@ARTICLE{Piens20073971,
author={Piens, K. and Henriksson, A.-M. and Gullfot, F. and Lopez, M. and Fauré, R. and Ibatullin, F.M. and Teeri, T.T. and Driguez, H. and Brumer, H.},
title={Glycosynthase activity of hybrid aspen xyloglucan endo-transglycosylase PttXET16-34 nucleophile mutants},
journal={Organic and Biomolecular Chemistry},
year={2007},
volume={5},
number={24},
pages={3971-3978},
doi={10.1039/b714570e},
note={cited By 20},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-36749095084&doi=10.1039%2fb714570e&partnerID=40&md5=2db6d80ea903a5f97675e2ec94acd10b},
affiliation={School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91, Stockholm, Sweden; Laboratory for Protein Biochemistry and Biomolecular Engineering, Department of Biochemistry, Physiology and Microbiology, Ghent University, K.L.-Ledeganckstraat 35, 9000, Ghent, Belgium; Centre de Recherches sur les Macromolécules Végé tales, (CERMAV-CNRS), B.P. 53, F-38041, Grenoble cedex 9, France; Joseph Fourier University, France; Institut de Chimie Moléculaire de Grenoble FR-CNRS 2607, France},
abstract={Glycosynthases are active-site mutants of glycoside hydrolases that catalyse glycosyl transfer using suitable activated donor substrates without competing product hydrolysis (S. M. Hancock, M. D. Vaughan and S. G. Withers, Curr. Opin. Chem. Biol., 2006, 10, 509-519). Site-directed mutagenesis of the catalytic nucleophile, Glu-85, of a Populus tremula x tremuloides xyloglucan endo-transglycosylase (PttXET16-34, EC 2.4.1.207) into alanine, glycine, and serine yielded enzymes with glycosynthase activity. Product analysis indicated that PttXET16-34 E85A in particular was able to catalyse regio- and stereospecific homo- and hetero-condensations of α-xylogluco- oligosaccharyl fluoride donors XXXGαF and XLLGαF to produce xyloglucans with regular sidechain substitution patterns. This substrate promiscuity contrasts that of the Humicola insolens Cel7B E197A glycosynthase, which was not able to polymerise the di-galactosylated substrate XLLGαF. The production of the PttXET16-34 E85A xyloglucosynthase thus expands the repertoire of glycosynthases to include those capable of synthesising structurally homogenenous xyloglucans for applications. © The Royal Society of Chemistry.},
correspondence_address1={Brumer, H.; School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91, Stockholm, Sweden; email: harry@biotech.kth.se},
publisher={Royal Society of Chemistry},
issn={14770520},
coden={OBCRA},
language={English},
abbrev_source_title={Org. Biomol. Chem.},
document_type={Article},
source={Scopus},
}

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M. Hancock, M. D. Vaughan and S. G. Withers, Curr. Opin. Chem. Biol., 2006, 10, 509-519). Site-directed mutagenesis of the catalytic nucleophile, Glu-85, of a Populus tremula x tremuloides xyloglucan endo-transglycosylase (PttXET16-34, EC 2.4.1.207) into alanine, glycine, and serine yielded enzymes with glycosynthase activity. Product analysis indicated that PttXET16-34 E85A in particular was able to catalyse regio- and stereospecific homo- and hetero-condensations of α-xylogluco- oligosaccharyl fluoride donors XXXGαF and XLLGαF to produce xyloglucans with regular sidechain substitution patterns. This substrate promiscuity contrasts that of the Humicola insolens Cel7B E197A glycosynthase, which was not able to polymerise the di-galactosylated substrate XLLGαF. The production of the PttXET16-34 E85A xyloglucosynthase thus expands the repertoire of glycosynