D.; Lapidus, A.; Ibatullin, F.; Saleem, U.; Sandgren, M.; Payne, C.; Kulminskaya, A.; and Stahlberg, J.\n\n\n \n\n\n\n FEBS Journal, 282(23): 4515-4537. 2015.\n cited By 14\n\n\n\n
\n\n\n\n \n \n $\"Sequencing,$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n \n \n 3 downloads\n \n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Borisova20154515,\r\nauthor={Borisova, A.S. and Eneyskaya, E.V. and Bobrov, K.S. and Jana, S. and Logachev, A. and Polev, D.E. and Lapidus, A.L. and Ibatullin, F.M. and Saleem, U. and Sandgren, M. and Payne, C.M. and Kulminskaya, A.A. and Stahlberg, J.},\r\ntitle={Sequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3C},\r\njournal={FEBS Journal},\r\nyear={2015},\r\nvolume={282},\r\nnumber={23},\r\npages={4515-4537},\r\ndoi={10.1111/febs.13509},\r\nnote={cited By 14},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84961331730&doi=10.1111%2ffebs.13509&partnerID=40&md5=b1587711d771fe0a70ea4e28e8780d03},\r\naffiliation={Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, PO Box 7015, Uppsala, SE-750 07, Sweden; National Research Centre Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Orlova roscha, 188300, Russian Federation; Department of Chemical and Materials Engineering, University of Kentucky, 177 F. Paul Anderson Tower, Lexington, KY  40506, United States; Theodosius Dobzhansky Center for Genome Bioinformatics, St. Petersburg State University, Russian Federation; Research Resource Centre Molecular and Cell Technologies, St. Petersburg State University, Russian Federation; Centre for Algorithmic Biotechnology, St. Petersburg Academic University, Russian Federation; Department of Medical Physics, Peter the Great St. Petersburg Polytechnic University, Russian Federation; Umair Saleem, Birkedommervej 17 3TH, København NV, 2400, Denmark},\r\nabstract={The ascomycete Geotrichum candidum is a versatile and efficient decay fungus that is involved, for example, in biodeterioration of compact discs; notably, the 3C strain was previously shown to degrade filter paper and cotton more efficiently than several industrial enzyme preparations. Glycoside hydrolase (GH) family 7 cellobiohydrolases (CBHs) are the primary constituents of industrial cellulase cocktails employed in biomass conversion, and feature tunnel-enclosed active sites that enable processive hydrolytic cleavage of cellulose chains. Understanding the structure-function relationships defining the activity and stability of GH7 CBHs is thus of keen interest. Accordingly, we report the comprehensive characterization of the GH7 CBH secreted by G. candidum (GcaCel7A). The bimodular cellulase consists of a family 1 cellulose-binding module (CBM) and linker connected to a GH7 catalytic domain that shares 64% sequence identity with the archetypal industrial GH7 CBH of Hypocrea jecorina (HjeCel7A). GcaCel7A shows activity on Avicel cellulose similar to HjeCel7A, with less product inhibition, but has a lower temperature optimum (50 °C versus 60-65 °C, respectively). Five crystal structures, with and without bound thio-oligosaccharides, show conformational diversity of tunnel-enclosing loops, including a form with partial tunnel collapse at subsite -4 not reported previously in GH7. Also, the first O-glycosylation site in a GH7 crystal structure is reported - on a loop where the glycan probably influences loop contacts across the active site and interactions with the cellulose surface. The GcaCel7A structures indicate higher loop flexibility than HjeCel7A, in accordance with sequence modifications. However, GcaCel7A retains small fluctuations in molecular simulations, suggesting high processivity and low endo-initiation probability, similar to HjeCel7A. Database Structural data are available in the Protein Data Bank under the accession numbers 5AMP, 4ZZV, 4ZZW, 4ZZT, and 4ZZU. The Geotrichum candidum GH family 7 cellobiohydrolase nucleotide sequence is available in GenBank under accession number KJ958925. Enzymes Glycoside hydrolase family 7 reducing end acting cellobiohydrolase We report the characterization of the GH7 CBH secreted by ascomycete G. candidum (GcaCel7A). X-ray data revealed the first O-glycosylation in a GH7 crystal structure on a loop where the glycan influences loop contacts and interactions with the cellulose surface. Even though GcaCel7A structures indicate higher loop flexibility than H. jecorina Cel7A, molecular simulations suggest high processivity and low endo-initiation probability similar to HjeCel7A. © 2015 FEBS.},\r\nauthor_keywords={biomass degradation;  cellulase;  Geotrichum candidum;  molecular dynamics;  X-ray structure},\r\ncorrespondence_address1={Stahlberg, J.; Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, PO Box 7015, Sweden; email: Jerry.Stahlberg@slu.se},\r\npublisher={Blackwell Publishing Ltd},\r\nissn={1742464X},\r\ncoden={FJEOA},\r\npubmed_id={26367132},\r\nlanguage={English},\r\nabbrev_source_title={FEBS J.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n The ascomycete Geotrichum candidum is a versatile and efficient decay fungus that is involved, for example, in biodeterioration of compact discs; notably, the 3C strain was previously shown to degrade filter paper and cotton more efficiently than several industrial enzyme preparations. Glycoside hydrolase (GH) family 7 cellobiohydrolases (CBHs) are the primary constituents of industrial cellulase cocktails employed in biomass conversion, and feature tunnel-enclosed active sites that enable processive hydrolytic cleavage of cellulose chains. Understanding the structure-function relationships defining the activity and stability of GH7 CBHs is thus of keen interest. Accordingly, we report the comprehensive characterization of the GH7 CBH secreted by G. candidum (GcaCel7A). The bimodular cellulase consists of a family 1 cellulose-binding module (CBM) and linker connected to a GH7 catalytic domain that shares 64% sequence identity with the archetypal industrial GH7 CBH of Hypocrea jecorina (HjeCel7A). GcaCel7A shows activity on Avicel cellulose similar to HjeCel7A, with less product inhibition, but has a lower temperature optimum (50 °C versus 60-65 °C, respectively). Five crystal structures, with and without bound thio-oligosaccharides, show conformational diversity of tunnel-enclosing loops, including a form with partial tunnel collapse at subsite -4 not reported previously in GH7. Also, the first O-glycosylation site in a GH7 crystal structure is reported - on a loop where the glycan probably influences loop contacts across the active site and interactions with the cellulose surface. The GcaCel7A structures indicate higher loop flexibility than HjeCel7A, in accordance with sequence modifications. However, GcaCel7A retains small fluctuations in molecular simulations, suggesting high processivity and low endo-initiation probability, similar to HjeCel7A. Database Structural data are available in the Protein Data Bank under the accession numbers 5AMP, 4ZZV, 4ZZW, 4ZZT, and 4ZZU. The Geotrichum candidum GH family 7 cellobiohydrolase nucleotide sequence is available in GenBank under accession number KJ958925. Enzymes Glycoside hydrolase family 7 reducing end acting cellobiohydrolase We report the characterization of the GH7 CBH secreted by ascomycete G. candidum (GcaCel7A). X-ray data revealed the first O-glycosylation in a GH7 crystal structure on a loop where the glycan influences loop contacts and interactions with the cellulose surface. Even though GcaCel7A structures indicate higher loop flexibility than H. jecorina Cel7A, molecular simulations suggest high processivity and low endo-initiation probability similar to HjeCel7A. © 2015 FEBS.\n

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\n \n\n \n \n \n \n \n \n Structural and functional characterization of a lytic polysaccharide monooxygenase with broad substrate specificity.\n \n \n \n \n\n\n \n Borisova, A.; Isaksen, T.; Dimarogona, M.; Kognole, A.; Mathiesen, G.; Várnai, A.; Røhr, Å.; Payne, C.; Sørlie, M.; Sandgren, M.; and Eijsink, V.\n\n\n \n\n\n\n Journal of Biological Chemistry, 290(38): 22955-22969. 2015.\n cited By 74\n\n\n\n
\n\n\n\n \n \n $\"Structural$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Borisova201522955,\r\nauthor={Borisova, A.S. and Isaksen, T. and Dimarogona, M. and Kognole, A.A. and Mathiesen, G. and Várnai, A. and Røhr, Å.K. and Payne, C.M. and Sørlie, M. and Sandgren, M. and Eijsink, V.G.H.},\r\ntitle={Structural and functional characterization of a lytic polysaccharide monooxygenase with broad substrate specificity},\r\njournal={Journal of Biological Chemistry},\r\nyear={2015},\r\nvolume={290},\r\nnumber={38},\r\npages={22955-22969},\r\ndoi={10.1074/jbc.M115.660183},\r\nnote={cited By 74},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84942879811&doi=10.1074%2fjbc.M115.660183&partnerID=40&md5=ef57f93717569c3c28b35ac2eb492255},\r\naffiliation={Dept. of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, Uppsala, SE-750 07, Sweden; Dept. of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences, Ås, N-1432, Norway; Department of Biosciences, University of Oslo, Oslo, N-0316, Norway; Department of Chemical and Materials Engineering, University of Kentucky, Lexington, KY  40506, United States},\r\nabstract={The recently discovered lytic polysaccharide monooxygenases (LPMOs) carry out oxidative cleavage of polysaccharides and are of major importance for efficient processing of biomass. NcLPMO9C from Neurospora crassa acts both on cellulose and on non-celluloseβ-glucans, including cellodextrins and xyloglucan. The crystal structure of the catalytic domain of NcLPMO9C revealed an extended, highly polar substrate-binding surface well suited to interact with a variety of sugar substrates. The ability of NcLPMO9C to act on soluble substrates was exploited to study enzyme-substrate interactions. EPR studies demonstrated that the Cu2+ center environment is altered upon substrate binding, whereas isothermal titration calorimetry studies revealed binding affinities in the low micromolar range for polymeric substrates that are due in part to the presence of a carbohydrate-binding module (CBM1). Importantly, the novel structure of NcLPMO9Cenabled a comparative study, revealing that the oxidative regioselectivity of LPMO9s (C1, C4, or both) correlates with distinct structural features of the copper coordination sphere. In strictly C1-oxidizing LPMO9s, access to the solvent-facing axial coordination position is restricted by a conserved tyrosine residue, whereas access to this same position seems unrestricted in C4-oxidizing LPMO9s. LPMO9s known to produce a mixture of C1- and C4-oxidized products show an intermediate situation. © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.},\r\n}

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\n \n\n \n \n \n \n \n \n The method of integrated kinetics and its applicability to the exo-glycosidase-catalyzed hydrolyses of p-nitrophenyl glycosides.\n \n \n \n \n\n\n \n Borisova, A.; Reddy, S.; Ivanen, D.; Bobrov, K.; Eneyskaya, E.; Rychkov, G.; Sandgren, M.; Stålbrand, H.; Sinnott, M.; Kulminskaya, A.; and Shabalin, K.\n\n\n \n\n\n\n Carbohydrate Research, 412: 43-49. 2015.\n cited By 2\n\n\n\n
\n\n\n\n \n \n $\"The$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Borisova201543,\r\nauthor={Borisova, A.S. and Reddy, S.K. and Ivanen, D.R. and Bobrov, K.S. and Eneyskaya, E.V. and Rychkov, G.N. and Sandgren, M. and Stålbrand, H. and Sinnott, M.L. and Kulminskaya, A.A. and Shabalin, K.A.},\r\ntitle={The method of integrated kinetics and its applicability to the exo-glycosidase-catalyzed hydrolyses of p-nitrophenyl glycosides},\r\njournal={Carbohydrate Research},\r\nyear={2015},\r\nvolume={412},\r\npages={43-49},\r\ndoi={10.1016/j.carres.2015.03.021},\r\nnote={cited By 2},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84929649802&doi=10.1016%2fj.carres.2015.03.021&partnerID=40&md5=f216c9f632b9a6d57c20a434a9dbc525},\r\naffiliation={National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Orlova roscha, 188300, Russian Federation; Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, Uppsala, Sweden; Department of Biochemistry and Structural Biology, Lund University, Lund, S-221 00, Sweden; Department of Chemical Sciences, University of Huddersfield, Queensgate, Huddersfield, HD1 3DH, United Kingdom; St. Petersburg State Polytechnical University, 29 Politekhnicheskaya st., St. Petersburg, 195251, Russian Federation},\r\nabstract={In the present work we suggest an efficient method, using the whole time course of the reaction, whereby parameters k<inf>cat</inf>, K<inf>m</inf> and product K<inf>I</inf> for the hydrolysis of a p-nitrophenyl glycoside by an exo-acting glycoside hydrolase can be estimated in a single experiment. Its applicability was demonstrated for three retaining exo-glycoside hydrolases, β-xylosidase from Aspergillus awamori, β-galactosidase from Penicillium sp. and α-galactosidase from Thermotoga maritima (TmGalA). During the analysis of the reaction course catalyzed by the TmGalA enzyme we had observed that a non-enzymatic process, mutarotation of the liberated α-d-galactose, affected the reaction significantly. © 2015 Elsevier Ltd. All rights reserved.},\r\nauthor_keywords={Integrated kinetics;  Mutarotation;  Retaining glycoside hydrolase},\r\nfunding_details={Российский Фонд Фундаментальных Исследований (РФФИ)12-08-00813-a},\r\n}

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\n \n\n \n \n \n \n \n \n The novel strain Fusarium proliferatum LE1 (RCAM02409) produces α-L-fucosidase and arylsulfatase during the growth on fucoidan.\n \n \n \n \n\n\n \n Shvetsova, S.; Zhurishkina, E.; Bobrov, K.; Ronzhina, N.; Lapina, I.; Ivanen, D.; Gagkaeva, T.; and Kulminskaya, A.\n\n\n \n\n\n\n Journal of Basic Microbiology, 55(4): 471-479. 2015.\n cited By 10\n\n\n\n
\n\n\n\n \n \n $\"The$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Shvetsova2015471,\r\nauthor={Shvetsova, S.V. and Zhurishkina, E.V. and Bobrov, K.S. and Ronzhina, N.L. and Lapina, I.M. and Ivanen, D.R. and Gagkaeva, T.Y. and Kulminskaya, A.A.},\r\ntitle={The novel strain Fusarium proliferatum LE1 (RCAM02409) produces α-L-fucosidase and arylsulfatase during the growth on fucoidan},\r\njournal={Journal of Basic Microbiology},\r\nyear={2015},\r\nvolume={55},\r\nnumber={4},\r\npages={471-479},\r\ndoi={10.1002/jobm.201400309},\r\nnote={cited By 10},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84964296282&doi=10.1002%2fjobm.201400309&partnerID=40&md5=5abfbe90837307b502556b4393fc9c2e},\r\naffiliation={National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Russian Federation; St. Petersburg State Polytechnical University, St. Petersburg, Russian Federation; All-Russian Institute of Plant Protection, Russian Academy of Agricultural Sciences, St. Petersburg, Pushkin, Russian Federation},\r\nabstract={Enzymes capable of modifying the sulfated polymeric molecule of fucoidan are mainly produced by different groups of marine organisms: invertebrates, bacteria, and also some fungi. We have discovered and identified a new strain of filamentous fungus Fusarium proliferatum LE1 (deposition number in Russian Collection of Agricultural Microorganisms is RCAM02409), which is a potential producer of fucoidan-degrading enzymes. The strain LE1 (RCAM02409) was identified on the basis of morphological characteristics and analysis of ITS sequences of ribosomal DNA. During submerged cultivation of F. proliferatum LE1 in the nutrient medium containing natural fucoidan sources (the mixture of brown algae Laminaria digitata and Fucus vesiculosus), enzymic activities of α-L-fucosidase and arylsulfatase were inducible. These enzymes hydrolyzed model substrates, para-nitrophenyl α-L-fucopyranoside and para-nitrophenyl sulfate, respectively. However, the α-L-fucosidase is appeared to be a secreted enzyme while the arylsulfatase was an intracellular one. No detectable fucoidanase activity was found during F. proliferatum LE1 growth in submerged culture or in a static one. Comparative screening for fucoidanase/arylsulfatase/α-L-fucosidase activities among several related Fusarium strains showed a uniqueness of F. proliferatum LE1 to produce arylsulfatase and α-L-fucosidase enzymes. Apart them, the strain was shown to produce other glycoside hydrolyses. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.},\r\nauthor_keywords={Arylsulfatase;  Fucoidan;  Fusarium proliferatum;  α-L-Fucosidase},\r\ncorrespondence_address1={Kulminskaya, A.A.; Laboratory of Enzymology, Petersburg Nuclear Physics InstituteRussian Federation; email: kulm@omrb.pnpi.spb.ru},\r\npublisher={Wiley-VCH Verlag},\r\nissn={0233111X},\r\ncoden={JBMIE},\r\npubmed_id={25346501},\r\nlanguage={English},\r\nabbrev_source_title={J. Basic Microbiol.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n α-Galactobiosyl units: Thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima.\n \n \n \n \n\n\n \n Borisova, A.; Ivanen, D.; Bobrov, K.; Eneyskaya, E.; Rychkov, G.; Sandgren, M.; Kulminskaya, A.; Sinnott, M.; and Shabalin, K.\n\n\n \n\n\n\n Carbohydrate Research, 401: 115-121. 2015.\n cited By 5\n\n\n\n
\n\n\n\n \n \n $\"α-Galactobiosyl$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Borisova2015115,\r\nauthor={Borisova, A.S. and Ivanen, D.R. and Bobrov, K.S. and Eneyskaya, E.V. and Rychkov, G.N. and Sandgren, M. and Kulminskaya, A.A. and Sinnott, M.L. and Shabalin, K.A.},\r\ntitle={α-Galactobiosyl units: Thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima},\r\njournal={Carbohydrate Research},\r\nyear={2015},\r\nvolume={401},\r\npages={115-121},\r\ndoi={10.1016/j.carres.2014.11.003},\r\nnote={cited By 5},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84918807980&doi=10.1016%2fj.carres.2014.11.003&partnerID=40&md5=a72be071ed1f9fe275f7d4cc1bf43ce0},\r\naffiliation={National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina, 188300, Russian Federation; Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, Uppsala, Sweden; St. Petersburg State Polytechnical University, 29 Politechnicheskaya str., St. Petersburg, 195251, Russian Federation; Department of Chemical Sciences, University of Huddersfield, Queensgate, Huddersfield, HD1 3DH, United Kingdom},\r\nabstract={Broad regioselectivity of α-galactosidase from Thermotoga maritima (TmGal36A) is a limiting factor for application of the enzyme in the directed synthesis of oligogalactosides. However, this property can be used as a convenient tool in studies of thermodynamics of a glycosidic bond. Here, a novel approach to energy difference estimation is suggested. Both transglycosylation and hydrolysis of three types of galactosidic linkages were investigated using total kinetics of formation and hydrolysis of pNP-galactobiosides catalysed by monomeric glycoside hydrolase family 36 α-galactosidase from T. maritima, a retaining exo-acting glycoside hydrolase. We have estimated transition state free energy differences between the 1,2- and 1,3-linkage (ΔΔG‡0 values were equal 5.34 ± 0.85 kJ/mol) and between 1,6-linkage and 1,3-linkage (ΔΔG‡0 = 1.46 ± 0.23 kJ/mol) in pNP-galactobiosides over the course of the reaction catalysed by TmGal36A. Using the free energy difference for formation and hydrolysis of glycosidic linkages (ΔΔG‡F - ΔΔG‡H), we found that the 1,2-linkage was 2.93 ± 0.47 kJ/mol higher in free energy than the 1,3-linkage, and the 1,6-linkage 4.44 ± 0.71 kJ/mol lower. © 2014 Elsevier Ltd. All rights reserved.},\r\nfunding_details={Российский Фонд Фундаментальных Исследований (РФФИ)12-08-00813-a},\r\n}

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\n \n\n \n \n \n \n \n \n Xylan degradation improved by a combination of monolithic columns bearing immobilized recombinant β-xylosidase from Aspergillus awamori X-100 and Grindamyl H121 β-xylanase.\n \n \n \n \n\n\n \n Volokitina, M.; Bobrov, K.; Piens, K.; Eneyskaya, E.; Tennikova, T.; Vlakh, E.; and Kulminskaya, A.\n\n\n \n\n\n\n Biotechnology Journal, 10(1): 210-221. 2015.\n cited By 4\n\n\n\n
\n\n\n\n \n \n $\"Xylan$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Volokitina2015210,\r\nauthor={Volokitina, M.V. and Bobrov, K.S. and Piens, K. and Eneyskaya, E.V. and Tennikova, T.B. and Vlakh, E.G. and Kulminskaya, A.A.},\r\ntitle={Xylan degradation improved by a combination of monolithic columns bearing immobilized recombinant β-xylosidase from Aspergillus awamori X-100 and Grindamyl H121 β-xylanase},\r\njournal={Biotechnology Journal},\r\nyear={2015},\r\nvolume={10},\r\nnumber={1},\r\npages={210-221},\r\ndoi={10.1002/biot.201400417},\r\nnote={cited By 4},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84921527685&doi=10.1002%2fbiot.201400417&partnerID=40&md5=1d1119ed1e45a14decf086be0a4ec5d9},\r\naffiliation={Russian Academy of Sciences, Institute of Macromolecular Compounds, St. Petersburg, Russian Federation; National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Orlova roscha, Russian Federation; Ghent University, Department of Biochemistry and Microbiology, Ghent, Belgium; Saint-Petersburg State University, Institute of Chemistry, St. Petersburg, Russian Federation; St.Petersburg State Polytechnical University, St. Petersburg, Russian Federation},\r\nabstract={Synergistic action of exo- and endohydrolazes is preferred for effective destruction of biopolymers. The main purpose of the present work was to develop an efficient tool for degradation of xylan. Macroporous lab-made monolithic columns and commercial CIM-Epoxy disk were used to immobilize the recombinant β-xylosidase from Aspergillus awamori and Grindamyl β-xylanase. The efficiency of xylan degradation using the low-loaded β-xylosidase column appeared to be four times higher than for the in-solution process and about six times higher than for the high-loaded bioreactor. Disk bioreactor with the Grindamil β-xylanase operated in a recirculation mode has shown noticeable advantages over the column design. Additionally, a system comprised of two immobilized enzyme reactors (IMERs) was tested to accelerate the biopolymer hydrolysis, yielding total xylan conversion into xylose within 20 min. Fast online monitoring HPLC procedure was developed where an analytical DEAE CIM disk was added to the two-enzyme system in a conjoint mode. A loss of activity of immobilized enzymes did not exceed 7% after 5 months of the bioreactor usage. We can therefore conclude that the bioreactors developed exhibit high efficiency and remarkable long-term stability. Macroporous lab-made monolithic columns and a commercial disk are used to immobilize the recombinant β-xylosidase from Aspergillus awamori and Grindamyl β-xylanase for the efficient degradation of xylan. A system comprising two immobilized enzyme reactors is tested to accelerate the xylan hydrolysis, yielding its fast total conversion into xylose. Both bioreactors exhibit high efficiency and remarkable long-term stability. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.},\r\nauthor_keywords={Immobilized enzyme reactors;  Macroporous monoliths;  Xylan degradation;  Xylanase;  β-xylosidase},\r\ncorrespondence_address1={Kulminskaya, A.A.; National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics InstituteRussian Federation},\r\npublisher={Wiley-VCH Verlag},\r\nissn={18606768},\r\npubmed_id={25367775},\r\nlanguage={English},\r\nabbrev_source_title={Biotechnol. J.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Enzymatic degradation of Xylan for production of xylooligosaccharides and xylose.\n \n \n \n \n\n\n \n Volokitina, M.; Bobrov, K.; Kulminskaya, A.; Tennikova, T.; and Vlakh, E.\n\n\n \n\n\n\n Proceedings of the Estonian Academy of Sciences, 64(2014): 106. 2015.\n cited By 0; Conference of 14th Baltic Polymer Symposium 2014, BPS 2014 ; Conference Date: 24 September 2014 Through 26 September 2014; Conference Code:113706\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Volokitina2015106,\r\nauthor={Volokitina, M. and Bobrov, K. and Kulminskaya, A. and Tennikova, T. and Vlakh, E.},\r\ntitle={Enzymatic degradation of Xylan for production of xylooligosaccharides and xylose},\r\njournal={Proceedings of the Estonian Academy of Sciences},\r\nyear={2015},\r\nvolume={64},\r\nnumber={2014},\r\npages={106},\r\nnote={cited By 0; Conference of 14th Baltic Polymer Symposium 2014, BPS 2014 ; Conference Date: 24 September 2014 Through 26 September 2014;  Conference Code:113706},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84988979474&partnerID=40&md5=59749aaf4ff7a1b461df0bb2661d05b3},\r\naffiliation={Faculty of Chemical and Biochemical Technology, Saint-Petersburg State Institute of Technology (Technical Univercity), Moskovsky pr. 26, St. Petersburg, 190013, Russian Federation; Institute of Macromolecular Compounds, Russian Academy of Sciences, Bolshoy pr. 31, St. Petersburg, 199004, Russian Federation; Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Molecular and Radiation Biology Division, Gatchina, 188300, Russian Federation; Institute of Chemistry, Saint-Petersburg State University, Universitetskiy pr. 26, St. Petersburg, Russian Federation},\r\ncorrespondence_address1={Volokitina, M.; Faculty of Chemical and Biochemical Technology, Saint-Petersburg State Institute of Technology (Technical Univercity), Moskovsky pr. 26, Russian Federation},\r\nsponsors={},\r\npublisher={Estonian Academy Publishers},\r\nissn={17366046},\r\nlanguage={English},\r\nabbrev_source_title={Proc. Est. Acad. Sci.},\r\ndocument_type={Conference Paper},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n EFFECT OF FUCOIDANS ISOLATED FROM SEAWEEDS LAMINARIA DIGITATA AND FUCUS VESICULOSUS ON CELL LINES HELA G-63, ECV 304 AND PC 12.\n \n \n \n \n\n\n \n Zhurishkina, E.; Lapina, I.; Ivanen, D.; Stepanov, S.; Shvetsova, S.; Shavarda, A.; Giliano, N.; and Kulminskaya, A.\n\n\n \n\n\n\n Tsitologiia, 57(10): 727-735. 2015.\n cited By 1\n\n\n\n
\n\n\n\n \n \n $\"EFFECT$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Zhurishkina2015727,\r\nauthor={Zhurishkina, E.V. and Lapina, I.M. and Ivanen, D.R. and Stepanov, S.I. and Shvetsova, S.V. and Shavarda, A.L. and Giliano, N.Y. and Kulminskaya, A.A.},\r\ntitle={EFFECT OF FUCOIDANS ISOLATED FROM SEAWEEDS LAMINARIA DIGITATA AND FUCUS VESICULOSUS ON CELL LINES HELA G-63, ECV 304 AND PC 12},\r\njournal={Tsitologiia},\r\nyear={2015},\r\nvolume={57},\r\nnumber={10},\r\npages={727-735},\r\nnote={cited By 1},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84964695769&partnerID=40&md5=dc7d1a17857cb900156646bd14df7310},\r\nabstract={The aim of the research was to investigate cytotoxicity of fucoidans on mammals cells. Three different samples of fucoidans were isolated from mechanically grounded brown algae Laminaria digitata and Fucus ve- siculosus. The sample F2 that differed from the others by higher sulfatation level and suppression of HeLa G-63 line culture growth was taken for further study in cell lines HeLa G-63, ECV 304 and PC 12. We have shown that fucoidan preparation F2 inhibits proliferation and induces cell death in a dose- and time-dependent manner for all investigated cell lines. Neuroendocrine tumor rat cell line PC 12 appeared to be the most sensitive to fucoidan treatment whereas endothelial human cells ECV 304 were the least sensitive.},\r\nissn={00413771},\r\npubmed_id={26863772},\r\nlanguage={Russian},\r\nabbrev_source_title={Tsitologiia},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n\n\n\n\n\n

\n

\n \n 2014\n \n \n (2)\n \n \n

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\n \n \n

\n \n\n \n \n \n \n \n \n Impact of an N-terminal extension on the stability and activity of the GH11 xylanase from Thermobacillus xylanilyticus.\n \n \n \n \n\n\n \n Song, L.; Dumon, C.; Siguier, B.; André, I.; Eneyskaya, E.; Kulminskaya, A.; Bozonnet, S.; and O'Donohue, M.\n\n\n \n\n\n\n Journal of Biotechnology, 174(1): 64-72. 2014.\n cited By 8\n\n\n\n
\n\n\n\n \n \n $\"Impact$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Song201464,\r\nauthor={Song, L. and Dumon, C. and Siguier, B. and André, I. and Eneyskaya, E. and Kulminskaya, A. and Bozonnet, S. and O'Donohue, M.J.},\r\ntitle={Impact of an N-terminal extension on the stability and activity of the GH11 xylanase from Thermobacillus xylanilyticus},\r\njournal={Journal of Biotechnology},\r\nyear={2014},\r\nvolume={174},\r\nnumber={1},\r\npages={64-72},\r\ndoi={10.1016/j.jbiotec.2014.01.004},\r\nnote={cited By 8},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84894326081&doi=10.1016%2fj.jbiotec.2014.01.004&partnerID=40&md5=32145c13217f258f78972382f1ea9cdc},\r\naffiliation={Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France; CNRS, UMR5504, F-31400 Toulouse, France; CNRS, Institut de Pharmacologie et de Biologie Structurale, F-31077 Toulouse, France; National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, 188350 St. Petersburg, Russian Federation; Institut National de la Recherche Scientifique, INRS-InstitutArmand-Frappier, Laval, QC, H7V 1B7, Canada},\r\nabstract={To understand structure-function relationships in the N-terminal region of GH11 xylanases, the 17 N-terminal amino acids of the GH11 xylanase from Neocallimastix patriciarum (Np-Xyn) have been grafted onto the N-terminal extremity of the untypically short GH11 xylanase from Thermobacillus xylanilyticus (Tx-Xyn), creating a hybrid enzyme denoted NTfus. The hybrid xylanase displayed properties (pH and temperature optima) similar to those of the parental enzyme, although thermostability was lowered, with the Tm value, being reduced by 5°C. Kinetic assays using oNP-Xylo-oligosaccharides (DP2 and 3) indicated that the N-extension did not procure more extensive substrate binding, even when further mutagenesis was performed to promote this. However, these experiments confirmed weak subsite -3 for both NTfus and the parental enzyme. The catalytic efficiency of NTfus was shown to be 17% higher than that of the parental enzyme on low viscosity wheat arabinoxylan and trials using milled wheat straw as the substrate revealed that NTfus released more substituted oligosaccharide products (Xyl/Ara=8.97±0.13 compared to Xyl/Ara=9.70±0.21 for the parental enzyme), suggesting that the hybrid enzyme possesses wider substrate selectivity. Combining either the parental enzyme or NTfus with the cellulolytic cocktail Accellerase 1500 boosted the impact of the latter on wheat straw, procuring yields of solubilized xylose and glucose of 23 and 24% of theoretical yield, respectively, thus underlining the benefits of added xylanase activity when using this cellulase cocktail. Overall, in view of the results obtained for NTfus, we propose that the N-terminal extension leads to the modification of a putative secondary substrate binding site, a hypothesis that is highly consistent with previous data. © 2014 Elsevier B.V.},\r\nauthor_keywords={-3 subsite mapping;  GH11 xylanase;  Hybrid enzyme;  N-terminal region;  Secondary binding site},\r\nfunding_details={PICT},\r\n}

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\n \n\n \n \n \n \n \n \n Draft genome sequence of Geotrichum candidum strain 3C.\n \n \n \n \n\n\n \n Polev, D.; Bobrov, K.; Eneyskaya, E.; and Kulminskaya, A.\n\n\n \n\n\n\n Genome Announcements, 2(5). 2014.\n cited By 8\n\n\n\n
\n\n\n\n \n \n $\"Draft$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Polev2014,\r\nauthor={Polev, D.E. and Bobrov, K.S. and Eneyskaya, E.V. and Kulminskaya, A.A.},\r\ntitle={Draft genome sequence of Geotrichum candidum strain 3C},\r\njournal={Genome Announcements},\r\nyear={2014},\r\nvolume={2},\r\nnumber={5},\r\ndoi={10.1128/genomeA.00956-14},\r\nart_number={e00956-14},\r\nnote={cited By 8},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-85004168771&doi=10.1128%2fgenomeA.00956-14&partnerID=40&md5=67ae8307bc8e28faf9683dec80f2a97f},\r\naffiliation={Research Resource Center for Molecular and Cell Technologies, St. Petersburg State University, St. Petersburg, Russian Federation; National Research Centre, Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Orlova Roscha, Russian Federation; St. Petersburg State Polytechnical University, St. Petersburg, Russian Federation},\r\nabstract={We report here the draft genome sequence of Geotrichum candidum strain 3C, which is a filamentous yeast-like fungus that holds great promise for biotechnology. The genome was sequenced using Ion Torrent and 454 platforms. The estimated genome size was 41.4 Mb, and 14,579 protein-coding genes were predicted ab initio. © 2014 Polev et al.},\r\ncorrespondence_address1={Polev, D.E.; Research Resource Center for Molecular and Cell Technologies, St. Petersburg State UniversityRussian Federation; email: dmitry.polev@gmail.com},\r\npublisher={American Society for Microbiology},\r\nissn={21698287},\r\nlanguage={English},\r\nabbrev_source_title={Genome Announce.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2013\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n Improvement of the efficiency of transglycosylation catalyzed by α-galactosidase from Thermotoga maritima by protein engineering.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Biochemistry (Moscow), 78(10): 1112-1123. 2013.\n cited By 10\n\n\n\n
\n\n\n\n \n \n $\"Improvement$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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\n \n 2010\n \n \n (2)\n \n \n

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\n \n\n \n \n \n \n \n \n Mutagenesis and subsite mapping underpin the importance for substrate specificity of the aglycon subsites of glycoside hydrolase family 11 xylanases.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Biochimica et Biophysica Acta - Proteins and Proteomics, 1804(4): 977-985. 2010.\n cited By 26\n\n\n\n
\n\n\n\n \n \n $\"Mutagenesis$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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\n \n\n \n \n \n \n \n \n Catalytic mechanism of human α-galactosidase.\n \n \n \n \n\n\n \n Guce, A.; Clark, N.; Salgado, E.; Ivanen, D.; Kulminskaya, A.; Brumer III, H.; and Garman, S.\n\n\n \n\n\n\n Journal of Biological Chemistry, 285(6): 3625-3632. 2010.\n cited By 67\n\n\n\n
\n\n\n\n \n \n $\"Catalytic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Guce20103625,\r\nauthor={Guce, A.I. and Clark, N.E. and Salgado, E.N. and Ivanen, D.R. and Kulminskaya, A.A. and Brumer III, H. and Garman, S.C.},\r\ntitle={Catalytic mechanism of human α-galactosidase},\r\njournal={Journal of Biological Chemistry},\r\nyear={2010},\r\nvolume={285},\r\nnumber={6},\r\npages={3625-3632},\r\ndoi={10.1074/jbc.M109.060145},\r\nnote={cited By 67},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-77950511400&doi=10.1074%2fjbc.M109.060145&partnerID=40&md5=d7be48e5b0e0006198e363b1127b3879},\r\naffiliation={Dept. of Biochemistry and Molecular Biology, University of Massachusetts, 710 North Pleasant St., Amherst, MA, United States; Department of Chemistry, University of Massachusetts, Amherst, MA 01003, United States; Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Russian Academy of Science, Leningrad District, Orlova Roscha, Gatchina 188300, Russian Federation; Department of Biotechnology, Royal Insitute of Technology (KTH), 10691 Stockholm, Sweden},\r\nabstract={The enzyme α-galactosidase (α-GAL, also known as α-GAL A; E.C. 3.2.1.22) is responsible for the breakdown of α-galactosides in the lysosome. Defects in human α-GAL lead to the development of Fabry disease, a lysosomal storage disorder characterized by the buildup of α-galactosylated substrates in the tissues. α-GAL is an active target of clinical research: there are currently two treatment options for Fabry disease, recombinant enzyme replacement therapy (approved in the United States in 2003) and pharmacological chaperone therapy (currently in clinical trials). Previously, we have reported the structure of human α-GAL, which revealed the overall structure of the enzyme and established the locations of hundreds of mutations that lead to the development of Fabry disease. Here, we describe the catalytic mechanism of the enzyme derived from x-ray crystal structures of each of the four stages of the double displacement reaction mechanism. Use of a difluoro-α-galactopyranoside allowed trapping of a covalent intermediate. The ensemble of structures reveals distortion of the ligand into a 1S3 skew (or twist) boat conformation in the middle of the reaction cycle. The high resolution structures of each step in the catalytic cycle will allow for improved drug design efforts on α-GAL and other glycoside hydrolase family 27 enzymes by developing ligands that specifically target different states of the catalytic cycle. Additionally, the structures revealed a second ligand-binding site suitable for targeting by novel pharmacological chaperones. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.},\r\ncorrespondence_address1={Garman, S. C.; Dept. of Biochemistry and Molecular Biology, University of Massachusetts, 710 North Pleasant St., Amherst, MA, United States; email: garman@biochem.umass.edu},\r\nissn={00219258},\r\ncoden={JBCHA},\r\npubmed_id={19940122},\r\nlanguage={English},\r\nabbrev_source_title={J. Biol. Chem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2009\n \n \n (2)\n \n \n

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\n \n\n \n \n \n \n \n \n Transglycosylating and hydrolytic activities of the β-mannosidase from Trichoderma reesei.\n \n \n \n \n\n\n \n Eneyskaya, E.; Sundqvist, G.; Golubev, A.; Ibatullin, F.; Ivanen, D.; Shabalin, K.; Brumer, H.; and Kulminskaya, A.\n\n\n \n\n\n\n Biochimie, 91(5): 632-638. 2009.\n cited By 18\n\n\n\n
\n\n\n\n \n \n $\"Transglycosylating$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Eneyskaya2009632,\r\nauthor={Eneyskaya, E.V. and Sundqvist, G. and Golubev, A.M. and Ibatullin, F.M. and Ivanen, D.R. and Shabalin, K.A. and Brumer, H. and Kulminskaya, A.A.},\r\ntitle={Transglycosylating and hydrolytic activities of the β-mannosidase from Trichoderma reesei},\r\njournal={Biochimie},\r\nyear={2009},\r\nvolume={91},\r\nnumber={5},\r\npages={632-638},\r\ndoi={10.1016/j.biochi.2009.03.009},\r\nnote={cited By 18},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-64049097092&doi=10.1016%2fj.biochi.2009.03.009&partnerID=40&md5=2eb0f1a7d4883969c402b5c2be2284dd},\r\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biophysics Division, Orlova Roscha, Gatchina, 188300 Leningrad District, Russian Federation; School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre, 106 91 Stockholm, Sweden},\r\nabstract={A purified β-mannosidase (EC 3.2.1.25) from the fungus Trichoderma reesei has been identified as a member of glycoside hydrolase family 2 through mass spectrometry analysis of tryptic peptides. In addition to hydrolysis, the enzyme catalyzes substrate transglycosylation with p-nitrophenyl β-mannopyranoside. Structures of the major and minor products of this reaction were identified by NMR analysis as p-nitrophenyl mannobiosides and p-nitrophenyl mannotriosides containing β-(1 → 4) and β-(1 → 3) linkages. The rate of donor substrate hydrolysis increased in presence of acetonitrile and dimethylformamide, while transglycosylation was weakly suppressed by these organic solvents. Differential ultraviolet spectra of the protein indicate that a rearrangement of the hydrophobic environment of the active site following the addition of the organic solvents may be responsible for this hydrolytic activation. © 2009 Elsevier Masson SAS. All rights reserved.},\r\nauthor_keywords={β-Mannosidase;  Organic solvents;  p-Nitrophenyl β-mannooligosaccharides;  Transglycosylation},\r\nfunding_details={Российский Фонд Фундаментальных Исследований (РФФИ)07-04-01071-a},\r\n}

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\n \n\n \n \n \n \n \n \n Novel precipitated fluorescent substrates for the screening of cellulolytic microorganisms.\n \n \n \n \n\n\n \n Ivanen, D.; Rongjina, N.; Shishlyannikov, S.; Litviakova, G.; Isaeva-Ivanova, L.; Shabalin, K.; and Kulminskaya, A.\n\n\n \n\n\n\n Journal of Microbiological Methods, 76(3): 295-300. 2009.\n cited By 13\n\n\n\n
\n\n\n\n \n \n $\"Novel$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Ivanen2009295,\r\nauthor={Ivanen, D.R. and Rongjina, N.L. and Shishlyannikov, S.M. and Litviakova, G.I. and Isaeva-Ivanova, L.S. and Shabalin, K.A. and Kulminskaya, A.A.},\r\ntitle={Novel precipitated fluorescent substrates for the screening of cellulolytic microorganisms},\r\njournal={Journal of Microbiological Methods},\r\nyear={2009},\r\nvolume={76},\r\nnumber={3},\r\npages={295-300},\r\ndoi={10.1016/j.mimet.2008.12.008},\r\nnote={cited By 13},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-59849118700&doi=10.1016%2fj.mimet.2008.12.008&partnerID=40&md5=96f7e79d16abff046af9b50afee31c1a},\r\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biophysics Division, 188300, Orlova roscha 1, Gatchina, Leningrad District, Russian Federation},\r\nabstract={New substrates, 2-(2′-benzothiazolyl)-phenyl (BTP) cellooligosaccharides with degree of polymerization (d.p.) 2-4 (BTPG2-4) were synthesized for the screening of microbial cellulolytic activity in plate assays. The substrates were very efficient that was shown for several cellulolytic bacteria, including yeast-like isolates from Kamchatka hot springs. Three tested bacterial strains and eighteen of 30 of the yeast isolates showed ability to degrade cellulose with cellobiohydrolase, β-glucosidase and endo-cellulase activities measured with standard substrates. The structures of 2-(2′-benzothiazolyl)-phenyl oligosaccharides were solved by NMR- and mass-spectrometry. The usefulness of the 2-(2′-benzothiazolyl)-phenyl substrates were also shown during purification of the B. polymyxa cellulolytic complex, which consists of at least three types of the enzymes: cellobiohydrolase, endo-β-d-glucanase and β-glucosidase. © 2008 Elsevier B.V. All rights reserved.},\r\nauthor_keywords={2-(2′-Benzothiazolyl)-phenyl cellooligosaccharides;  Cellulases;  Fluorescent precipitated substrates},\r\nfunding_details={Российский Фонд Фундаментальных Исследований (РФФИ)05-04-50825-MF_a},\r\n}

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\n \n 2008\n \n \n (3)\n \n \n

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\n \n\n \n \n \n \n \n \n Enzymatic hydrolysis of 1,3-1,4-β-glucosyl oligosaccharides by 1,3-1,4-β-glucanase from Synechocystis PCC6803: A comparison with assays using polymer and chromophoric oligosaccharide substrates.\n \n \n \n \n\n\n \n Fukamizo, T.; Hayashi, K.; Tamoi, M.; Fujimura, Y.; Kurotaki, H.; Kulminskaya, A.; and Kitaoka, M.\n\n\n \n\n\n\n Archives of Biochemistry and Biophysics, 478(2): 187-194. 2008.\n cited By 8\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Fukamizo2008187,\r\nauthor={Fukamizo, T. and Hayashi, K. and Tamoi, M. and Fujimura, Y. and Kurotaki, H. and Kulminskaya, A. and Kitaoka, M.},\r\ntitle={Enzymatic hydrolysis of 1,3-1,4-β-glucosyl oligosaccharides by 1,3-1,4-β-glucanase from Synechocystis PCC6803: A comparison with assays using polymer and chromophoric oligosaccharide substrates},\r\njournal={Archives of Biochemistry and Biophysics},\r\nyear={2008},\r\nvolume={478},\r\nnumber={2},\r\npages={187-194},\r\ndoi={10.1016/j.abb.2008.07.019},\r\nnote={cited By 8},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-52249117218&doi=10.1016%2fj.abb.2008.07.019&partnerID=40&md5=55602366a3c9a982965d25b953ec29bc},\r\naffiliation={Department of Advanced Bioscience, Kinki University, 3327-204 Nakamachi, Nara, 631-8505, Japan; Laboratory of Enzymology, Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Orlova roscha, 188300, Gatchina, Len. District, Russian Federation; National Food Research Institute, 2-1-2 Kannondai, Tsukuba, Ibaraki, 305-8642, Japan},\r\nabstract={The specificity of 1,3-1,4-β-glucanase from Synechocystis PCC6803 (SsGlc) was investigated using novel substrates 1,3-1,4-β-glucosyl oligosaccharides, in which 1,3- and 1,4-linkages are located in various arrangements. After the enzymatic reaction, the reaction products were separated and determined by high-performance anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD). As a result, SsGlc was found to hydrolyze the pentasaccharides, which possess three contiguous 1,4-β-glycosidic linkages (cellotetraose sequence) adjacent to 1,3-β-linkage, but none of the other oligosaccharides were hydrolyzed. To further analyze the specificity, kinetic measurements were performed using polymeric substrates and 4-methylumbelliferyl derivatives of laminaribiose and cellobiose (1,3-β-(Glc)2-MU and 1,4-β-(Glc)2-MU). The kcat/Km value obtained for barley β-glucan was considerably larger than that for lichenan, indicating that SsGlc prefers 1,3-1,4-β-glucan possessing a larger amount of cellotetraose sequence. This is consistent with the data obtained for 1,3-1,4-β-glucosyl oligosaccharides. However, the kcat/Km value obtained for 1,4-β-(Glc)2-MU was considerably lower than that for 1,3-β-(Glc)2-MU, suggesting inconsistency with the data obtained from the other natural substrates. It is likely that the kinetic data obtained from such chromophoric substrates do not always reflect the true enzymatic properties. © 2008 Elsevier Inc. All rights reserved.},\r\nauthor_keywords={1,3-1,4-β-glucanase;  Cleavage specificity;  Cyanobacterium;  Glucosyl oligosaccharides;  HPAEC-PAD},\r\n}

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\n \n\n \n \n \n \n \n \n Crystallization and preliminary crystallographic analysis of laminarinase from Rhodothermus marinus: A case of pseudomerohedral twinning.\n \n \n \n \n\n\n \n Golubev, A.; Rojas, A.; Nascimento, A.; Bleicher, L.; Kulminskaya, A.; Eneyskaya, E.; and Polikarpov, I.\n\n\n \n\n\n\n Protein and Peptide Letters, 15(10): 1142-1144. 2008.\n cited By 1\n\n\n\n
\n\n\n\n \n \n $\"Crystallization$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Golubev20081142,\r\nauthor={Golubev, A.M. and Rojas, A.L. and Nascimento, A.S. and Bleicher, L. and Kulminskaya, A.A. and Eneyskaya, E.V. and Polikarpov, I.},\r\ntitle={Crystallization and preliminary crystallographic analysis of laminarinase from Rhodothermus marinus: A case of pseudomerohedral twinning},\r\njournal={Protein and Peptide Letters},\r\nyear={2008},\r\nvolume={15},\r\nnumber={10},\r\npages={1142-1144},\r\ndoi={10.2174/092986608786071139},\r\nnote={cited By 1},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-54249097528&doi=10.2174%2f092986608786071139&partnerID=40&md5=ed7b68584148c82d770a92eb81124ed8},\r\naffiliation={Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, 188300, Russian Federation; Instituto de Física de São Carlos, Universidade de São Paulo, Av Trabalhador Saocarlense 400, CEP 13560-970, São Carlos, SP, Brazil; National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, United States},\r\nabstract={Thermophilic endo-1,3(4)-β-glucanase (laminarinase) from Rhodothermus marinus was crystallized by the hanging-drop vapor diffusion method. The needle-like crystals belong to space group P21 and contain two protein molecules in the asymmetric unit with a solvent content of 51.75 %. Diffraction data were collected to a resolution of 1.95Å and resulted in a dataset with an overall Rmerge of 10.4% and a completeness of 97.8%. Analysis of the structure factors revealed pseudomerohedral twinning of the crystals with a twin fraction of approximately 42%. © 2008 Bentham Science Publishers Ltd.},\r\nauthor_keywords={Crystallization;  Laminarinase;  Pseudomerohedral twinning;  Rhodothermus marinus},\r\ncorrespondence_address1={Polikarpov, I.; Instituto de Física de São Carlos, Universidade de São Paulo, Av Trabalhador Saocarlense 400, CEP 13560-970, São Carlos, SP, Brazil; email: ipolikarpov@if.sc.usp.br},\r\nissn={09298665},\r\ncoden={PPELE},\r\npubmed_id={19075828},\r\nlanguage={English},\r\nabbrev_source_title={Protein Pept. Lett.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Electron transfer processes between sputtered O atoms and Ag(110):O(n × 1) reconstructed surfaces.\n \n \n \n \n\n\n \n Guillemot, L.; Bandurin, Y.; Bobrov, K.; and Esaulov, V.\n\n\n \n\n\n\n Journal of Physics Condensed Matter, 20(35). 2008.\n cited By 3\n\n\n\n
\n\n\n\n \n \n $\"Electron$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Guillemot2008,\r\nauthor={Guillemot, L. and Bandurin, Y. and Bobrov, K. and Esaulov, V.A.},\r\ntitle={Electron transfer processes between sputtered O atoms and Ag(110):O(n × 1) reconstructed surfaces},\r\njournal={Journal of Physics Condensed Matter},\r\nyear={2008},\r\nvolume={20},\r\nnumber={35},\r\ndoi={10.1088/0953-8984/20/35/355008},\r\nart_number={355008},\r\nnote={cited By 3},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-56349133176&doi=10.1088%2f0953-8984%2f20%2f35%2f355008&partnerID=40&md5=6be3ee35740b286430c22acdb496e66c},\r\naffiliation={CNRS, UMR 8625, UPS-11, F-91405 Orsay, France; LCAM, Université Paris-Sud, F-91405 Orsay, France; Uzhgorod Centre, Kiev National Trade-Economic University, Korytnjanska, 4, 88020 Uzhgorod, Ukraine},\r\nabstract={We present results of a study of sputtered oxygen atom outgoing trajectory dependence of the electron transfers with oxidized Ag(110) surfaces reconstructed in different (n × 1) added row structures. With a charge state resolved time-of-flight-direct recoil spectroscopy investigation using 4 keV Ar+ incident ions, we determine relative yields of sputtered O and Ag atoms as well as the fraction of sputtered O- ions, for different incident polar and azimuthal angles. The relative yields of sputtered O atoms are satisfactorily reproduced by a classical dynamics simulation. No sputtered Ag- ions were detected. A qualitative discussion of the features of the oxygen negative ion fractions suggests that its description needs, in general, to take into account both capture and loss of electrons as the oxygen atom leaves the surface. The experimental data also suggest that one needs to correctly describe the corrugation of the surface and that the electron loss rates should be site-specific. © 2008 IOP Publishing Ltd.},\r\ncorrespondence_address1={Guillemot, L.; CNRS, UMR 8625, UPS-11, F-91405 Orsay, France; email: laurent.guillemot@u-psud.fr},\r\nissn={09538984},\r\ncoden={JCOME},\r\nlanguage={English},\r\nabbrev_source_title={J Phys Condens Matter},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2007\n \n \n (5)\n \n \n

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\n \n\n \n \n \n \n \n \n Nanostructure formation by reactions of H2O with pre-adsorbed O on a Ag(1 1 0) surface.\n \n \n \n \n\n\n \n Bobrov, K.; and Guillemot, L.\n\n\n \n\n\n\n Surface Science, 601(15): 3268-3275. 2007.\n cited By 11\n\n\n\n
\n\n\n\n \n \n $\"Nanostructure$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Bobrov20073268,\r\nauthor={Bobrov, K. and Guillemot, L.},\r\ntitle={Nanostructure formation by reactions of H2O with pre-adsorbed O on a Ag(1 1 0) surface},\r\njournal={Surface Science},\r\nyear={2007},\r\nvolume={601},\r\nnumber={15},\r\npages={3268-3275},\r\ndoi={10.1016/j.susc.2007.06.002},\r\nnote={cited By 11},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-34447503742&doi=10.1016%2fj.susc.2007.06.002&partnerID=40&md5=638a6992048944cf37693db73cd1e14c},\r\naffiliation={Laboratoire des Collisions Atomiques et Moléculaires, Unité Mixte de Recherche CNRS-Université Paris-Sud No. 8625, Fédération Lumière-Matière, Bât. 351, Orsay, France},\r\nabstract={We present results of an STM investigation of water interaction with an oxygen covered Ag(1 1 0) in the case of the O(4 × 1) reconstructed surface. Regarding the formation of one-layer-thick silver nanostructures previously demonstrated, they point to the key role of the surface temperature at which the water dosing is made. Indeed we measure silver nanostructuring for dosing temperatures lower than 235 K. We follow, in real time during the water dosing, the modifications induced at the surface for two temperatures of 200 K and 240 K. Drastic differences are exhibited. At 200 K, after an initial stage of formation of molecular assembly strips along the [0 0 1], the reactive process leading to the conversion to an OH layer occurs clearly going along with the appearance and development of quasi-rectangular silver nanostructures. At 240 K, no such initial phase is evidenced. The complete conversion to an OH row structure of the scanned area occurs with no concomitant silver nanostructure formation. The dynamical behaviour of the reaction front allows the unravelling of the key role of the developing OH row ends intersecting the remaining Ag-O rows as particular reactive adsorption sites for the completion of the OH layer. © 2007 Elsevier B.V. All rights reserved.},\r\nauthor_keywords={Ag(1 1 0);  Nanostructures;  Oxygen;  Reaction at surfaces;  STM;  Water},\r\n}

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\n \n\n \n \n \n \n \n \n Aminomethyl derivatives of furancarboxylic acids in the Paal-Knorr reaction.\n \n \n \n \n\n\n \n Lapina, I.; Pevzner, L.; and Potekhin, A.\n\n\n \n\n\n\n Russian Journal of General Chemistry, 77(5): 923-925. 2007.\n cited By 1\n\n\n\n
\n\n\n\n \n \n $\"Aminomethyl$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Lapina2007923,\r\nauthor={Lapina, I.M. and Pevzner, L.M. and Potekhin, A.A.},\r\ntitle={Aminomethyl derivatives of furancarboxylic acids in the Paal-Knorr reaction},\r\njournal={Russian Journal of General Chemistry},\r\nyear={2007},\r\nvolume={77},\r\nnumber={5},\r\npages={923-925},\r\ndoi={10.1134/S1070363207050180},\r\nnote={cited By 1},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-34547286365&doi=10.1134%2fS1070363207050180&partnerID=40&md5=36d001443faf1871418fcef4ed6c90b9},\r\naffiliation={St. Petersburg State University, Universitetskii pr. 26, St. Petersburg, 198504, Russian Federation},\r\nabstract={Aminomethyl derivatives of furancarboxylic acids react with 1,4-dicarbonyl compounds under Paal-Knorr reaction conditions to form the pyrrole ring. It is found that α-aminomethyl derivatives of furancarboxylic acids react faster than their β analogs. The carboxy group adjacent to the aminomethyl fragment decelerates the process. © Nauka/Interperiodica 2007.},\r\ncorrespondence_address1={Lapina, I.M.; St. Petersburg State University, Universitetskii pr. 26, St. Petersburg, 198504, Russian Federation},\r\nissn={10703632},\r\nlanguage={English},\r\nabbrev_source_title={Russ. J. Gen. Chem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Biochemical analysis of Thermotoga maritima GH36 α-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases.\n \n \n \n \n\n\n \n Comfort, D.; Bobrov, K.; Ivanen, D.; Shabalin, K.; Harris, J.; Kulminskaya, A.; Brumer, H.; and Kelly, R.\n\n\n \n\n\n\n Biochemistry, 46(11): 3319-3330. 2007.\n cited By 62\n\n\n\n
\n\n\n\n \n \n $\"Biochemical$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Comfort20073319,\r\nauthor={Comfort, D.A. and Bobrov, K.S. and Ivanen, D.R. and Shabalin, K.A. and Harris, J.M. and Kulminskaya, A.A. and Brumer, H. and Kelly, R.M.},\r\ntitle={Biochemical analysis of Thermotoga maritima GH36 α-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases},\r\njournal={Biochemistry},\r\nyear={2007},\r\nvolume={46},\r\nnumber={11},\r\npages={3319-3330},\r\ndoi={10.1021/bi061521n},\r\nnote={cited By 62},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-33947433621&doi=10.1021%2fbi061521n&partnerID=40&md5=0052f204a32353c216bae321a8599fe1},\r\naffiliation={Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905, United States; Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biology Division, Gatchina, St. Petersburg 188300, Russian Federation; School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre, Stockholm, Sweden},\r\nabstract={Organization of glycoside hydrolase (GH) families into clans expands the utility of information on catalytic mechanisms of member enzymes. This issue was examined for GH27 and GH36 through biochemical analysis of GH36 α-galactosidase from Thermotoga maritima (TmGalA). Catalytic residues in TmGalA were inferred through structural homology with GH27 members to facilitate design of site-directed mutants. Product analysis confirmed that the wild type (WT) acted with retention of anomeric stereochemistry, analogous to GH27 enzymes. Conserved acidic residues were confirmed through kinetic analysis of D327G and D387G mutant enzymes, azide rescue, and determination of azide rescue products. Mutation of Asp327 to Gly resulted in a mutant that had a 200-800-fold lower catalytic rate on aryl galactosides relative to the WT enzyme. Azide rescue experiments using the D327G enzyme showed a 30-fold higher catalytic rate compared to without azide. Addition of azide to the reaction resulted in formation of azide β-D-galactopyranoside, confirming Asp327 as the nucleophilic residue. The Asp387Gly mutation was 1500-fold catalytically slower than the WT enzyme on p-nitrophenyl α-D-galactopyranoside. Analysis at different pH values produced a bell-shaped curve of the WT enzyme, but D387G exhibited higher activity with increasing pH. Catalyzed reactions with the D387G mutant in the presence of azide resulted in formation of azide α-D-galactopryanoside as the product of a retaining mechanism. These results confirm that Asp387 is the acid/base residue of TmGalA. Furthermore, they show that the biochemical characteristics of GH36 TmGalA are closely related to GH27 enzymes, confirming the mechanistic commonality of clan GH-D members. © 2007 American Chemical Society.},\r\ncorrespondence_address1={Kelly, R.M.; Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905, United States; email: rmkelly@eos.ncsu.edu},\r\nissn={00062960},\r\ncoden={BICHA},\r\npubmed_id={17323919},\r\nlanguage={English},\r\nabbrev_source_title={Biochemistry},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n On the formation of OH ordered layers by dissociation of H2O on an oxygen covered Ag(1 1 0) surface: An STM investigation.\n \n \n \n \n\n\n \n Guillemot, L.; and Bobrov, K.\n\n\n \n\n\n\n Surface Science, 601(3): 871-875. 2007.\n cited By 17\n\n\n\n
\n\n\n\n \n \n $\"On$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Guillemot2007871,\r\nauthor={Guillemot, L. and Bobrov, K.},\r\ntitle={On the formation of OH ordered layers by dissociation of H2O on an oxygen covered Ag(1 1 0) surface: An STM investigation},\r\njournal={Surface Science},\r\nyear={2007},\r\nvolume={601},\r\nnumber={3},\r\npages={871-875},\r\ndoi={10.1016/j.susc.2006.11.027},\r\nnote={cited By 17},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-33846489172&doi=10.1016%2fj.susc.2006.11.027&partnerID=40&md5=70cec31623d41a91d73dd05867e51bb7},\r\naffiliation={Laboratoire des Collisions Atomiques et Moléculaires, Unité Mixte de Recherche CNRS-Université Paris-Sud No 8625, Fédération Lumière-Matière, Bât. 351, Orsay, France},\r\nabstract={We present results of an STM investigation of water interaction with an oxygen covered Ag(1 1 0) on the example of the O(4 × 1) reconstructed surface. In agreement with numerous previous experimental works, using diffraction techniques, we found that a structure of OH(1 × 2) type, displaying rows in the [1 -1 0] direction, is formed. The new features revealed by this local probe study, is the presence of quasi rectangular islands evenly distributed across the terraces, with a density of 0.22 ± 0.03 and a mean area of 90 ± 15 nm2 at 220 K. They are imaged at an apparent height of 0.14 nm. It is remarkable that the same OH row structure is present on the whole terrace "on top" and "in between" the islands. These features are attributed to silver islands of mono-atomic height, formed by clustering of silver ad-atoms released during reaction of the O atoms with the water molecules. These findings point to a more complex behaviour of the reaction dynamics than previously described. They emphasise the key role of the silver ad-atoms, present in the added rows of the initial Ag(1 1 0)-O(4 × 1) surface, in the formation of the nanostructures. In turn it is concluded that the rows evidenced by this STM and previous diffraction studies, are formed by OH chains. © 2006 Elsevier B.V. All rights reserved.},\r\nauthor_keywords={Ag(1 1 0);  Oxygen;  Reaction at surfaces;  STM;  Water},\r\n}

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\n \n\n \n \n \n \n \n \n Biochemical and kinetic analysis of the GH3 family β-xylosidase from Aspergillus awamori X-100.\n \n \n \n \n\n\n \n Eneyskaya, E.; Ivanen, D.; Bobrov, K.; Isaeva-Ivanova, L.; Shabalin, K.; Savel'ev, A.; Golubev, A.; and Kulminskaya, A.\n\n\n \n\n\n\n Archives of Biochemistry and Biophysics, 457(2): 225-234. 2007.\n cited By 33\n\n\n\n
\n\n\n\n \n \n $\"Biochemical$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Eneyskaya2007225,\r\nauthor={Eneyskaya, E.V. and Ivanen, D.R. and Bobrov, K.S. and Isaeva-Ivanova, L.S. and Shabalin, K.A. and Savel'ev, A.N. and Golubev, A.M. and Kulminskaya, A.A.},\r\ntitle={Biochemical and kinetic analysis of the GH3 family β-xylosidase from Aspergillus awamori X-100},\r\njournal={Archives of Biochemistry and Biophysics},\r\nyear={2007},\r\nvolume={457},\r\nnumber={2},\r\npages={225-234},\r\ndoi={10.1016/j.abb.2006.10.024},\r\nnote={cited By 33},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-33846088514&doi=10.1016%2fj.abb.2006.10.024&partnerID=40&md5=1f794098c23a02469d18a5c7da5e4f5d},\r\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biology Division, Gatchina, 188300, Russian Federation; St. Petersburg Polytechnical University, Biophysics Department, Russian Federation},\r\nabstract={The β-xylosidase from Aspergillus awamori X-100 belonging to the family 3 glycoside hydrolase revealed a distinctive transglycosylating ability to produce xylooligosaccharides with degree of polymerization more than 7. In order to explain this fact, the enzyme has been subjected to the detailed biochemical study. The enzymatic hydrolysis of p-nitrophenyl β-d-xylopyranoside was found to occur with overall retention of substrate anomeric configuration suggesting cleavage of xylosidic bonds through a double-displacement mechanism. Kinetic study with aryl β-xylopyranosides substrates, in which leaving group pKas were in the range of 3.96-10.32, revealed monotonic function of log(kcat) and no correlation of log(kcat/Km) versus pKa values indicating deglycosylation as a rate-limiting step for the enzymatic hydrolysis. The classical bell-shaped pH dependence of kcat/Km indicated two ionizable groups in the β-xylosidase active site with apparent pKa values of 2.2 and 6.4. The kinetic parameters of hydrolysis, Km and kcat, of p-nitrophenyl β-d-1,4-xylooligosaccharides were very close to those for hydrolysis of p-nitrophenyl-β-d-xylopyranoside. Increase of p-nitrophenyl-β-d-xylopyranoside concentration up to 80 mM led to increasing of the reaction velocity resulting in kcatapp = 81 s- 1. Addition of α-methyl d-xylopyranoside to the reaction mixture at high concentration of p-nitrophenyl-β-d-xylopyranoside (50 mM) caused an acceleration of the β-xylosidase-catalyzed reactions and appearance of a new transglycosylation product, α-methyl d-xylopyranosyl-1,4-β-d-xylopyranoside, that was identified by 1H NMR spectroscopy. The kinetic model suggested for the enzymatic reaction was consistent with the results obtained. © 2006 Elsevier Inc. All rights reserved.},\r\nauthor_keywords={β-Xylosidase;  Acceleration and slowing of hydrolysis;  Brønsted analysis;  Exogenous nucleophile;  Transglycosylation},\r\nfunding_details={05-04-50825-MF_a, 01S03006},\r\nfunding_details={Российский Фонд Фундаментальных Исследований (РФФИ)05-04-49216-a},\r\n}

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\n \n\n \n \n \n \n \n \n Transferase and hydrolytic activities of the laminarinase from rhodothermus marinus and its M133A, M133C, and M133W mutants.\n \n \n \n \n\n\n \n Neustroev, K.; Golubev, A.; Sinnott, M.; Borriss, R.; Krah, M.; Brumer III, H.; Eneyskaya, E.; Shishlyannikov, S.; Shabalin, K.; Peshechonov, V.; Korolev, V.; and Kulminskaya, A.\n\n\n \n\n\n\n Glycoconjugate Journal, 23(7-8): 501-511. 2006.\n cited By 9\n\n\n\n
\n\n\n\n \n \n $\"Transferase$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Neustroev2006501,\r\nauthor={Neustroev, K.N. and Golubev, A.M. and Sinnott, M.L. and Borriss, R. and Krah, M. and Brumer III, H. and Eneyskaya, E.V. and Shishlyannikov, S. and Shabalin, K.A. and Peshechonov, V.T. and Korolev, V.G. and Kulminskaya, A.A.},\r\ntitle={Transferase and hydrolytic activities of the laminarinase from rhodothermus marinus and its M133A, M133C, and M133W mutants},\r\njournal={Glycoconjugate Journal},\r\nyear={2006},\r\nvolume={23},\r\nnumber={7-8},\r\npages={501-511},\r\ndoi={10.1007/s10719-006-6733-0},\r\nnote={cited By 9},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-33749165434&doi=10.1007%2fs10719-006-6733-0&partnerID=40&md5=40a9fe7a331bd7dd7076485066cc694e},\r\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biology Division, Gatchina 188300, Russian Federation; Department of Chemical and Biological Sciences, University of Huddersfield, Queensgate, Huddersfield HD1 3DH, United Kingdom; AG Bakteriengenetik, Institut fur Biologie, Humboldt Universitt Berlin, Chausseestrasse 117, Berlin D-10115, Germany; Department of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, Stockholm S-106 91, Sweden},\r\nabstract={Comparative studies of the transglycosylation and hydrolytic activities have been performed on the Rhodothermus marinus β-1,3-glucanase (laminarinase) and its M133A, M133C, and M133W mutants. The M133C mutant demonstrated near 20% greater rate of transglycosylation activity in comparison with the M133A and M133W mutants that was measured by NMR quantitation of nascent β(1-4) and β(1-6) linkages. To obtain kinetic probes for the wild-type enzyme and Met-133 mutants, p-nitrophenyl β-laminarin oligosaccharides of degree of polymerisation 2-8 were synthesized enzymatically. Catalytic efficiency values, k cat/K m, of the laminarinase catalysed hydrolysis of these oligosaccharides suggested possibility of four negative and at least three positive binding subsites in the active site. Comparison of action patterns of the wild-type and M133C mutant in the hydrolysis of the p-nitrophenyl-β-D-oligosac- charides indicated that the increased transglycosylation activity of the M133C mutant did not result from altered subsite affinities. The stereospecificity of the transglycosylation reaction also was unchanged in all mutants; the major transglycosylation products in hydrolysis of p-nitrophenyl laminaribioside were β-glucopyranosyl-β-1,3-D-glucopy- ranosyl-β-1,3-D-glucopyranose and β-glucopyranosyl-β-1, 3-D-glucopyranosyl-β-1,3-D- glucpyranosyl-β-1,3-D- glucopyranoxside. © 2006 Springer Science + Business Media, LLC.},\r\nauthor_keywords={Laminarinase;  p-nitrophenyl β-laminarin oligosaccharides;  Rhodothermus marinus;  Transglycosylation},\r\nfunding_details={Russian Academy of Sciences03-04-48756},\r\n}

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\n \n\n \n \n \n \n \n \n Reactions of alkyl (halomethyl)furancarboxylates with hexamethylenetetramine.\n \n \n \n \n\n\n \n Lapina, I.; Pevzner, L.; and Potekhin, A.\n\n\n \n\n\n\n Russian Journal of General Chemistry, 76(8): 1304-1309. 2006.\n cited By 2\n\n\n\n
\n\n\n\n \n \n $\"Reactions$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Lapina20061304,\r\nauthor={Lapina, I.M. and Pevzner, L.M. and Potekhin, A.A.},\r\ntitle={Reactions of alkyl (halomethyl)furancarboxylates with hexamethylenetetramine},\r\njournal={Russian Journal of General Chemistry},\r\nyear={2006},\r\nvolume={76},\r\nnumber={8},\r\npages={1304-1309},\r\ndoi={10.1134/S1070363206080251},\r\nnote={cited By 2},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-33749394412&doi=10.1134%2fS1070363206080251&partnerID=40&md5=595d8dd3026456a14ef45b6191d3be98},\r\naffiliation={St. Petersburg State University, Universitetskii pr. 26, St. Petersburg, 198504, Russian Federation},\r\nabstract={All isomers of (aminomethyl)furancarboxylic acids were prepared by the Delepine reaction from alkyl (halomethyl)furancarboxylates. Treatment of the initially formed quaternary salt with an ethanolic HCl solution yielded the salts of the corresponding unstable amino acid esters. A procedure for their purification to a high degree of purity was developed. Hydrolysis of the crude esters yielded stable amino acid salts. © Nauka/Interperiodica 2006.},\r\ncorrespondence_address1={Lapina, I.M.; St. Petersburg State University, Universitetskii pr. 26, St. Petersburg, 198504, Russian Federation},\r\nissn={10703632},\r\nlanguage={English},\r\nabbrev_source_title={Russ. J. Gen. Chem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Human milk antibodies with polysaccharide kinase activity.\n \n \n \n \n\n\n \n Karataeva, N.; Gorbunov, D.; Prokudin, I.; Buneva, V.; Kulminskaya, A.; Neustroev, K.; and Nevinsky, G.\n\n\n \n\n\n\n Immunology Letters, 103(1): 58-67. 2006.\n cited By 18\n\n\n\n
\n\n\n\n \n \n $\"Human$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Karataeva200658,\r\nauthor={Karataeva, N.A. and Gorbunov, D. and Prokudin, I.V. and Buneva, V.N. and Kulminskaya, A.A. and Neustroev, K.N. and Nevinsky, G.A.},\r\ntitle={Human milk antibodies with polysaccharide kinase activity},\r\njournal={Immunology Letters},\r\nyear={2006},\r\nvolume={103},\r\nnumber={1},\r\npages={58-67},\r\ndoi={10.1016/j.imlet.2005.10.009},\r\nnote={cited By 18},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-31544472062&doi=10.1016%2fj.imlet.2005.10.009&partnerID=40&md5=6ae82eba80fe4fde978964978d30782e},\r\naffiliation={Institute of Chemical Biology and Fundamental Medicine, Siberian Division, Russian Academy of Sciences, Lavrentieva Ave. 8, Novosibirsk 630090, Russian Federation; Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina, Russian Federation},\r\nabstract={It was shown for the first time that a small fraction of milk secretory IgA (sIgA) is tightly bound to oligosaccharides (oligoSACs) and polysaccharides (polySACs). The ability of sIgA to phosphorylate oligo- and polysaccharides was shown to be an intrinsic property of this antibody. In contrast to known kinases, sIgAs with polysaccharide kinase activity can transfer phosphoryl group to oligo- and polysaccharides not only from [γ-32P]ATP but can also use [32P]orthophosphate as a substrate of phosphorylation reaction. An extremely unusual property of polysaccharide kinase Abs is their high affinity for orthophosphate (Km = 15-77 μM), and orthophosphate is a better substrate than ATP. Two first examples of natural abzymes (Abzs) with synthetic activity were milk sIgA with protein and lipid kinase activities. Polysaccharide kinase sIgA of human milk is the third example of natural antibodies (Abs) with synthetic activity. © 2005 Elsevier B.V. All rights reserved.},\r\nauthor_keywords={Catalytic sIgA;  Human milk;  Phosphorylation of polysaccharides},\r\nfunding_details={Российский Фонд Фундаментальных Исследований (РФФИ)04-04-48211},\r\nfunding_details={04-04-81017},\r\n}

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\n \n 2005\n \n \n (3)\n \n \n

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\n \n\n \n \n \n \n \n \n Structural insights into the β-xylosidase from Trichoderma reesei obtained by synchrotron small-angle x-ray scattering and circular dichroism spectroscopy.\n \n \n \n \n\n\n \n Rojas, A.; Fischer, H.; Eneiskaya, E.; Kulminskaya, A.; Shabalin, K.; Neustroev, K.; Craievich, A.; Golubev, A.; and Polikarpov, I.\n\n\n \n\n\n\n Biochemistry, 44(47): 15578-15584. 2005.\n cited By 8\n\n\n\n
\n\n\n\n \n \n $\"Structural$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Rojas200515578,\r\nauthor={Rojas, A.L. and Fischer, H. and Eneiskaya, E.V. and Kulminskaya, A.A. and Shabalin, K.A. and Neustroev, K.N. and Craievich, A.F. and Golubev, A.M. and Polikarpov, I.},\r\ntitle={Structural insights into the β-xylosidase from Trichoderma reesei obtained by synchrotron small-angle x-ray scattering and circular dichroism spectroscopy},\r\njournal={Biochemistry},\r\nyear={2005},\r\nvolume={44},\r\nnumber={47},\r\npages={15578-15584},\r\ndoi={10.1021/bi050826j},\r\nnote={cited By 8},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-28244477099&doi=10.1021%2fbi050826j&partnerID=40&md5=a4b10b3dd7e1cbc9cc39cc98e1f48297},\r\naffiliation={Instituto de Física de São Carlos, Universidade de São Paulo, Av. Trabalhador Sao-carlense 400, CEP 13560-970, São Carlos, SP, Brazil; Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, 188300, Russian Federation; Instituto de Física, Universidade de São Paulo, São Paulo, SP, Brazil},\r\nabstract={The enzyme β-xylosidase from Trichoderma reesei, a member of glycosil hydrolase family 3 (GH3), is a glycoside hydrolase which acts at the glycosidic linkages of 1,4-β-xylooligosaccharides and that also exhibits α-L-arabinofuranosidase activity on 4-nitrophenyl α-L- arabinofuranoside. In this work, we show that the enzyme forms monomers in solution and derive the low-resolution molecular envelope of the β-xylosidase from small-angle X-ray scattering (SAXS) data using the ab initio simulated annealing algorithm. The radius of gyration and the maximum dimension of the β-xylosidase are 30.3 ± 0.2 and 90 ± 5 Å, respectively. In contrast to the fold of the only two structurally characterized members of GH3, the barley β-D-glucan exohydrolase and β-hexosaminidase from Vibrio cholerae, which have respectively two or one distinct domains, the shape of the β-xylosidase indicates the presence of three distinct structural modules. Domain recognition algorithms were used to show that the C-terminal part of the amino acid sequence of the protein forms the third domain. Circular dichroism spectroscopy and secondary structure prediction programs demonstrate that this additional domain adopts a predominantly β conformation. © 2005 American Chemical Society.},\r\ncorrespondence_address1={Polikarpov, I.; Instituto de Física de São Carlos, Universidade de São Paulo, Av. Trabalhador Sao-carlense 400, CEP 13560-970, São Carlos, SP, Brazil; email: ipolikarpov@if.sc.usp.br},\r\nissn={00062960},\r\ncoden={BICHA},\r\npubmed_id={16300407},\r\nlanguage={English},\r\nabbrev_source_title={Biochemistry},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Synthesis of arabinitol 1-phosphate and its use for characterization of arabinitol-phosphate dehydrogenase.\n \n \n \n \n\n\n \n Soroka, N.; Kulminskaya, A.; Eneyskaya, E.; Shabalin, K.; Uffimtcev, A.; Povelainen, M.; Miasnikov, A.; and Neustroev, K.\n\n\n \n\n\n\n Carbohydrate Research, 340(4): 539-546. 2005.\n cited By 1\n\n\n\n
\n\n\n\n \n \n $\"Synthesis$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Soroka2005539,\r\nauthor={Soroka, N.V. and Kulminskaya, A.A. and Eneyskaya, E.V. and Shabalin, K.A. and Uffimtcev, A.V. and Povelainen, M. and Miasnikov, A.N. and Neustroev, K.N.},\r\ntitle={Synthesis of arabinitol 1-phosphate and its use for characterization of arabinitol-phosphate dehydrogenase},\r\njournal={Carbohydrate Research},\r\nyear={2005},\r\nvolume={340},\r\nnumber={4},\r\npages={539-546},\r\ndoi={10.1016/j.carres.2004.11.030},\r\nnote={cited By 1},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-13844318805&doi=10.1016%2fj.carres.2004.11.030&partnerID=40&md5=7b3c8c2f5c84032596610ea7f0129cf7},\r\naffiliation={Molec. and Radiat. Biology Division, Petersburg Nuclear Physics Institute, Russian Academy of Science, Gatchina 188300, Russian Federation; Danisco Innovation, Sokeritehtaantie 20, Kantvik 02460, Finland},\r\nabstract={D-Arabinitol 1-phosphate (Ara-ol1-P), a substrate for d-arabinitol- phosphate dehydrogenase (APDH), was chemically synthesized from d-arabinonic acid in five steps (O-acetylation, chlorination, reduction, phosphorylation, and de-O-acetylation). Ara-ol1-P was used as a substrate for the characterization of APDH from Bacillus halodurans. APDH converts Ara-ol1-P to xylulose 5-phosphate in the oxidative reaction; both NAD+ and NADP+ were accepted as co-factors. Kinetic parameters for the oxidative and reductive reactions are consistent with a ternary complex mechanism. © 2004 Elsevier Ltd. All rights reserved.},\r\nauthor_keywords={Arabinitol 1-phosphate;  D-Arabinitol-phosphate dehydrogenase;  Pentitol metabolism;  Xylulose 5-phosphate},\r\n}

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\n \n\n \n \n \n \n \n \n Chemo-enzymatic synthesis of 4-methylumbelliferyl β-(1→4)-D-xylooligosides: New substrates for β-D-xylanase assays.\n \n \n \n \n\n\n \n Eneyskaya, E.; Ivanen, D.; Shabalin, K.; Kulminskaya, A.; Backinowsky, L.; Brumer III, H.; and Neustroev, K.\n\n\n \n\n\n\n Organic and Biomolecular Chemistry, 3(1): 146-151. 2005.\n cited By 21\n\n\n\n
\n\n\n\n \n \n $\"Chemo-enzymatic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Eneyskaya2005146,\r\nauthor={Eneyskaya, E.V. and Ivanen, D.R. and Shabalin, K.A. and Kulminskaya, A.A. and Backinowsky, L.V. and Brumer III, H. and Neustroev, K.N.},\r\ntitle={Chemo-enzymatic synthesis of 4-methylumbelliferyl β-(1→4)-D-xylooligosides: New substrates for β-D-xylanase assays},\r\njournal={Organic and Biomolecular Chemistry},\r\nyear={2005},\r\nvolume={3},\r\nnumber={1},\r\npages={146-151},\r\ndoi={10.1039/b409583a},\r\nnote={cited By 21},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-11844304068&doi=10.1039%2fb409583a&partnerID=40&md5=03142869ce72c091ef461d3d8b59f0b9},\r\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Molec. and Radiat. Biology Division, Gatchina, 188300, Russian Federation; N.D.Zelinsky Inst. of Organ. Chem., Russian Academy of Sciences, Leninsky prosp. 47, Moscow, 119991, Russian Federation; Department of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, S-106 91, Stockholm, Sweden},\r\nabstract={Transglycosylation catalyzed by a β-D-xylosidase from Aspergillus sp. was used to synthesize a set of 4-methylumbelliferyl (MU) β-1→4-D-xylooligosides having the common structure [β-D-Xyl-(1→4)]2-5-β-D-Xyl-MU. MU xylobioside synthesized chemically by the condensation of protected MU β-D-xylopyranoside with ethyl 2,3,4-tri-O-acetyl-l-thio-β-D-xylopyranoside was used as a substrate for transglycosylation with the β-D-xylosidase from Aspergillus sp. to produce higher MU xylooligosides. The structures of oligosaccharides obtained were established by 1H and 13C NMR spectroscopy and electrospray tandem mass spectrometry. MU β-D-xylooligosides synthesized were tested as fluorogenic substrates for the GH-10 family β-D-xylanase from Aspergillus orizae and the GH-11 family β-D-xylanase I from Trichoderma reesei. Both xylanases released the aglycone from MU xylobioside and the corresponding trioside. With substrates having d.p. 4 and 5, the enzymes manifested endolytic activities, splitting off MU, MUX, and MUX, primarily.},\r\ncorrespondence_address1={Kulminskaya, A.A.; Petersburg Nuclear Physics Institute, Russian Academy of Science, Molec. and Radiat. Biology Division, Gatchina, 188300, Russian Federation; email: kulm@omrb.pnpi.spb.ru},\r\nissn={14770520},\r\npubmed_id={15602610},\r\nlanguage={English},\r\nabbrev_source_title={Org. Biomol. Chem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Crystal structure of exo-inulinase from Aspergillus awamori: The enzyme fold and structural determinants of substrate recognition.\n \n \n \n \n\n\n \n Nagem, R.; Rojas, A.; Golubev, A.; Korneeva, O.; Eneyskaya, E.; Kulminskaya, A.; Neustroev, K.; and Polikarpov, I.\n\n\n \n\n\n\n Journal of Molecular Biology, 344(2): 471-480. 2004.\n cited By 119\n\n\n\n
\n\n\n\n \n \n $\"Crystal$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Nagem2004471,\r\nauthor={Nagem, R.A.P. and Rojas, A.L. and Golubev, A.M. and Korneeva, O.S. and Eneyskaya, E.V. and Kulminskaya, A.A. and Neustroev, K.N. and Polikarpov, I.},\r\ntitle={Crystal structure of exo-inulinase from Aspergillus awamori: The enzyme fold and structural determinants of substrate recognition},\r\njournal={Journal of Molecular Biology},\r\nyear={2004},\r\nvolume={344},\r\nnumber={2},\r\npages={471-480},\r\ndoi={10.1016/j.jmb.2004.09.024},\r\nnote={cited By 119},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-7444232112&doi=10.1016%2fj.jmb.2004.09.024&partnerID=40&md5=492321cd11eb0b00716a957cf862d721},\r\naffiliation={Inst. de Fís. de S. Carlos, Universidade de São Paulo, Av. Trabalhador S.-carlense 400, C., Brazil; Petersburg Nuclear Physics Institute, Gatchina, St Petersburg, 188300, Russia, Russian Federation; Voronezh State Technological Academy, Pr. Revolutsii 19, Voronezh, 394017, Russia, Russian Federation},\r\nabstract={Exo-inulinases hydrolyze terminal, non-reducing 2,1-linked and 2,6-linked β-d-fructofuranose residues in inulin, levan and sucrose releasing β-d-fructose. We present the X-ray structure at 1.55 Å resolution of exo-inulinase from Aspergillus awamori, a member of glycoside hydrolase family 32, solved by single isomorphous replacement with the anomalous scattering method using the heavy-atom sites derived from a quick cryo-soaking technique. The tertiary structure of this enzyme folds into two domains: the N-terminal catalytic domain of an unusual five-bladed β-propeller fold and the C-terminal domain folded into a β-sandwich-like structure. Its structural architecture is very similar to that of another member of glycoside hydrolase family 32, invertase (β-fructosidase) from Thermotoga maritima, determined recently by X-ray crystallography The exo-inulinase is a glycoprotein containing five N-linked oligosaccharides. Two crystal forms obtained under similar crystallization conditions differ by the degree of protein glycosylation. The X-ray structure of the enzyme:fructose complex, at a resolution of 1.87 Å, reveals two catalytically important residues: Asp41 and Glu241, a nucleophile and a catalytic acid/base, respectively. The distance between the side-chains of these residues is consistent with a double displacement mechanism of reaction. Asp189, which is part of the Arg-Asp-Pro motif, provides hydrogen bonds important for substrate recognition. © 2004 Elsevier Ltd. All rights reserved.},\r\nauthor_keywords={Aspergillus awamori;  crystallographic structure;  exo-inulinase;  glycoside hydrolase;  X-ray structure},\r\ncorrespondence_address1={Inst. de Fís. de S. Carlos, Universidade de São Paulo, Av. Trabalhador S.-carlense 400, C.Brazil; email: ipolikarpov@if.sc.usp.br},\r\nissn={00222836},\r\ncoden={JMOBA},\r\npubmed_id={15522299},\r\nlanguage={English},\r\nabbrev_source_title={J. Mol. Biol.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Crystal structures of β-galactosidase from Penicillium sp. and its complex with galactose.\n \n \n \n \n\n\n \n Rojas, A.; Nagem, R.; Neustroev, K.; Arand, M.; Adamska, M.; Eneyskaya, E.; Kulminskaya, A.; Garratt, R.; Golubev, A.; and Polikarpov, I.\n\n\n \n\n\n\n Journal of Molecular Biology, 343(5): 1281-1292. 2004.\n cited By 71\n\n\n\n
\n\n\n\n \n \n $\"Crystal$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n \n \n 1 download\n \n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Rojas20041281,\r\nauthor={Rojas, A.L. and Nagem, R.A.P. and Neustroev, K.N. and Arand, M. and Adamska, M. and Eneyskaya, E.V. and Kulminskaya, A.A. and Garratt, R.C. and Golubev, A.M. and Polikarpov, I.},\r\ntitle={Crystal structures of β-galactosidase from Penicillium sp. and its complex with galactose},\r\njournal={Journal of Molecular Biology},\r\nyear={2004},\r\nvolume={343},\r\nnumber={5},\r\npages={1281-1292},\r\ndoi={10.1016/j.jmb.2004.09.012},\r\nnote={cited By 71},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-6344266960&doi=10.1016%2fj.jmb.2004.09.012&partnerID=40&md5=06e4dd1641185ec1e9ccdb8cbf12cbde},\r\naffiliation={Inst. de Fís. de S. Carlos, Universidade de São Paulo, Av. Trabalhador S.-carlense 400, C., Brazil; Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg 188300, Russia, Russian Federation; Inst. of Pharmacology and Toxicology, University of Wuerzburg, Versbacher Str. 9, D-97078 W., Germany},\r\nabstract={β-Galactosidases catalyze the hydrolysis of β(1-3) and β(1-4) galactosyl bonds in oligosaccharides as well as the inverse reaction of enzymatic condensation and transglycosylation. Here we report the crystallographic structures of Penicillium sp. β-galactosidase and its complex with galactose solved by the SIRAS quick cryo-soaking technique at 1.90 Å and 2.10 Å resolution, respectively. The amino acid sequence of this 120 kDa protein was first assigned putatively on the basis of inspection of the experimental electron density maps and then determined by nucleotide sequence analysis. Primary structure alignments reveal that Penicillium sp. β-galactosidase belongs to family 35 of glycosyl hydrolases (GHF-35). This model is the first 3D structure for a member of GHF-35. Five distinct domains which comprise the structure are assembled in a way previously unobserved for β-galactosidases. Superposition of this complex with other β-galactosidase complexes from several hydrolase families allowed the identification of residue Glu200 as the proton donor and residue Glu299 as the nucleophile involved in catalysis. Penicillium sp. β-galactosidase is a glycoprotein containing seven N-linked oligosaccharide chains and is the only structure of a glycosylated β-galactosidase described to date. © 2004 Elsevier Ltd. All rights reserved.},\r\nauthor_keywords={β-galactosidases;  crystal structure;  glycosyl hydrolases;  Penicillium sp.;  quick cryo-soaking},\r\nfunding_details={Conselho Nacional de Desenvolvimento Científico e Tecnológico300220/96-0},\r\nfunding_details={Fundação de Amparo à Pesquisa do Estado de São Paulo99/03387-4, 01/07014-0, 02/14208-8},\r\nfunding_details={03-04-48756},\r\n}

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\n \n\n \n \n \n \n \n \n Catalytic properties of IgMs with amylolytic activity isolated from patients with multiple sclerosis.\n \n \n \n \n\n\n \n Ivanen, D.; Kulminskaya, A.; Shabalin, K.; Isaeva-Ivanova, L.; Ershova, N.; Saveliev, A.; Nevinsky, G.; and Neustroev, K.\n\n\n \n\n\n\n Medical Science Monitor, 10(8): BR273-BR280. 2004.\n cited By 15\n\n\n\n
\n\n\n\n \n \n $\"Catalytic$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Ivanen2004,\r\nauthor={Ivanen, D.R. and Kulminskaya, A.A. and Shabalin, K.A. and Isaeva-Ivanova, L.V. and Ershova, N.A. and Saveliev, A.N. and Nevinsky, G.A. and Neustroev, K.N.},\r\ntitle={Catalytic properties of IgMs with amylolytic activity isolated from patients with multiple sclerosis},\r\njournal={Medical Science Monitor},\r\nyear={2004},\r\nvolume={10},\r\nnumber={8},\r\npages={BR273-BR280},\r\nnote={cited By 15},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-4444373080&partnerID=40&md5=f7cf0fbd8ee67057a1c7571eec95efd2},\r\naffiliation={Molec. and Radiat. Biophys. Division, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina, Russian Federation; Novosibirsk Inst. of Bioorg. Chem., Siberian Div. Russ. Acad. Sci., Novosibirsk, Russian Federation; Biophysics Department, St. Petersburg Technical University, St. Petersburg, Russian Federation},\r\nabstract={Background: Recently, amylolytic activity was detected in IgMs isolated from the sera of the patients with multiple sclerosis. Materials/Methods: All purified samples of IgM were electrophoretically homogenous and did not contain any co-purified α-amylase and α-glucosidase activities, in accordance with a set of criteria developed for abzymes. The amylolytic activity of abzymes was studied in the hydrolysis of p-nitrophenyl α-D- maltooligosaccharides with different degrees of polymerization from 1 to 8 by TLC and reverse-phase HPLC techniques. Results: All IgM samples isolated from 54 patients with clinically definite multiple sclerosis demonstrated hydrolytic activity towards the above artificial substrates. The Michaelis constant values (Km) in the hydrolysis of p-nitrophenyl α-D-maltoheptaoside were in the range of 10 μmole to 0.1 mM. A part of the IgMs exhibited the ability to liberate free p-nitrophenyl or p-nitrophenyl α-D-glucosides, thus indicating the presence of an α-D-glucosidase activity. For a number of the investigated samples, specific amylolytic activity increased depending on the length of substrates (from p-nitrophenyl maltopentaoside to p-nitrophenyl maltohexaoside); for other IgMs, the opposite dependence was observed. All IgMs studied did not exhibit any other glycoside hydrolase activities toward p-nitrophenyl glycoside substrates. Conclusions: Abzyme fractions from different donors demonstrated catalytic heterogeneity in Michaelis-Menten parameters and different modes of action in the hydrolysis of p-nitrophenyl maltooligosaccharides. Enzymatic properties of the IgMs tested varied from human α-amylases. All investigated abzyme samples did not show transglycosylating ability.},\r\nauthor_keywords={Abzymes;  Amylolytic activity;  IgM;  Multiple sclerosis},\r\ncorrespondence_address1={Ivanen, D.R.; Molec. and Radiat. Biophys. Division, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina, Russian Federation},\r\nissn={12341010},\r\ncoden={MSMOF},\r\npubmed_id={15277988},\r\nlanguage={English},\r\nabbrev_source_title={Med. Sci. Monit.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Crystal structure of α-galactosidase from Trichoderma reesei and its complex with galactose: Implications for catalytic mechanism.\n \n \n \n \n\n\n \n Golubev, A.; Nagem, R.; Brandão Neto, J.; Neustroev, K.; Eneyskaya, E.; Kulminskaya, A.; Shabalin, K.; Savel'ev, A.; and Polikarpov, I.\n\n\n \n\n\n\n Journal of Molecular Biology, 339(2): 413-422. 2004.\n cited By 60\n\n\n\n
\n\n\n\n \n \n $\"Crystal$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Golubev2004413,\r\nauthor={Golubev, A.M. and Nagem, R.A.P. and Brandão Neto, J.R. and Neustroev, K.N. and Eneyskaya, E.V. and Kulminskaya, A.A. and Shabalin, K.A. and Savel'ev, A.N. and Polikarpov, I.},\r\ntitle={Crystal structure of α-galactosidase from Trichoderma reesei and its complex with galactose: Implications for catalytic mechanism},\r\njournal={Journal of Molecular Biology},\r\nyear={2004},\r\nvolume={339},\r\nnumber={2},\r\npages={413-422},\r\ndoi={10.1016/j.jmb.2004.03.062},\r\nnote={cited By 60},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-2342515384&doi=10.1016%2fj.jmb.2004.03.062&partnerID=40&md5=7b74bf3ff3c0db547bf566e37d2a41b9},\r\naffiliation={Petersburg Nuclear Physics Institute, Gatchina, St Petersburg, 188300, Russian Federation; Instituto de Física, Universidade de São Paulo, Av. Trabalhador Saocarlense, 400, CEP 13560-970, São Carlos, SP, Brazil; Biophysics Department, St. Petersburg Technical University, 29 Politechnicheskaya St., St Petersburg, 195251, Russian Federation},\r\nabstract={The crystal structures of α-galactosidase from the mesophilic fungus Trichoderma reesei and its complex with the competitive inhibitor, β-D-galactose, have been determined at 1.54Å and 2.0Å resolution, respectively. The α-galactosidase structure was solved by the quick cryo-soaking method using a single Cs derivative. The refined crystallographic model of the α-galactosidase consists of two domains, an N-terminal catalytic domain of the (β/α)8 barrel topology and a C-terminal domain which is formed by an antiparallel β-structure. The protein contains four N-glycosylation sites located in the catalytic domain. Some of the oligosaccharides were found to participate in inter-domain contacts. The galactose molecule binds to the active site pocket located in the center of the barrel of the catalytic domain. Analysis of the α-galactosidase- galactose complex reveals the residues of the active site and offers a structural basis for identification of the putative mechanism of the enzymatic reaction. The structure of the α-galactosidase closely resembles those of the glycoside hydrolase family 27. The conservation of two catalytic Asp residues, identified for this family, is consistent with a double-displacement reaction mechanism for the α-galactosidase. Modeling of possible substrates into the active site reveals specific hydrogen bonds and hydrophobic interactions that could explain peculiarities of the enzyme kinetics. © 2004 Elsevier Ltd. All rights reserved.},\r\nauthor_keywords={α-GAL, α-galactosidase;  α-galactosidase;  galactose;  GHF, glycoside hydrolase family;  N-glycosylation;  oxidative activation;  SIRAS, single isomorphous replacement with anomalous scattering;  Trichoderma reesei},\r\nfunding_details={Fundação de Amparo à Pesquisa do Estado de São Paulo03-04-48756},\r\nfunding_details={99/03387-4, 02/14208-8},\r\n}

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\n \n\n \n \n \n \n \n \n Human abzymes with amylolytic activity.\n \n \n \n \n\n\n \n Kulminskaya, A.; Saveliev, A.; and Neustroev, K.\n\n\n \n\n\n\n Trends in Glycoscience and Glycotechnology, 16(87): 17-31. 2004.\n cited By 10\n\n\n\n
\n\n\n\n \n \n $\"Human$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Kulminskaya200417,\r\nauthor={Kulminskaya, A.A. and Saveliev, A.N. and Neustroev, K.N.},\r\ntitle={Human abzymes with amylolytic activity},\r\njournal={Trends in Glycoscience and Glycotechnology},\r\nyear={2004},\r\nvolume={16},\r\nnumber={87},\r\npages={17-31},\r\ndoi={10.4052/tigg.16.17},\r\nnote={cited By 10},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-1942454781&doi=10.4052%2ftigg.16.17&partnerID=40&md5=a1f5d60fa308f499596c135dbbb0648e},\r\naffiliation={Molec. and Radiat. Biophys. Division, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina, Russian Federation; Biophysics Department, St.-Petersburg Technical University, St. Petersburg, Russian Federation; Petersburg Nuclear Physics Institute, Russian Academy of Science, Gatchina, St. Petersburg, 188300, Russian Federation; St. Petersburg Technol. Institute, Russian Federation; Petersburg Nuclear Physics Institute, Russian Federation; Laboratory of Enzymology; Biophysics Department, St. Petersburg Polytech. University, Russian Federation; Leningrad Nuclear Physics Institute, Russian Federation},\r\nabstract={Amylolytic abzymes are a new type of catalytically active human antibodies that have been found recently. Various immunoglobulins from the sera of patients with autoimmune diseases and human milk were found to possess amylolytic activity, which is expressed in their ability to hydrolyze α-(1,4)-D- glucosyl linkages of maltooligosaccharides, starch, glycogen, and several artificial substrates. Pure IgM fractions isolated from several tens of analyzed patients with clinically definite diagnoses of multiple sclerosis (MS) and systemic lupus erythematosus (SLE) had approximately three orders of magnitude higher specific amylolytic activity than those for healthy donors. Average values for the specific amylolytic activity of IgGs and slgAs from human milk were five times less than of IgMs from autoimmune patients. Strict criteria were used to prove that the amylolytic activity of abzymes was their intrinsic property and was not due to any enzyme contamination. Fab fragments derived from IgM and IgG fractions of human abzymes displayed the same level of amylolytic activity. Values for Michaelis constants KM in the abzyme-mediated hydrolysis of different α-D-maltooligosaccharides and α-D- maltooligosaccharides with chromogenic and fluorescent label on reducing end were in the range of 1-2 to 0.01 mM. Abzyme fractions from different donors demonstrated catalytic heterogeneity in Michaelis-Menten parameters and different modes of action in the hydrolysis of natural and artificial substrates. One part of amylolytic immunoglobulins exhibited exo-amylase action when others have also α-glucosidase activity yielding glucose and capable of cleaving p-nitrophenyl α-D-glucopyranoside. Enzymatic properties of all tested amylolytic abzymes distinguished from those of putative human α-amylases. None of the IgM, IgG, and sIgA samples investigated showed transglycosylating ability.},\r\nauthor_keywords={Abzymes;  Amylolytic activity;  Autoimmune pothotogies},\r\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Russian Academy of Science, Gatchina, St. Petersburg, 188300, Russian Federation; email: neustk@omrb.pnpi.spb.ru},\r\npublisher={Gakushin Publishing Company},\r\nissn={09157352},\r\nlanguage={English; Japanese},\r\nabbrev_source_title={Trends Glycosci. Glycotechnol.},\r\ndocument_type={Short Survey},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2003\n \n \n (7)\n \n \n

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\n \n\n \n \n \n \n \n \n Low-temperature electron transport on semiconductor surfaces.\n \n \n \n \n\n\n \n Lastapis, M.; Riedel, D.; Mayne, A.; Bobrov, K.; and Dujardin, G.\n\n\n \n\n\n\n Low Temperature Physics, 29(3): 196-201. 2003.\n cited By 4\n\n\n\n
\n\n\n\n \n \n $\"Low-temperature$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Lastapis2003196,\r\nauthor={Lastapis, M. and Riedel, D. and Mayne, A. and Bobrov, K. and Dujardin, G.},\r\ntitle={Low-temperature electron transport on semiconductor surfaces},\r\njournal={Low Temperature Physics},\r\nyear={2003},\r\nvolume={29},\r\nnumber={3},\r\npages={196-201},\r\ndoi={10.1063/1.1542440},\r\nnote={cited By 4},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-21144435752&doi=10.1063%2f1.1542440&partnerID=40&md5=4e8d7e0d4d9733cb0c2cc169e7bc54e2},\r\naffiliation={Laboratoire de Photophysique Moleculaire, Batiment 210, Universite Paris-Sud, 91405 Orsay Cedex, France},\r\nabstract={The low-temperature electron transport on semiconductor surfaces has been studied using an ultrahigh-vacuum, variable temperature scanning tunneling microscope (STM). The STM I(V) spectroscopy performed at various temperatures has made it possible to investigate the temperature dependence (300 K to 35 K) of the surface conductivity of three different semiconductor surfaces: highly doped n-type Si(100), p-type Si(100), and hydrogenated C(100). Low temperature freezing of specific surface electronic channels on the highly doped n-type Si(100) and moderately doped p-type Si(100) surfaces could be achieved, whereas the total surface conductivity on the hydrogenated C(100) surface can be frozen below only 180 K. © 2003 American Institute of Physics.},\r\ncorrespondence_address1={Lastapis, M.; Laboratoire de Photophysique Moleculaire, Batiment 210, Universite Paris-Sud, 91405 Orsay Cedex, France},\r\nissn={1063777X},\r\nlanguage={English},\r\nabbrev_source_title={Low Temp. Phys},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Biochemical characterization of Aspergillus awamori exoinulinase: Substrate binding characteristics and regioselectivity of hydrolysis.\n \n \n \n \n\n\n \n Kulminskaya, A.; Arand, M.; Eneyskaya, E.; Ivanen, D.; Shabalin, K.; Shishlyannikov, S.; Saveliev, A.; Korneeva, O.; and Neustroev, K.\n\n\n \n\n\n\n Biochimica et Biophysica Acta - Proteins and Proteomics, 1650(1-2): 22-29. 2003.\n cited By 19\n\n\n\n
\n\n\n\n \n \n $\"Biochemical$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Kulminskaya200322,\r\nauthor={Kulminskaya, A.A. and Arand, M. and Eneyskaya, E.V. and Ivanen, D.R. and Shabalin, K.A. and Shishlyannikov, S.M. and Saveliev, A.N. and Korneeva, O.S. and Neustroev, K.N.},\r\ntitle={Biochemical characterization of Aspergillus awamori exoinulinase: Substrate binding characteristics and regioselectivity of hydrolysis},\r\njournal={Biochimica et Biophysica Acta - Proteins and Proteomics},\r\nyear={2003},\r\nvolume={1650},\r\nnumber={1-2},\r\npages={22-29},\r\ndoi={10.1016/S1570-9639(03)00187-0},\r\nnote={cited By 19},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141976294&doi=10.1016%2fS1570-9639%2803%2900187-0&partnerID=40&md5=76f2ea6fad6e6c41f67115d15b3b1df9},\r\naffiliation={Div. of Molec. and Radiat. Biophys., Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Orlova Rosha, St. Petersburg 188350, Russian Federation; Inst. of Pharmacology and Toxicology, University of Wuerzburg, Germany; Biophysics Department, St. Petersburg Technical University, Russian Federation; Voronesh State Technological Academy, Russian Federation},\r\nabstract={1H-NMR analysis was applied to investigate the hydrolytic activity of Aspergillus awamori inulinase. The obtained NMR signals and deduced metabolite pattern revealed that the enzyme cleaves off only fructose from inulin and does not possess transglycosylating activity. Kinetics for the enzyme hydrolysis of inulooligosaccharides with different degree of polymerization (d.p.) were recorded. The enzyme hydrolyzed both β2,1- as well as β2,6-fructosyl linkages in fructooligosaccharides. From the k cat/Km ratios obtained with inulooligosaccharides with d.p. from 2 to 7, we deduce that the catalytic site of the inulinase contains at least five fructosyl-binding sites and can be classified as exo-acting enzyme. Product analysis of inulopentaose and inulohexaose hydrolysis by the Aspergillus inulinase provided no evidence for a possible multiple-attack mode of action, suggesting that the enzyme acts exclusively as an exoinulinase. © 2003 Elsevier B.V. All rights reserved.},\r\nauthor_keywords={Exoinulinase;  Fructooligosaccharide;  Fructosyl-binding site;  Multiple attack},\r\n}

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\n \n\n \n \n \n \n \n \n Multiple enzymic activities of human milk lactoferrin.\n \n \n \n \n\n\n \n Kanyshkova, T.; Babina, S.; Semenov, D.; Isaeva, N.; Vlassov, A.; Neustroev, K.; Kul'minskaya, A.; Buneva, V.; and Nevinsky, G.\n\n\n \n\n\n\n European Journal of Biochemistry, 270(16): 3353-3361. 2003.\n cited By 60\n\n\n\n
\n\n\n\n \n \n $\"Multiple$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Kanyshkova20033353,\r\nauthor={Kanyshkova, T.G. and Babina, S.E. and Semenov, D.V. and Isaeva, N. and Vlassov, A.V. and Neustroev, K.N. and Kul'minskaya, A.A. and Buneva, V.N. and Nevinsky, G.A.},\r\ntitle={Multiple enzymic activities of human milk lactoferrin},\r\njournal={European Journal of Biochemistry},\r\nyear={2003},\r\nvolume={270},\r\nnumber={16},\r\npages={3353-3361},\r\ndoi={10.1046/j.1432-1033.2003.03715.x},\r\nnote={cited By 60},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042928467&doi=10.1046%2fj.1432-1033.2003.03715.x&partnerID=40&md5=f17181fc4f39dda0aab4846a7354d100},\r\naffiliation={Novosibirsk Inst. of Bioorg. Chem., Siberian Div. of Russ. Acad. of Sci., Novosibirsk, Russian Federation; Novosibirsk State University, Novosibirsk, Russian Federation; Institute of Cytology and Genetics, Siberian Div. Russ. Acad. of Sci., Novosibirsk, Russian Federation; Petersburg Nucl. Phys. Inst. R., St Peterburg, Russian Federation; Laboratory of Repair Enzymes, Novosibirsk Inst. of Bioorg. Chem., 8, Lavrentieva Ave., 630090, Novosibirsk, Russian Federation},\r\nabstract={Lactoferrin (LF) is a Fe3+-binding glycoprotein, first recognized in milk and then in other human epithelial secretions and barrier fluids. Many different functions have been attributed to LF, including protection from iron-induced lipid peroxidation, immunomodulation and cell growth regulation, DNA binding, and transcriptional activation. Its physiological role is still unclear, but it has been suggested to be responsible for primary defense against microbial and viral infection. We present evidence that different subfractions of purified human milk LF possess five different enzyme activities: DNase, RNase, ATPase, phosphatase, and malto-oligosaccharide hydrolysis. LF is the predominant source of these activities in human milk. Some of its catalytically active subfractions are cytotoxic and induce apoptosis. The discovery that LF possesses these activities may help to elucidate its many physiological functions, including its protective role against microbial and viral infection.},\r\nauthor_keywords={Enzymic activities;  Human milk;  Lactoferrin;  Protection},\r\ncorrespondence_address1={Nevinsky, G.A.; Laboratory of Repair Enzymes, Novosibirsk Inst. of Bioorg. Chem., 8, Lavrentieva Ave., 630090, Novosibirsk, Russian Federation; email: nevinsky@niboch.nsc.ru},\r\nissn={00142956},\r\ncoden={EJBCA},\r\npubmed_id={12899692},\r\nlanguage={English},\r\nabbrev_source_title={Eur. J. Biochem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Enzymatic synthesis of 4-methylumbelliferyl (1→3)-β-D-glucooligosaccharides - New substrates for β-1,3-1,4-D-glucanase.\n \n \n \n \n\n\n \n Borriss, R.; Krah, M.; Brumer III, H.; Kerzhner, M.; Ivanen, D.; Eneyskaya, E.; Elyakova, L.; Shishlyannikov, S.; Shabalin, K.; and Neustroev, K.\n\n\n \n\n\n\n Carbohydrate Research, 338(14): 1455-1467. 2003.\n cited By 21\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Borriss20031455,\r\nauthor={Borriss, R. and Krah, M. and Brumer III, H. and Kerzhner, M.A. and Ivanen, D.R. and Eneyskaya, E.V. and Elyakova, L.A. and Shishlyannikov, S.M. and Shabalin, K.A. and Neustroev, K.N.},\r\ntitle={Enzymatic synthesis of 4-methylumbelliferyl (1→3)-β-D-glucooligosaccharides - New substrates for β-1,3-1,4-D-glucanase},\r\njournal={Carbohydrate Research},\r\nyear={2003},\r\nvolume={338},\r\nnumber={14},\r\npages={1455-1467},\r\ndoi={10.1016/S0008-6215(03)00199-X},\r\nnote={cited By 21},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-12444289585&doi=10.1016%2fS0008-6215%2803%2900199-X&partnerID=40&md5=6b826af425843700bdd66b4c7e201fd7},\r\naffiliation={AG Bakteriengenetik, Institut fur Biologie, Humboldt Universität Berlin, Chausseestrasse 117, D-10115 Berlin, Germany; Department of Biotechnology, Royal Institute of Technology (KTH), Stockholm Ctr. Phys., Astron.,/B., Roslagsvägen 30 B, S-106 91 Stockholm, Sweden; Petersburg Nuclear Physics Institute, Russian Academy of Science, Molec./Radiation Biology Division, Gatchina, St. Petersburg 188300, Russian Federation; Pac. Inst. of Bioorganic Chemistry, Far E. Div. Russ. Acad. of Sciences, pr. 100-letiya Vladivostoka 159, Vladivostok 690022, Russian Federation},\r\nabstract={The transglycosylation reactions catalyzed by β-1,3-D-glucanases (laminaranases) were used to synthesize a number of 4-methylumbelliferyl (MeUmb) (1→3)-β-D-gluco-oligosaccharides having the common structure [β-D-Glcp-(1→3)]n-β-D-Glcp-MeUmb, where n=1-5. The β-1,3-D-glucanases used were purified from the culture liquid of Oerskovia sp. and from a homogenate of the marine mollusc Spisula sachalinensis. Laminaran and curdlan were used as (1→3)-β-D-glucan donor substrates, while MeUmb-β-D-glucoside (MeUmbGlcp) was employed as a transglycosylation acceptor. Modification of [β-D-Glcp-(1→3)]2-β-D-Glcp-MeUmb (MeUmbG3) gives 4,6-O-benzylidene-D-glucopyranosyl or 4,6-O-ethylidene-D-glucopyranosyl groups at the non-reducing end of artificial oligosaccharides. The structures of all oligosaccharides obtained were solved by 1H and 13C NMR spectroscopy and electrospray tandem mass spectrometry. The synthetic oligosaccharides were shown to be substrates for a β-1,3-1,4-D-glucanase from Rhodothermus marinus, which releases MeUmb from β-di- and β-triglucosides and from acetal-protected β-triglucosides. When acting upon substrates with d.p.&gt;3, the enzyme exhibits an endolytic activity, primarily cleaving off MeUmbGlcp and MeUmbG2. © 2003 Elsevier Science Ltd. All rights reserved.},\r\nauthor_keywords={4-Methylumbelliferyl (1→3)-β-D-glucoside;  Laminaranase;  Rhodothermus marinus;  Transglycosylation;  β-1,3-1,4-D-Glucanase},\r\n}

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\n \n\n \n \n \n \n \n \n Amylolytic activity of IgM and IgG antibodies from patients with multiple sclerosis.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Immunology Letters, 86(3): 291-297. 2003.\n cited By 54\n\n\n\n
\n\n\n\n \n \n $\"Amylolytic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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\n \n\n \n \n \n \n \n \n Biochemical and genetic characterization of a novel enzyme of pentitol metabolism: D-arabitol-phosphate dehydrogenase.\n \n \n \n \n\n\n \n Povelainen, M.; Eneyskaya, E.; Kulminskaya, A.; Ivanen, D.; Kalkkinen, N.; Neustroev, K.; and Miasnikov, A.\n\n\n \n\n\n\n Biochemical Journal, 371(1): 191-197. 2003.\n cited By 12\n\n\n\n
\n\n\n\n \n \n $\"Biochemical$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Povelainen2003191,\r\nauthor={Povelainen, M. and Eneyskaya, E.V. and Kulminskaya, A.A. and Ivanen, D.R. and Kalkkinen, N. and Neustroev, K.N. and Miasnikov, A.N.},\r\ntitle={Biochemical and genetic characterization of a novel enzyme of pentitol metabolism: D-arabitol-phosphate dehydrogenase},\r\njournal={Biochemical Journal},\r\nyear={2003},\r\nvolume={371},\r\nnumber={1},\r\npages={191-197},\r\ndoi={10.1042/BJ20021096},\r\nnote={cited By 12},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242286156&doi=10.1042%2fBJ20021096&partnerID=40&md5=df69825a9a36085bf9b1f3869e73e4b1},\r\naffiliation={Danisco Cultor Innovation, Sokeritehtaantie 20, Kantvik 02460, Finland; Petersburg Nuclear Physics Institute, Gatchina, Leningrad District 188300, Russian Federation; Institute of Biotechnology, University of Helsinki, Viikinkaari 9, Helsinki 00014, Finland},\r\nabstract={An enzyme with a specificity that has not been described previously, D-arabitol-phosphate dehydrogenase (APDH), has been purified from cell lysate of Enterococcus avium. SDS/PAGE indicated that the enzyme had a molecular mass of 41 ± 2 kDa, whereas a molecular mass of 160 ± 5 kDa was observed under non-denaturing conditions, implying that the APDH may exist as a tetramer with identical subunits. Purified APDH was found to have a narrow substrate specificity, converting only D-arabitol 1-phosphate and D-arabitol 5-phosphate into xylulose 5-phosphate and ribulose 5-phosphate, respectively, in the oxidative reaction. Both NAD+ and NADP+ were accepted as cofactors. Based on the partial protein sequences, the APDH gene was cloned. Homology comparisons place APDH within the medium-range dehydrogenase family. Unlike most members of this family, APDH requires Mn2+ but no Zn2+ for enzymic activity. The DNA sequence surrounding the gene suggests that it belongs to an operon that also contains several components of phosphotransferase system. Both biochemical evidence and protein sequence homology comparisons indicate that similar enzymes are widespread among the Gram-positive bacteria. Their apparent biological role is to participate in arabitol catabolism via the 'arabitol phosphate route', similar to the ribitol and xylitol catabolic routes described previously.},\r\nauthor_keywords={Enterococcus avium;  NADH-dependent dehydrogenase;  Pentitol phosphate metabolism;  Xylulose 5-phosphate},\r\ncorrespondence_address1={Miasnikov, A.N.; Danisco Cultor Innovation, Sokeritehtaantie 20, Kantvik 02460, Finland; email: andrei.miasnikov@danisco.com},\r\nissn={02646021},\r\ncoden={BIJOA},\r\npubmed_id={12467497},\r\nlanguage={English},\r\nabbrev_source_title={Biochem. J.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Enzymatic synthesis of β-xylanase substrates: Transglycosylation reactions of the β-xylosidase from Aspergillus sp.\n \n \n \n \n\n\n \n Eneyskaya, E.; Brumer III, H.; Backinowsky, L.; Ivanen, D.; Kulminskaya, A.; Shabalin, K.; and Neustroev, K.\n\n\n \n\n\n\n Carbohydrate Research, 338(4): 313-325. 2003.\n cited By 56\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Eneyskaya2003313,\r\nauthor={Eneyskaya, E.V. and Brumer III, H. and Backinowsky, L.V. and Ivanen, D.R. and Kulminskaya, A.A. and Shabalin, K.A. and Neustroev, K.N.},\r\ntitle={Enzymatic synthesis of β-xylanase substrates: Transglycosylation reactions of the β-xylosidase from Aspergillus sp.},\r\njournal={Carbohydrate Research},\r\nyear={2003},\r\nvolume={338},\r\nnumber={4},\r\npages={313-325},\r\ndoi={10.1016/S0008-6215(02)00467-6},\r\nnote={cited By 56},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347895063&doi=10.1016%2fS0008-6215%2802%2900467-6&partnerID=40&md5=7a4c435abc1b32da3037d9f62b6fc467},\r\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Molec./Radiation Biology Division, Gatchina, St. Petersburg 188350, Russian Federation; Department of Biotechnology, Royal Institute of Technology (KTH), Stockholm Ctr. for Phys., A.,/B., Roslagsvägen 30 B, S-106 91 Stockholm, Sweden; N.D. Zelinsky Inst. of Organ. Chem., Russian Academy of Sciences, Leninsky prosp. 47, Moscow 119991, Russian Federation},\r\nabstract={A β-D-xylosidase with molecular mass of 250±5 kDa consisting of two identical subunits was purified to homogeneity from a cultural filtrate of Aspergillus sp. The enzyme manifested high transglycosylation activity in transxylosylation with p-nitrophenyl β-D-xylopyranoside (PNP-X) as substrate, resulting in regio- and stereoselective synthesis of p-nitrophenyl (PNP) β-(1→4)-D-xylooligosaccharides with dp 2-7. All transfer products were isolated from the reaction mixtures by HPLC and their structures established by electrospray mass spectrometry and 1H and 13C NMR spectroscopy. The glycosides synthesised, β-Xyl-1→(4-β-Xyl-1→)n4-β-Xyl-OC 6H4NO2-p (n=1-5), were tested as chromogenic substrates for family 10 β-xylanase from Aspergillus orizae (XynA) and family 11 β-xylanase I from Trichoderma reesei (XynT) by reversed-phase HPLC and UV-spectroscopy techniques. The action pattern of XynA against the foregoing PNP β-(1→4)-D-xylooligosaccharides differed from that of XynT in that the latter released PNP mainly from short PNP xylosides (dp 2-3) while the former liberated PNP from the entire set of substrates synthesised. © 2002 Elsevier Science Ltd. All rights reserved.},\r\nauthor_keywords={β-D-Xylosidase;  β-Xylanase substrates;  Aspergillus sp.;  P-Nitrophenyl β-(1→4)-D-xylooligosaccharides;  Transglycosylation},\r\n}

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\n \n 2002\n \n \n (6)\n \n \n

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\n \n\n \n \n \n \n \n \n Human autoantibodies with amylolytic activity.\n \n \n \n \n\n\n \n Ivanen, D.; Kulminskaya, A.; Ershova, N.; Eneyskaya, E.; Shabalin, K.; Savel'ev, A.; Kanyshkova, T.; Buneva, V.; Nevinsky, G.; and Neustroev, K.\n\n\n \n\n\n\n Biologia - Section Cellular and Molecular Biology, 57(SUPPL. 11): 253-260. 2002.\n cited By 6\n\n\n\n
\n\n\n\n \n \n $\"Human$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Ivanen2002253,\r\nauthor={Ivanen, D.R. and Kulminskaya, A.A. and Ershova, N.A. and Eneyskaya, E.V. and Shabalin, K.A. and Savel'ev, A.N. and Kanyshkova, T.G. and Buneva, V.N. and Nevinsky, G.A. and Neustroev, K.N.},\r\ntitle={Human autoantibodies with amylolytic activity},\r\njournal={Biologia - Section Cellular and Molecular Biology},\r\nyear={2002},\r\nvolume={57},\r\nnumber={SUPPL. 11},\r\npages={253-260},\r\nnote={cited By 6},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-19044395559&partnerID=40&md5=7b3dc1b59273e9e8db00ebaa3013ce73},\r\naffiliation={Molec. and Radiat. Biophys. Division, Petersburg Nucl. Phys. Inst. R., 188350, Gatchina, St. Petersburg, Russian Federation; Novosibirsk Inst. of Bioorg. Chem., Siberian Div. of Russ. Acad. of Sci., Novosibirsk, Russian Federation; Biophysics Department, St. Petersburg Technical University, St. Petersburg, Russian Federation},\r\nabstract={We have investigated the activity of IgG and IgM fractions from patients suffering from multiple sclerosis, as well as that of IgG and sIgA fractions isolated from human milk of healthy women, in the hydrolysis of artificial substrates and maltooligosaccharides with different degrees of polymerisation. All electrophoretically-homogeneous preparations of IgG and its Fab fragments, as well as sIgA and IgM antibodies, possessed amylolytic activity. The specific activities of catalytic antibodies from human milk varied in the range from 0.11 up to 0.2 U/mg, i.e. about three orders higher than those for IgGs from the sera of multiple sclerosis patients and one order higher than those for cancer patients. Milk IgG and sIgA fractions revealed Michaelis constants for hydrolysis of p-nitrophenyl α-D-maltooligosides in the range of 10-4 M. Fractions of autoantibodies from various donors revealed different modes of action in hydrolysis of maltooligosaccharides, p-nitrophenyl maltooligosaccharides and p-nitrophenyl α-D-glucopyranoside.},\r\nauthor_keywords={α-amylase;  Autoantibodies from human;  Autoimmunity disease},\r\ncorrespondence_address1={Neustroev, K.N.; Molec. and Radiat. Biophys. Division, Petersburg Nucl. Phys. Inst. R., 188350, Gatchina, St. Petersburg, Russian Federation; email: neustk@omrb.pnpi.spb.ru},\r\nissn={13356399},\r\nlanguage={English},\r\nabbrev_source_title={Biol. Sect. Cell. Mol. Biol.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Resonant electron injection as an atomic-scale tool for surface studies.\n \n \n \n \n\n\n \n Bobrov, K.; Soukiassian, L.; Mayne, A.; Dujardin, G.; and Hoffman, A.\n\n\n \n\n\n\n Physical Review B - Condensed Matter and Materials Physics, 66(19): 1954031-1954036. 2002.\n cited By 13\n\n\n\n
\n\n\n\n \n \n $\"Resonant$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Bobrov20021954031,\r\nauthor={Bobrov, K. and Soukiassian, L. and Mayne, A.J. and Dujardin, G. and Hoffman, A.},\r\ntitle={Resonant electron injection as an atomic-scale tool for surface studies},\r\njournal={Physical Review B - Condensed Matter and Materials Physics},\r\nyear={2002},\r\nvolume={66},\r\nnumber={19},\r\npages={1954031-1954036},\r\nart_number={195403},\r\nnote={cited By 13},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037113733&partnerID=40&md5=1bd66bb7c030253934ae0e3464732bc3},\r\naffiliation={Lab. de Photophysique Moleculaire, Bâtiment 210, Université Paris-Sud, 91405 Orsay Cedex, France; Department of Chemistry, Technion Israel Inst. of Technology, Haifa 32000, Israel; Lab. des Collisions Atomiques/Molec., Bâtiment 351, Université Paris-Sud, 91405 Orsay Cedex, France},\r\nabstract={Three surfaces - clean C(100)-(2x1) diamond, hydrogenated C(100)-(2x1):H diamond and clean Si(100)-(2x1) silicon - were imaged at the atomic scale using the scanning tunneling microscope (STM) operating in an unconventional resonant electron injection mode. The reflection of electrons, forming a resonance in the tip-simple vacuum gap, would seem to play a crucial role in the STM's ability to visualize surfaces under these conditions. The first barrier resonance was found to be critical for this surface visualization in two respects. First, a necessary condition was that the STM topographies had to be recorded at a bias coinciding with the energy of the first barrier resonance. Second, the corrugation of the STM topographies was found to be directly proportional to the fineness of the first barrier resonance. Barrier resonances were found to be very sensitive to the difference in energy from the bottom of conduction band. The influence of the bulk electronic structure of the particular sample on the resonance fineness is discussed.},\r\ncorrespondence_address1={Bobrov, K.; Lab. des Collisions Atomiques/Molec., Bâtiment 351, Université Paris-Sud, 91405 Orsay Cedex, France},\r\nissn={01631829},\r\ncoden={PRBMD},\r\nlanguage={English},\r\nabbrev_source_title={Phys. Rev. B Condens. Matter Mater. Phys.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Structural insights into the β-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography.\n \n \n \n \n\n\n \n Aparicio, R.; Fischer, H.; Scott, D.; Verschueren, K.; Kulminskaya, A.; Eneiskaya, E.; Neustroev, K.; Craievich, A.; Golubev, A.; and Polikarpov, I.\n\n\n \n\n\n\n Biochemistry, 41(30): 9370-9375. 2002.\n cited By 13\n\n\n\n
\n\n\n\n \n \n $\"Structural$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Aparicio20029370,\r\nauthor={Aparicio, R. and Fischer, H. and Scott, D.J. and Verschueren, K.H.G. and Kulminskaya, A.A. and Eneiskaya, E.V. and Neustroev, K.N. and Craievich, A.F. and Golubev, A.M. and Polikarpov, I.},\r\ntitle={Structural insights into the β-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography},\r\njournal={Biochemistry},\r\nyear={2002},\r\nvolume={41},\r\nnumber={30},\r\npages={9370-9375},\r\ndoi={10.1021/bi025811p},\r\nnote={cited By 13},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037199487&doi=10.1021%2fbi025811p&partnerID=40&md5=993fa9e3c01e8e6234bfe0cce91b71f8},\r\naffiliation={Instituto de Física Gleb Wataghin, Universidade Estadual de Campinas, Campinas, SP, Brazil; Instituto de Física, Universidade de Sao Paulo, Sao Paulo, SP, Brazil; Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol, United Kingdom; Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom; Instituto de Física de Sao Carlos, Universidade de Sao Paulo, CP 369, 13560-970, Sao Carlos, SP, Brazil; Division of Molecular Carcinogenesis, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, Netherlands; Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, 188300, Russian Federation},\r\nabstract={A molecular envelope of the β-mannosidase from Trichoderma reesei has been obtained by combined use of solution small-angle X-ray scattering (SAXS) and protein crystallography. Crystallographic data at 4 Å resolution have been used to enhance informational content of the SAXS data and to obtain an independent, more detailed protein shape. The phased molecular replacement technique using a low resolution SAXS model, building, and refinement of a free atom model has been employed successfully. The SAXS and crystallographic free atom models exhibit a similar globular form and were used to assess available crystallographic models of glycosyl hydrolases. The structure of the β-galactosidase, a member of a family 2, clan GHA glycosyl hydrolases, shows an excellent fit to the experimental molecular envelope and distance distribution function of the β-mannosidase, indicating gross similarities in their three-dimensional structures. The secondary structure of β-mannosidase quantified by circular dichroism measurements is in a good agreement with that of β-galactosidase. We show that a comparison of distance distribution functions in combination with 1D and 2D sequence alignment techniques was able to restrict the number of possible structurally homologous proteins. The method could be applied as a general method in structural genomics and related fields once protein solution scattering data are available.},\r\ncorrespondence_address1={Polikarpov, I.; Instituto de Fisica de Sao Carlos, Universidade de São Paulo, CP 369, 13560-970 São Carlos, SP, Brazil; email: ipolikarpov@if.sc.usp.br},\r\nissn={00062960},\r\ncoden={BICHA},\r\npubmed_id={12135358},\r\nlanguage={English},\r\nabbrev_source_title={Biochemistry},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n 1-O-Acetyl-β-D-galactopyranose: A novel substrate for the transglycosylation reaction catalyzed by the β-galactosidase from Penicillium sp.\n \n \n \n \n\n\n \n Zinin, A.; Eneyskaya, E.; Shabalin, K.; Kulminskaya, A.; Shishlyannikov, S.; and Neustroev, K.\n\n\n \n\n\n\n Carbohydrate Research, 337(7): 635-642. 2002.\n cited By 16\n\n\n\n
\n\n\n\n \n \n $\"1-O-Acetyl-β-D-galactopyranose:$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Zinin2002635,\r\nauthor={Zinin, A.I. and Eneyskaya, E.V. and Shabalin, K.A. and Kulminskaya, A.A. and Shishlyannikov, S.M. and Neustroev, K.N.},\r\ntitle={1-O-Acetyl-β-D-galactopyranose: A novel substrate for the transglycosylation reaction catalyzed by the β-galactosidase from Penicillium sp.},\r\njournal={Carbohydrate Research},\r\nyear={2002},\r\nvolume={337},\r\nnumber={7},\r\npages={635-642},\r\ndoi={10.1016/S0008-6215(02)00027-7},\r\nnote={cited By 16},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036128984&doi=10.1016%2fS0008-6215%2802%2900027-7&partnerID=40&md5=dd8c17b8538ee682f3d3b6bbf0809956},\r\naffiliation={N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky av. 47, Moscow 119991, Russian Federation; Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biology Division, Gatchina, St. Petersburg 188350, Russian Federation},\r\nabstract={1-O-Acetyl-β-D-galactopyranose (AcGal), a new substrate for β-galactosidase, was synthesized in a stereoselective manner by the trichloroacetimidate procedure. Kinetic parameters (KM and kcat) for the hydrolysis of 1-O-acetyl-β-D-galactopyranose catalyzed by the β-D-galactosidase from Penicillium sp. were compared with similar characteristics for a number of natural and synthetic substrates. The value for kcat in the hydrolysis of AcGal was three orders of magnitude greater than for other known substrates. The β-galactosidase hydrolyzes AcGal with retention of anomeric configuration. The transglycosylation activity of the β-D-galactosidase in the reaction of AcGal and methyl β-D-galactopyranoside (1) as substrates was investigated by 1H NMR spectroscopy and HPLC techniques. The transglycosylation product using AcGal as a substrate was β-D-galactopyranosyl-(1→6)-1-O-acetyl-β-D-galactopyranose (with a yield of ∼70%). In the case of 1 as a substrate, the main transglycosylation product was methyl β-D-galactopyranosyl-(1→6)-β-D-galactopyranoside. Methyl β-D-galactopyranosyl-(1→3)-β-D-galactopyranoside was found to be minor product in the latter reaction. © 2002 Elsevier Science Ltd. All rights reserved.},\r\nauthor_keywords={β-D-Galactosidase;  1-O-Acetyl-β-D-galactopyranose;  Disaccharides;  Penicillium sp.;  Transglycosylation},\r\n}

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\n \n\n \n \n \n \n \n \n Purification, characterization, gene cloning and preliminary X-ray data of the exo-inulinase from Aspergillus awamori.\n \n \n \n \n\n\n \n Arand, M.; Golubev, A.; Neto, J.; Polikarpov, I.; Wattiez, R.; Korneeva, O.; Eneyskaya, E.; Kulminskaya, A.; Shabalin, K.; Shishliannikov, S.; Chepurnaya, O.; and Neustroev, K.\n\n\n \n\n\n\n Biochemical Journal, 362(1): 131-135. 2002.\n cited By 61\n\n\n\n
\n\n\n\n \n \n $\"Purification,$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Arand2002131,\r\nauthor={Arand, M. and Golubev, A.M. and Neto, J.R.B. and Polikarpov, I. and Wattiez, R. and Korneeva, O.S. and Eneyskaya, E.V. and Kulminskaya, A.A. and Shabalin, K.A. and Shishliannikov, S.M. and Chepurnaya, O.V. and Neustroev, K.N.},\r\ntitle={Purification, characterization, gene cloning and preliminary X-ray data of the exo-inulinase from Aspergillus awamori},\r\njournal={Biochemical Journal},\r\nyear={2002},\r\nvolume={362},\r\nnumber={1},\r\npages={131-135},\r\ndoi={10.1042/0264-6021:3620131},\r\nnote={cited By 61},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037084266&doi=10.1042%2f0264-6021%3a3620131&partnerID=40&md5=2fed1a311246671244653a7304594bc8},\r\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Gatchina, St. Petersburg 188350, Russian Federation},\r\nabstract={Extracellular exo-inulinase has been isolated from a solid-phase culture of the filamentous fungus Aspergillus awamori var. 2250. The apparent molecular mass of the monomer enzyme was 69±1 kDa, with a pI of 4.4 and a pH optimum of 4.5. The enzyme hydrolysed the β-(2 → 1)-fructan (inulin) and β-(2 → 6)-fructan (levan) via exo-cleavage, releasing fructose. The values for the Michaelis constants Km and Vmax in the hydrolysis of inulin were 0.003±0.0001 mM and 175±5 μmol·min-1·mg-1. The same parameters in the hydrolysis of levan were 2.08± 0.04 mg/ml and 1.2±0.02 μmol/min per mg, respectively. The gene and cDNA encoding the A. awamori exo-inulinase were cloned and sequenced. The amino acid sequence indicated that the protein belongs to glycoside hydrolase family 32. A surprisingly high similarity was found to fructosyltransferase from Aspergillus foetidus (90.7% on the level of the amino acid sequence), despite the fact that the latter enzyme is unable to hydrolyse inulin and levan. Crystals of the native exo-inulinase were obtained and found to belong to the orthorhombic space group P212121 with cell parameters a = 64.726 Å (1Å = 0.1 nm), b = 82.041 Å and c = 136.075 Å. Crystals diffracted beyond 1.54 Å, and useful X-ray data were collected to a resolution of 1.73 Å.},\r\nauthor_keywords={Family 32;  Inulin degradation;  Levan},\r\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Russian Academy of Science, Gatchina, St. Petersburg 188350, Russian Federation; email: neustk@omrb.pnpi.spb.ru},\r\nissn={02646021},\r\ncoden={BIJOA},\r\npubmed_id={11829749},\r\nlanguage={English},\r\nabbrev_source_title={Biochem. J.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Enzymatic properties of α-galactosidase from Trichoderma reesei in the hydrolysis of galactooligosaccharides.\n \n \n \n \n\n\n \n Shabalin, K.; Kulminskaya, A.; Savel'ev, A.; Shishlyannikov, S.; and Neustroev, K.\n\n\n \n\n\n\n Enzyme and Microbial Technology, 30(2): 231-239. 2002.\n cited By 26\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Shabalin2002231,\r\nauthor={Shabalin, K.A. and Kulminskaya, A.A. and Savel'ev, A.N. and Shishlyannikov, S.M. and Neustroev, K.N.},\r\ntitle={Enzymatic properties of α-galactosidase from Trichoderma reesei in the hydrolysis of galactooligosaccharides},\r\njournal={Enzyme and Microbial Technology},\r\nyear={2002},\r\nvolume={30},\r\nnumber={2},\r\npages={231-239},\r\ndoi={10.1016/S0141-0229(01)00482-3},\r\nnote={cited By 26},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037074922&doi=10.1016%2fS0141-0229%2801%2900482-3&partnerID=40&md5=6f935b6c0dccc7b33e46c5b4635baff4},\r\naffiliation={Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Gatchina, St.Petersburg, 188300, Russian Federation; St. Petersburg Technical University, Department of Biophysics, 29 Polytechnicheskaya str., St. Petersburg, 195251, Russian Federation},\r\nabstract={Enzymatic properties of the α-galactosidase (α-galactoside galactohydrolase, EC 3.2.1.22) from Trichoderma reesei in the hydrolysis of natural galactooligosaccharides and α-O-methyl D-galactopyranoside have been investigated in a wide range of substrate concentrations. The hydrolyses of α-O-methyl D-galactopyranoside and melibiose were inhibited by substrate at concentrations higher than 100 mM while in the hydrolysis of raffinose and stachyose such an effect was not observed. It was shown by 1H and 13C NMR spectroscopy and HPLC techniques that inhibition by the excess of α-O-methyl D-galactopyranoside or melibiose strongly correlated with formation of transglycosylation products. The product of autocondensation reaction with α-O-methyl D-galactopyranoside as substrate was found to be α-O-methyl galactopyranosyl-1,6-D-galactopyranoside. The stereochemical course of stachyose hydrolysis has been determined. The enzyme catalyses the hydrolysis with retention of anomeric configuration and is assumed to operate via a double displacement mechanism. Simultaneous hydrolysis of stachyose and raffinose effected by the α-D-galactosidase was studied by direct 1H NMR measurements. Cleavage of the terminal galactose residue of stachyose was found to be the rate-limiting step. Formation constants of enzyme-substrate complex for stachyose and raffinose were calculated. The suggested model can be used for simulating the two-substrate system and predicting the extent of stachyose hydrolysis. © 2002 Elsevier Science Inc. All rights reserved.},\r\nauthor_keywords={α-galactoside;  Stachyose;  Transglycosylation;  Trichoderma reesei},\r\n}

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\n \n 2001\n \n \n (6)\n \n \n

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\n \n\n \n \n \n \n \n \n Isolation, enzymatic properties, and mode of action of an exo-1,3-β-glucanase from Trichoderma viride.\n \n \n \n \n\n\n \n Kulminskaya, A.; Thomsen, K.; Shabalin, K.; Sidorenko, I.; Eneyskaya, E.; Savel'Ev, A.; and Neustroev, K.\n\n\n \n\n\n\n European Journal of Biochemistry, 268(23): 6123-6131. 2001.\n cited By 31\n\n\n\n
\n\n\n\n \n \n $\"Isolation,$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Kulminskaya20016123,\r\nauthor={Kulminskaya, A.A. and Thomsen, K.K. and Shabalin, K.A. and Sidorenko, I.A. and Eneyskaya, E.V. and Savel'Ev, A.N. and Neustroev, K.N.},\r\ntitle={Isolation, enzymatic properties, and mode of action of an exo-1,3-β-glucanase from Trichoderma viride},\r\njournal={European Journal of Biochemistry},\r\nyear={2001},\r\nvolume={268},\r\nnumber={23},\r\npages={6123-6131},\r\ndoi={10.1046/j.0014-2956.2001.02558.x},\r\nnote={cited By 31},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035206899&doi=10.1046%2fj.0014-2956.2001.02558.x&partnerID=40&md5=63957ac4cbf45c675d617c1643b28948},\r\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Russian Federation; Carlsberg Laboratory, Department of Physiology, Copenhagen, Denmark; St Petersburg Technical University, Biophysics Department, Russian Federation; Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, Russian Federation},\r\nabstract={An exo-1,3-β-glucanase has been isolated from cultural filtrate of Trichoderma viride AZ36. The N-terminal sequence of the purified enzyme (m = 61 ± 1 kDa) showed no significant homology to other known glucanases. The 1,3-β-glucanase displayed high activity against laminarins, curdlan, and 1,3-β-oligoglucosides, but acted slowly on 1,3-1,4-β-oligoglucosides. No significant activity was detected against high molecular mass 1,3-1,4-β-glucans. The enzyme carried out hydrolysis with inversion of the anomeric configuration. Whereas only glucose was released from the nonreducing terminus during hydrolysis of 1,3-β-oligoglucosides, transient accumulation of gentiobiose was observed during hydrolysis of laminarins. The gentiobiose was subsequently degraded to glucose. The Michaelis constants Km and Vmax have been determined for the hydrolysis of 1,3-β-oligoglucosides with degrees of polymerization ranging from 2 to 6. Based on these data, binding affinities for subsites were calculated. Substrate binding site contained at least five binding sites for sugar residues.},\r\nauthor_keywords={3-β-glucanase;  Anomerity of hydrolysis;  Exo-1;  Trichoderma viride},\r\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Gatchina, St Petersburg 188350, Russian Federation; email: neustk@omrb.pnpi.spb.ru},\r\nissn={00142956},\r\ncoden={EJBCA},\r\npubmed_id={11733006},\r\nlanguage={English},\r\nabbrev_source_title={Eur. J. Biochem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Atomic-scale imaging of insulating diamond through resonant electron injection.\n \n \n \n \n\n\n \n Bobrov, K.; Mayne, A.; and Dujardin, G.\n\n\n \n\n\n\n Nature, 413(6856): 616-619. 2001.\n cited By 82\n\n\n\n
\n\n\n\n \n \n $\"Atomic-scale$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Bobrov2001616,\r\nauthor={Bobrov, K. and Mayne, A.J. and Dujardin, G.},\r\ntitle={Atomic-scale imaging of insulating diamond through resonant electron injection},\r\njournal={Nature},\r\nyear={2001},\r\nvolume={413},\r\nnumber={6856},\r\npages={616-619},\r\ndoi={10.1038/35098053},\r\nnote={cited By 82},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035846182&doi=10.1038%2f35098053&partnerID=40&md5=8c558c3b434a5217449836cb3672e989},\r\naffiliation={Lab. de Photophysique Moleculaire, Bât. 210, Université Paris-Sud, 91405 Orsay, France},\r\nabstract={The electronic properties of insulators such as diamond are of interest not only for their passive dielectric capabilities for use in electronic devices, but also for their strong electron confinement on atomic scales. However, the inherent lack of electrical conductivity in insulators usually prevents the investigation of their surfaces by atomic-scale characterization techniques such as scanning tunnelling microscopy (STM). And although atomic force microscopy could in principle be used, imaging diamond surfaces has not yet been possible. Here, we demonstrate that STM can be used in an unconventional resonant electron injection mode to image insulating diamond surfaces and to probe their electronic properties at the atomic scale. Our results reveal striking electronic features in high-purity diamond single crystals, such as the existence of one-dimensional fully delocalized electronic states and a very long diffusion length for conduction-band electrons. We expect that our method can be applied to investigate the electronic properties of other insulating materials and so help in the design of atomic-scale electronic devices.},\r\ncorrespondence_address1={Dujardin, G.; Lab. de Photophysique Moleculaire, Bât. 210, Université Paris-Sud, 91405 Orsay, France; email: gerald.dujardin@ppm.u-psud.fr},\r\nissn={00280836},\r\ncoden={NATUA},\r\npubmed_id={11595944},\r\nlanguage={English},\r\nabbrev_source_title={Nature},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n An α-L-fucosidase from Thermus sp. with unusually broad specificity.\n \n \n \n \n\n\n \n Eneyskaya, E.; Kulminskaya, A.; Kalkkinen, N.; Nifantiev, N.; Arbatskii, N.; Saenko, A.; Chepurnaya, O.; Arutyunyan, A.; Shabalin, K.; and Neustroev, K.\n\n\n \n\n\n\n Glycoconjugate Journal, 18(10): 827-834. 2001.\n cited By 23\n\n\n\n
\n\n\n\n \n \n $\"An$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Eneyskaya2001827,\r\nauthor={Eneyskaya, E.V. and Kulminskaya, A.A. and Kalkkinen, N. and Nifantiev, N.E. and Arbatskii, N.P. and Saenko, A.I. and Chepurnaya, O.V. and Arutyunyan, A.V. and Shabalin, K.A. and Neustroev, K.N.},\r\ntitle={An α-L-fucosidase from Thermus sp. with unusually broad specificity},\r\njournal={Glycoconjugate Journal},\r\nyear={2001},\r\nvolume={18},\r\nnumber={10},\r\npages={827-834},\r\ndoi={10.1023/A:1021163720282},\r\nnote={cited By 23},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035497396&doi=10.1023%2fA%3a1021163720282&partnerID=40&md5=49a773d20350e43268d93da7f0b5b19d},\r\naffiliation={Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Russian Academy of Science, Gatchina, Orlova roscha, 188300, Russian Federation; Protein Chemistry Laboratory, Institute of Biotechnology, University of Helsinki, Finland; N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Science, Moscow, Russian Federation},\r\nabstract={An α-L-fucosidase (E.C. 3.2.1.51) exhibiting a wide aglycon specificity expressed in ability of cleaving α1 → 6-, α1 →3-, α1 → 4-, and α1 → 2-O-fucosyl bonds in fucosylated oligosaccharides, has been isolated from culture filtrate of Thermus sp. strain Y5. The α-L-fucosidase hydrolyzes p-nitrophenyl α-L-fucopyranoside with Vmax of 12.0 ± 0.1 μM/min/mg and Km= 0.20 ± 0.05 mM and is able to cleave off about 90% of total L-fucose from pronase-treated fractions of fucosyl-containing glycoproteins and about 30% from the native glycoproteins. The purified enzyme is a tetramer with a molecular mass of 240 ± 10 kDa consisting of four identical subunits with a molecular mass of 61.0 ± 0.5 kDa. The N-terminal sequence showed homology to some α-L-fucosidases from microbial and plant sources. Hydrolysis of p-nitrophenyl α-L-fucopyranoside occurs with retention of the anomeric configuration. Transglycosylating activity of the α-L-fucosidase was demonstrated in reactions with such acceptors as alcohols, N-acetylglucosamine and N-acetylgalactosamine while no transglycosylation products were observed in the reaction with p-nitrophenyl α-L-fucopyranoside. The enzyme can be classified in glycosyl hydrolase family 29.},\r\nauthor_keywords={Fucosyl-containing oligosaccharides;  Fucosylated glycoproteins;  α-L-fucosidase},\r\n}

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\n \n\n \n \n \n \n \n \n Acylation of amino acids with furancarboxylic acid chlorides.\n \n \n \n \n\n\n \n Lapina, I.; and Pevzner, L.\n\n\n \n\n\n\n Russian Journal of General Chemistry, 71(9): 1479-1483. 2001.\n cited By 3\n\n\n\n
\n\n\n\n \n \n $\"Acylation$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Lapina20011479,\r\nauthor={Lapina, I.M. and Pevzner, L.M.},\r\ntitle={Acylation of amino acids with furancarboxylic acid chlorides},\r\njournal={Russian Journal of General Chemistry},\r\nyear={2001},\r\nvolume={71},\r\nnumber={9},\r\npages={1479-1483},\r\ndoi={10.1023/A:1013926624228},\r\nnote={cited By 3},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035437963&doi=10.1023%2fA%3a1013926624228&partnerID=40&md5=d4ae43768b9d890afec5844ea6c91f38},\r\naffiliation={St. Petersburg Inst. of Technology, St. Petersburg, Russian Federation},\r\nabstract={Acylation of aromatic amino acids with furancarboxylic acid chlorides effectively proceeds in water-acetone medium at pH 8-9. Aliphatic amino acids are acylated at higher pH values, but under these conditions hydrolysis of acid chlorides becomes the main process. Acylation of chlorohydrates of methyl esters of aliphatic amino acids proceeds smoothly in chloroform in the presence of triethylamine. Alkaline hydrolysis of obtained products leads to N-acylated amino acids containing furan heteroring in the acyl radical.},\r\ncorrespondence_address1={Lapina, I.M.; St. Petersburg Inst. of Technology, St. Petersburg, Russian Federation},\r\nissn={10703632},\r\nlanguage={English},\r\nabbrev_source_title={Russ. J. Gen. Chem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Electronic structure of the hydrogenated diamond C(1 0 0)-(2 × 1):H surface.\n \n \n \n \n\n\n \n Bobrov, K.; Comtet, G.; Dujardin, G.; and Hellner, L.\n\n\n \n\n\n\n Surface Science, 482-485(PART 1): 437-441. 2001.\n cited By 9\n\n\n\n
\n\n\n\n \n \n $\"Electronic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Bobrov2001437,\r\nauthor={Bobrov, K. and Comtet, G. and Dujardin, G. and Hellner, L.},\r\ntitle={Electronic structure of the hydrogenated diamond C(1 0 0)-(2 × 1):H surface},\r\njournal={Surface Science},\r\nyear={2001},\r\nvolume={482-485},\r\nnumber={PART 1},\r\npages={437-441},\r\ndoi={10.1016/S0039-6028(01)00760-9},\r\nnote={cited By 9},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-18244423508&doi=10.1016%2fS0039-6028%2801%2900760-9&partnerID=40&md5=85e89329c70ef10cab5f9d12686b214f},\r\naffiliation={Laboratoire De Photophysique Moléculaire, Bâtiment 210, Université Paris-Sud, 91405 Orsay Cedex, France; Laboratoire Pour l'Utilisation Du Rayonnement Electromagnétique (LURE), Bâtiment 209D, Université Paris-Sud, 91405 Orsay Cedex, France},\r\nabstract={For the first time hydrogen induced surface states were experimentally observed on the hydrogenated diamond C(1 0 0)-(2 × 1):H surface. The photoemission spectra of the clean, ex situ and in situ hydrogenated diamond (1 0 0) surface were recorded at grazing incident angles in order to improve the surface sensitivity. The careful analysis of the photoemission spectra, recorded at different photon energies, indicates the presence of the hydrogen induced states in the valence band. The photoemission spectra, measured at different incident angles, suggest the surface character of the hydrogen induced states. These surface states, located at 8.8, 11.3-11.5 and 16.9 eV, displayed a slight dispersion with the photon energy and were interpreted as C-H surface states of the C(1 0 0)-(2 × 1):H surface. © 2001 Elsevier Science B.V.},\r\nauthor_keywords={Chemisorption;  Diamond;  Hydrogen atom;  Photoelectron spectroscopy},\r\ncorrespondence_address1={Bobrov, K.; Lab. de Photophysique Moleculaire, Bâtiment 210, Université Paris-Sud, 91405 Orsay Cedex, France},\r\nissn={00396028},\r\ncoden={SUSCA},\r\nlanguage={English},\r\nabbrev_source_title={Surf Sci},\r\ndocument_type={Conference Paper},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Electronic structure of partially hydrogenated Si(100)-(2 × 1) surfaces prepared by thermal and nonthermal desorption.\n \n \n \n \n\n\n \n Bobrov, K.; Comtet, G.; Dujardin, G.; and Hellner, L.\n\n\n \n\n\n\n Physical Review Letters, 86(12): 2633-2636. 2001.\n cited By 26\n\n\n\n
\n\n\n\n \n \n $\"Electronic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Bobrov20012633,\r\nauthor={Bobrov, K. and Comtet, G. and Dujardin, G. and Hellner, L.},\r\ntitle={Electronic structure of partially hydrogenated Si(100)-(2 × 1) surfaces prepared by thermal and nonthermal desorption},\r\njournal={Physical Review Letters},\r\nyear={2001},\r\nvolume={86},\r\nnumber={12},\r\npages={2633-2636},\r\ndoi={10.1103/PhysRevLett.86.2633},\r\nnote={cited By 26},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035911628&doi=10.1103%2fPhysRevLett.86.2633&partnerID=40&md5=bfa5306c2d9d5c1b97b89cb144d79701},\r\naffiliation={Laboratoire Pour l'Utilisation du Rayonnement Electromagnétique (LURE), Bâtiment 209D, Université Paris-Sud, 91405 Orsay Cedex, France; Laboratoire de Photophysique Moléculaire, Bâtiment 210, Université Paris-Sud, 91405 Orsay Cedex, France},\r\nabstract={Various types of partially hydrogenated Si(100)-(2×1) surfaces were prepared by thermal annealing and nonthermal photon-stimulated desorption. As a result, specific surface states with binding energies of 1.0 and 0.7 eV corresponding to isolated Si dimers and single Si dangling bonds were found. The validity of the whole procedure was inferred by comparing the experimental and statistically calculated dimer distributions as a function of the total hydrogen coverage.},\r\ncorrespondence_address1={Bobrov, K.; Lab. de Photophysique Moleculaire, Universite Paris-Sud, 91405 Orsay Cedex, France},\r\nissn={00319007},\r\ncoden={PRLTA},\r\nlanguage={English},\r\nabbrev_source_title={Phys Rev Lett},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2000\n \n \n (3)\n \n \n

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\n \n\n \n \n \n \n \n \n Purification, crystallization and preliminary diffraction study of β-galactosidase from Penicillium sp.\n \n \n \n \n\n\n \n Neustroev, K.; De Sousa, E.; Golubev, A.; Brandao Neto, J.; Eneyskaya, E.; Kulminskaya, A.; and Polikarpov, I.\n\n\n \n\n\n\n Acta Crystallographica Section D: Biological Crystallography, 56(11): 1508-1509. 2000.\n cited By 4\n\n\n\n
\n\n\n\n \n \n $\"Purification,$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Neustroev20001508,\r\nauthor={Neustroev, K.N. and De Sousa, E.A. and Golubev, A.M. and Brandao Neto, J.R. and Eneyskaya, E.V. and Kulminskaya, A.A. and Polikarpov, I.},\r\ntitle={Purification, crystallization and preliminary diffraction study of β-galactosidase from Penicillium sp.},\r\njournal={Acta Crystallographica Section D: Biological Crystallography},\r\nyear={2000},\r\nvolume={56},\r\nnumber={11},\r\npages={1508-1509},\r\ndoi={10.1107/S0907444900011756},\r\nnote={cited By 4},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033731794&doi=10.1107%2fS0907444900011756&partnerID=40&md5=30d861582afdd34d206fa1f6c68ec7bf},\r\naffiliation={LNLS, Caixa Postal 6192, CEP 13083-970, Campinas, Brazil},\r\nabstract={Crystals of an extracellular β-galactosidase from Penicillium sp. (MW = 120 ± 5 kDa) have been obtained from a sodium phosphate buffer using PEG as precipitant. The crystals belong to the tetragonal space group P41 or P43, with unit-cell parameters a = b = 110.82, c = 161.28 Å, and diffract to 1.85 Å resolution at a synchrotron source.},\r\ncorrespondence_address1={Polikarpov, I.; LNLS, Caixa Postal 6192, CEP 13083-970, Campinas, Brazil; email: igor@lnls.br},\r\nissn={09074449},\r\ncoden={ABCRE},\r\npubmed_id={11053867},\r\nlanguage={English},\r\nabbrev_source_title={Acta Crystallogr. Sect. D Biol. Crystallogr.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Purification, crystallization and preliminary X-ray study of β-xylosidase from Trichoderma reesei.\n \n \n \n \n\n\n \n Golubev, A.; Brand̃o Neto, J.; Eneyskaya, E.; Kulminskaya, A.; Kerzhner, M.; Neustroev, K.; and Polikarpov, I.\n\n\n \n\n\n\n Acta Crystallographica Section D: Biological Crystallography, 56(8): 1058-1060. 2000.\n cited By 12\n\n\n\n
\n\n\n\n \n \n $\"Purification,$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Golubev20001058,\r\nauthor={Golubev, A.M. and Brand̃o Neto, J.R. and Eneyskaya, E.V. and Kulminskaya, A.V. and Kerzhner, M.A. and Neustroev, K.N. and Polikarpov, I.},\r\ntitle={Purification, crystallization and preliminary X-ray study of β-xylosidase from Trichoderma reesei},\r\njournal={Acta Crystallographica Section D: Biological Crystallography},\r\nyear={2000},\r\nvolume={56},\r\nnumber={8},\r\npages={1058-1060},\r\ndoi={10.1107/S0907444900008210},\r\nnote={cited By 12},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033883952&doi=10.1107%2fS0907444900008210&partnerID=40&md5=a9629cabc1fa2164a490abf43f832f39},\r\naffiliation={Petersburg Nuclear Physics Institute, Gatchina, St Petersburg 188350, Russian Federation; National Synchrotron Light Laboratory, CP 6192, CEP 13083-970, Campinas, SP, Brazil},\r\nabstract={An extracellular multifunctional β-xylosidase was purified from a culture of the fungus Trichoderma reesei. The active 95 ± 5 kDa enzyme has been crystallized from sodium acetate buffer using PEG as a precipitant. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 67.75, b = 98.54, c 227.25 Å, and diffract beyond 2.7 Å resolution. X-ray data were collected from frozen crystals on a synchrotron source.},\r\ncorrespondence_address1={Polikarpov, I.; National Synchrotron Light Lab., CP 6192, CEP 13083-970 Campinas, SP, Brazil; email: igor@lnls.br},\r\nissn={09074449},\r\ncoden={ABCRE},\r\npubmed_id={10944353},\r\nlanguage={English},\r\nabbrev_source_title={Acta Crystallogr. Sect. D Biol. Crystallogr.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Crystallization and preliminary X-ray study of β-Mannosidase from Trichoderma reesei.\n \n \n \n \n\n\n \n Aparicio, R.; Eneiskaya, E.; Kulminskaya, A.; Savel'ev, A.; Golubev, A.; Neustroev, K.; Kobarg, J.; and Polikarpov, I.\n\n\n \n\n\n\n Acta Crystallographica Section D: Biological Crystallography, 56(3): 342-343. 2000.\n cited By 1\n\n\n\n
\n\n\n\n \n \n $\"Crystallization$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Aparicio2000342,\r\nauthor={Aparicio, R. and Eneiskaya, E.V. and Kulminskaya, A.A. and Savel'ev, A.N. and Golubev, A.M. and Neustroev, K.N. and Kobarg, J. and Polikarpov, I.},\r\ntitle={Crystallization and preliminary X-ray study of β-Mannosidase from Trichoderma reesei},\r\njournal={Acta Crystallographica Section D: Biological Crystallography},\r\nyear={2000},\r\nvolume={56},\r\nnumber={3},\r\npages={342-343},\r\ndoi={10.1107/S0907444999016625},\r\nnote={cited By 1},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034096065&doi=10.1107%2fS0907444999016625&partnerID=40&md5=5575fe505e58c1a9d3ce0f4492a33d61},\r\naffiliation={Natl. Synchrotron Light Laboratory, LNLS, Caixa Postal 6192, CEP 13083-970, Campinas, SP, Brazil; Gleb Wataghin Physics Institute, State University at Campinas, UNICAMP, Caixa Postal 6165, CEP 13083-970, Campinas, SP, Brazil; Petersburg Nuclear Physics Institute, Gatchina, St Petersburg, 188350, Russian Federation; St. Petersburg Technical University, 29 Politechnicheskaya Str., St Petersburg, 195251, Russian Federation},\r\nabstract={β-Mannosidase from Trichoderma reesei, a 105 kDa glycoprotein, has been crystallized. The crystals belong to the space group P41212 or P43212, with unit-cell dimensions a = b = 165.86, c = 122.46 Å, and diffract beyond 2.75 Å resolution. X-ray diffraction data were collected from a frozen crystal on a synchrotron X-ray source.},\r\ncorrespondence_address1={Polikarpov, I.; Natl. Synchrotron Light Laboratory, LNLS, Caixa Postal 6192, CEP 13083-970, Campinas, SP, Brazil; email: igor@lnls.br},\r\nissn={09074449},\r\ncoden={ABCRE},\r\npubmed_id={10713521},\r\nlanguage={English},\r\nabbrev_source_title={Acta Crystallogr. Sect. D Biol. Crystallogr.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

\n

\n\n\n\n\n\n

\n

\n \n 1999\n \n \n (2)\n \n \n

\n

\n \n \n

\n \n\n \n \n \n \n \n \n Enzymatic activity and β-galactomannan binding property of β-mannosidase from Trichoderm reesei.\n \n \n \n \n\n\n \n Kulminskaya, A.; Eneiskaya, E.; Isaeva-Ivanova, L.; Savel'ev, A.; Sidorenko, I.; Shabalin, K.; Golubev, A.; and Neustroev, K.\n\n\n \n\n\n\n Enzyme and Microbial Technology, 25(3-5): 372-377. 1999.\n cited By 25\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Kulminskaya1999372,\r\nauthor={Kulminskaya, A.A. and Eneiskaya, E.V. and Isaeva-Ivanova, L.S. and Savel'ev, A.N. and Sidorenko, I.A. and Shabalin, K.A. and Golubev, A.M. and Neustroev, K.N.},\r\ntitle={Enzymatic activity and β-galactomannan binding property of β-mannosidase from Trichoderm reesei},\r\njournal={Enzyme and Microbial Technology},\r\nyear={1999},\r\nvolume={25},\r\nnumber={3-5},\r\npages={372-377},\r\ndoi={10.1016/S0141-0229(99)00056-3},\r\nnote={cited By 25},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033180029&doi=10.1016%2fS0141-0229%2899%2900056-3&partnerID=40&md5=d1b176ab95e86e5ecbe3e3c06443ae87},\r\naffiliation={Petersburg Nuclear Physics Institute, Molec. Radiat. Biophys. Div., G., St. Petersburg, 188350, Russian Federation; St. Petersburg Technical University, Biophys. Dept., 29 P., St. Petersburg, 195251, Russian Federation},\r\nabstract={An extracellular 105-kDa β-mannosidase (β-D-mannoside-mannohydrolase, E.C. 3.2.1.25) was purified to homogeneity from culture filtrate of Trichoderma reesei. Specific activity of the β-mannosidase toward p-nitrophenyl-β-D-mannopyranoside was 3.2 U/mg at the optimal pH 3.5 (K(m) = 0.12 mM, k(CAT) = 2.95 x 10-3 μmol min/μg. An additional β-galactomannan (GM) binding site of the enzyme was found on the basis of kinetic studies. The enzyme GM dissociation constant (K(D)) was 1.21 mg/ml. β-1,4-mannooligosaccharides inhibited the binding of the enzyme to galactomannan. The inhibition constant of the sorption decreased with increasing of the β-1,4-mannooligosaccharide length. Mannose, the competitive inhibitor of the β-mannosidase in hydrolysis of p-nitrophenyl-β-D-mannopyranoside, did not inhibit sorption of the enzyme on β-GM. Chitin, xylan, raw starch, and microcrystalline cellulose had no affinity to the β-mannosidase. The enzyme hydrolyzed β-1,4-mannooligosaccharides with the rate depending on the chain length and liberated mannose from soluble and insoluble fractions of β-GM from locust beans with initial rates of 0.3 and 0.05 μmol min/ml U, respectively. Copyright (C) 1999 Elsevier Science Inc.\r\nAn extracellular 105-kDa β-mannosidase (β-D-mannoside-mannohydrolase, E.C. 3.2.1.25) was purified to homogeneity from culture filtrate of Trichoderma reesei. Specific activity of the β-mannosidase toward p-nitrophenyl-β-D-mannopyranoside was 3.2 U/mg at the optimal pH 3.5 (Km = 0.12 mM, kCAT = 2.95 × 10-3 μmol min/μg. An additional β-galactomannan (GM) binding site of the enzyme was found on the basis of kinetic studies. The enzyme GM dissociation constant (KD) was 1.21 mg/ml. β-1,4-mannooligosaccharides inhibited the binding of the enzyme to galactomannan. The inhibition constant of the sorption decreased with increasing of the β-1,4-mannooligosaccharide length. Mannose, the competitive inhibitor of the β-mannosidase in hydrolysis of p-nitrophenyl-β-D-mannopyranoside, did not inhibit sorption of the enzyme on β-GM. Chitin, xylan, raw starch, and microcrystalline cellulose had no affinity to the β-mannosidase. The enzyme hydrolyzed β-1,4-mannooligosaccharides with the rate depending on the chain length and liberated mannose from soluble and insoluble fractions of β-GM from locust beans with initial rates of 0.3 and 0.05 μmol min/ml U, respectively.},\r\nauthor_keywords={β-Galactomannan binding site;  β-Mannosidase;  Trichoderma reesei},\r\n}

\n

\n\n\n

\n An extracellular 105-kDa β-mannosidase (β-D-mannoside-mannohydrolase, E.C. 3.2.1.25) was purified to homogeneity from culture filtrate of Trichoderma reesei. Specific activity of the β-mannosidase toward p-nitrophenyl-β-D-mannopyranoside was 3.2 U/mg at the optimal pH 3.5 (K(m) = 0.12 mM, k(CAT) = 2.95 x 10-3 μmol min/μg. An additional β-galactomannan (GM) binding site of the enzyme was found on the basis of kinetic studies. The enzyme GM dissociation constant (K(D)) was 1.21 mg/ml. β-1,4-mannooligosaccharides inhibited the binding of the enzyme to galactomannan. The inhibition constant of the sorption decreased with increasing of the β-1,4-mannooligosaccharide length. Mannose, the competitive inhibitor of the β-mannosidase in hydrolysis of p-nitrophenyl-β-D-mannopyranoside, did not inhibit sorption of the enzyme on β-GM. Chitin, xylan, raw starch, and microcrystalline cellulose had no affinity to the β-mannosidase. The enzyme hydrolyzed β-1,4-mannooligosaccharides with the rate depending on the chain length and liberated mannose from soluble and insoluble fractions of β-GM from locust beans with initial rates of 0.3 and 0.05 μmol min/ml U, respectively. Copyright (C) 1999 Elsevier Science Inc. An extracellular 105-kDa β-mannosidase (β-D-mannoside-mannohydrolase, E.C. 3.2.1.25) was purified to homogeneity from culture filtrate of Trichoderma reesei. Specific activity of the β-mannosidase toward p-nitrophenyl-β-D-mannopyranoside was 3.2 U/mg at the optimal pH 3.5 (Km = 0.12 mM, kCAT = 2.95 × 10-3 μmol min/μg. An additional β-galactomannan (GM) binding site of the enzyme was found on the basis of kinetic studies. The enzyme GM dissociation constant (KD) was 1.21 mg/ml. β-1,4-mannooligosaccharides inhibited the binding of the enzyme to galactomannan. The inhibition constant of the sorption decreased with increasing of the β-1,4-mannooligosaccharide length. Mannose, the competitive inhibitor of the β-mannosidase in hydrolysis of p-nitrophenyl-β-D-mannopyranoside, did not inhibit sorption of the enzyme on β-GM. Chitin, xylan, raw starch, and microcrystalline cellulose had no affinity to the β-mannosidase. The enzyme hydrolyzed β-1,4-mannooligosaccharides with the rate depending on the chain length and liberated mannose from soluble and insoluble fractions of β-GM from locust beans with initial rates of 0.3 and 0.05 μmol min/ml U, respectively.\n

\n\n\n

\n \n\n \n \n \n \n \n \n Acid protease from Trichoderma reesei: Limited proteolysis of fungal carbohydrases.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Applied Microbiology and Biotechnology, 52(2): 226-231. 1999.\n cited By 28\n\n\n\n
\n\n\n\n \n \n $\"Acid$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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\n\n\n\n\n\n

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\n \n 1998\n \n \n (3)\n \n \n

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\n \n \n

\n \n\n \n \n \n \n \n \n Multiple attack of action of α-galactosidase from Trichoderma Reesei.\n \n \n \n \n\n\n \n Shabalin, K.; Eneyskaya, E.; Kulminskaya, A.; Savel'ev, A.; and Neustroev, K.\n\n\n \n\n\n\n Protein and Peptide Letters, 5(6): 341-348. 1998.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Multiple$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Shabalin1998341,\r\nauthor={Shabalin, K.A. and Eneyskaya, E.V. and Kulminskaya, A.A. and Savel'ev, A.N. and Neustroev, K.N.},\r\ntitle={Multiple attack of action of α-galactosidase from Trichoderma Reesei},\r\njournal={Protein and Peptide Letters},\r\nyear={1998},\r\nvolume={5},\r\nnumber={6},\r\npages={341-348},\r\nnote={cited By 0},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-17344373675&partnerID=40&md5=aef664cfd348ed524d61bc11e6ca9c7a},\r\naffiliation={Petersburg Nuclear Physics Institute, Molec. Radiat. Biophys. Div. G., St.-Petersburg, 188350, Russian Federation; St.Petersburg Technical University, Biophysics Department, 29 Polytechnicheskaya str, St.Petersburg, 195251, Russian Federation},\r\nabstract={The presence of multiple attack of action of α-galactosidase from Trichoderma reesei was demonstrated in hydrolysis of p-nitrophenyl-6-O-α-galactopyranosyl-O-gaIactopyranoside using NMR, GLC-MS and absorption spectra in the visible region. The degree of multiplicity of attack in this reaction appeared to be 2.1 and depended on pH. Studying some other glycosidases revealed the absence of the multiplicity in the hydrolysis of p-nitrophenyl oligosaccharides.},\r\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Molec. Radiat. Biophys. Div. G., St.-Petersburg, 188350, Russian Federation},\r\nissn={09298665},\r\ncoden={PPELE},\r\nlanguage={English},\r\nabbrev_source_title={Protein Pept. Lett.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Enzymatic properties of α-mannosidase from Trichoderma reesel.\n \n \n \n \n\n\n \n Kulminskaya, A.; Eneyskaya, E.; Isaeva-Ivanova, L.; Shabalin, K.; Savel'ev, A.; Backinowsky, L.; Abronina, P.; and Neustroev, K.\n\n\n \n\n\n\n Protein and Peptide Letters, 5(3): 163-170. 1998.\n cited By 3\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Kulminskaya1998163,\r\nauthor={Kulminskaya, A.A. and Eneyskaya, E.V. and Isaeva-Ivanova, L.S. and Shabalin, K.A. and Savel'ev, A.N. and Backinowsky, L.V. and Abronina, P.I. and Neustroev, K.N.},\r\ntitle={Enzymatic properties of α-mannosidase from Trichoderma reesel},\r\njournal={Protein and Peptide Letters},\r\nyear={1998},\r\nvolume={5},\r\nnumber={3},\r\npages={163-170},\r\nnote={cited By 3},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344245335&partnerID=40&md5=be4614ab5a300a4c1838611c326677b2},\r\naffiliation={Petersburg Nuclear Physics Institute, Molecular Division, St.Petersburg 188350, Russian Federation; St.Petersburg Technical University, Biophysics Department, 29 Polytechnicheskaya str., St.Petersburg 195251, Russian Federation; N.D.Zelinsky Inst. of Organ. Chem., 47 Leninsky av., 117913 Moscow, Russian Federation},\r\nabstract={Kinetic parameters of reactions catalyzed by α-mannosidase from Trichoderma reesei were determined using various mannooligosacharides as substrates. These reactions were found to go with retention of anomeric configuration. Kinetic experiments revealed the existence of a functionally significant SH-group in the active site of the enzyme. A transglycosylating activity toward p-nitrophenyl-α-D-mannopyranoside was found and single product of this reaction was identified as p-nitrophenyl-α-D-α1→2 mannopyranosyl-α-D-mannopyranose.},\r\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Molecular Division, St.Petersburg 188350, Russian Federation},\r\nissn={09298665},\r\ncoden={PPELE},\r\nlanguage={English},\r\nabbrev_source_title={Protein Pept. Lett.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

\n

\n\n\n\n\n\n

\n\n\n

\n \n\n \n \n \n \n \n \n α-mannosidase from Trichoderma reesei participates in the postsecretory deglycosylation of glycoproteins.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Biochemical and Biophysical Research Communications, 245(1): 43-49. 1998.\n cited By 14\n\n\n\n
\n\n\n\n \n \n $\"α-mannosidase$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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\n\n\n\n\n\n

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\n \n 1997\n \n \n (3)\n \n \n

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\n \n\n \n \n \n \n \n \n Sh-group in the active site of α-galactosidase from Trichoderma reesei.\n \n \n \n \n\n\n \n Eneyskaya, E.; Protasenya, S.; Kachurin, A.; Savel'ev, A.; and Neustroev, K.\n\n\n \n\n\n\n Protein and Peptide Letters, 4(3): 173-180. 1997.\n cited By 3\n\n\n\n
\n\n\n\n \n \n $\"Sh-group$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Eneyskaya1997173,\r\nauthor={Eneyskaya, E.V. and Protasenya, S.V. and Kachurin, A.M. and Savel'ev, A.N. and Neustroev, K.N.},\r\ntitle={Sh-group in the active site of α-galactosidase from Trichoderma reesei},\r\njournal={Protein and Peptide Letters},\r\nyear={1997},\r\nvolume={4},\r\nnumber={3},\r\npages={173-180},\r\nnote={cited By 3},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-2042484896&partnerID=40&md5=6a5132e7dc4d80d9494a48ce8297f9b2},\r\naffiliation={Petersburg Nuclear Physics Institute, Molec./Radiat. Biophysics Division, Gatchina, St.Petersburg 188350, Russian Federation; St.Petersburg Technical University, Biophysics Department, 29 Polytechnicheskaya str., St.Petersburg, 195251, Russian Federation},\r\nabstract={Modifications of an SH-group in active site of α-galactosidase from T. reesei by PHMB and Hg2+ inactivate the enzyme while following treatment with thiols activity is recovered. Galactose and substrates delay such recovery. This effect was utilized to compare affinity of substrates and galactose to native and inactive forms of the enzyme. It was concluded that the SH-group is important for binding of substrates in the active site.},\r\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Molec./Radiat. Biophysics Division, Gatchina, St.Petersburg 188350, Russian Federation},\r\nissn={09298665},\r\ncoden={PPELE},\r\nlanguage={English},\r\nabbrev_source_title={Protein Pept. Lett.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

\n

\n\n\n\n\n\n

\n\n\n

\n \n\n \n \n \n \n \n \n Transglycosylation activity of α-D-galactosidase from Trichoderma reesei. An investigation of the active site.\n \n \n \n \n\n\n \n Eneyskaya, E.; Golubev, A.; Kachurin, A.; Savel'ev, A.; and Neustroev, K.\n\n\n \n\n\n\n Carbohydrate Research, 305(1): 83-91. 1997.\n cited By 37\n\n\n\n
\n\n\n\n \n \n $\"Transglycosylation$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Eneyskaya199783,\r\nauthor={Eneyskaya, E.V. and Golubev, A.M. and Kachurin, A.M. and Savel'ev, A.N. and Neustroev, K.N.},\r\ntitle={Transglycosylation activity of α-D-galactosidase from Trichoderma reesei. An investigation of the active site},\r\njournal={Carbohydrate Research},\r\nyear={1997},\r\nvolume={305},\r\nnumber={1},\r\npages={83-91},\r\ndoi={10.1016/S0008-6215(97)00229-2},\r\nnote={cited By 37},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031392412&doi=10.1016%2fS0008-6215%2897%2900229-2&partnerID=40&md5=972b4f2c3b2cbb903cf7bb6e410aa2de},\r\naffiliation={Molecular Division, Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg 188350, Russian Federation; Department of Biophysics, St. Petersburg Technical University, 29 Polytechnicheskaya str., St. Petersburg 195251, Russian Federation},\r\nabstract={The transglycosylation reaction catalyzed by α-D-galactosidase from the mycelial fungus Trichoderma reesei was studied using p-nitrophenyl α-D- galactopyranoside (PNPG). An aliphatic alcohol or the substrate itself can be an acceptor of the galactose residue in this reaction. The transglycosylation products were identified as alkyl galactosides in the case of alcohols or as galactobioside and galactotrioside in the case of PNPG. The transglycosylation rates follow a first-order equation with respect to the alcohol concentrations except for methanol. Affinities of some substrates were estimated from their K(i) values in the reaction of the enzyme with PNPG. Transglycosylation of the substrate suggests a model for the enzyme active center. It is proposed that the active center includes two galactose- binding sites and a hydrophobic site.},\r\nauthor_keywords={α-D-Galactosidase;  Alkyl galactosides;  P-Nitrophenyl α-D-galactopyranoside;  Transglycosylation products;  Trichoderma reesei},\r\n}

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\n \n\n \n \n \n \n \n \n The action of α-mannosidase from oerskovia sp. on the mannose-rich O-linked sugar chains of glycoproteins.\n \n \n \n \n\n\n \n Bagiyan, F.; Eneyskaya, E.; Kulminskaya, A.; Savel'ev, A.; Shabalin, K.; and Neustroev, K.\n\n\n \n\n\n\n European Journal of Biochemistry, 249(1): 286-292. 1997.\n cited By 10\n\n\n\n
\n\n\n\n \n \n $\"The$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Bagiyan1997286,\r\nauthor={Bagiyan, F.G. and Eneyskaya, E.V. and Kulminskaya, A.A. and Savel'ev, A.K. and Shabalin, K.A. and Neustroev, K.N.},\r\ntitle={The action of α-mannosidase from oerskovia sp. on the mannose-rich O-linked sugar chains of glycoproteins},\r\njournal={European Journal of Biochemistry},\r\nyear={1997},\r\nvolume={249},\r\nnumber={1},\r\npages={286-292},\r\ndoi={10.1111/j.1432-1033.1997.t01-1-00286.x},\r\nnote={cited By 10},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030792737&doi=10.1111%2fj.1432-1033.1997.t01-1-00286.x&partnerID=40&md5=90009634edc08ac6476a12f86b654690},\r\naffiliation={Petersburg Nuclear Physics Institute, Molec. and Radiat. Biophys. Division, St Petersburg, Russian Federation; St. Petersburg Technical University, Biophysics Department, St Petersburg, Russian Federation; Petersburg Nuclear Physics Institute, Gatchina, 188350 St Petersburg, Russian Federation},\r\nabstract={α-Mannosidase was isolated from the culture liquid of Oerskovia sp. The purified enzyme had a molecular mass of 480 kDa and comprises four identical subunits. The enzyme cleaves bonds in side chains of yeast mannan (K(m) = 0.08 mM, k(cat) = 1.02 μmol min -1 · mg -1 ) and reveals a low activity towards p-nitrophenyl α-D-mannopyranoside. The α-mannosidase is a Ca 2+ -dependent enzyme and is inhibited by EDTA. The enzyme possess no endo-mannosidase activity releasing only mannose in the reaction with the inversion of anomeric configuration and could be classified as exo-α-mannanase. The enzyme revealed a high deglycosylating activity towards the short mannose-rich O-linked carbohydrate chains of glycoproteins.},\r\nauthor_keywords={1-Deoxymannojirimycin;  Deglycosylation;  exo-α-mannanase;  Glucoamylase;  Yeast mannan},\r\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Gatchina, 188350 St Petersburg, Russian Federation; email: neustk@omrb.pnpi.spb.ru},\r\npublisher={Blackwell Publishing Ltd},\r\nissn={00142956},\r\ncoden={EJBCA},\r\npubmed_id={9363781},\r\nlanguage={English},\r\nabbrev_source_title={EUR. J. BIOCHEM.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 1996\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n Aldo-enol transition in periodate-oxidized dextrans.\n \n \n \n \n\n\n \n Drobchenko, S.; Isaeva-Ivanova, L.; Kleiner, A.; and Eneyskaya, E.\n\n\n \n\n\n\n Carbohydrate Research, 280(1): 171-176. 1996.\n cited By 10\n\n\n\n
\n\n\n\n \n \n $\"Aldo-enol$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Drobchenko1996171,\r\nauthor={Drobchenko, S.N. and Isaeva-Ivanova, L.S. and Kleiner, A.R. and Eneyskaya, E.V.},\r\ntitle={Aldo-enol transition in periodate-oxidized dextrans},\r\njournal={Carbohydrate Research},\r\nyear={1996},\r\nvolume={280},\r\nnumber={1},\r\npages={171-176},\r\ndoi={10.1016/0008-6215(95)00307-X},\r\nnote={cited By 10},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030045423&doi=10.1016%2f0008-6215%2895%2900307-X&partnerID=40&md5=4660198d25d0a0367db9269dfa604e2f},\r\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina, St. Petersburg, 188350, Russian Federation},\r\nauthor_keywords={aldo-enol transition;  dextran;  electrophoretic light scattering (ELS);  nuclear magnetic resonance (NMR);  periodate oxidation},\r\ncorrespondence_address1={Drobchenko, S.N.; Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina, St. Petersburg 188350, Russian Federation},\r\npublisher={Elsevier Ltd},\r\nissn={00086215},\r\ncoden={CRBRA},\r\nlanguage={English},\r\nabbrev_source_title={CARBOHYDR. RES.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n

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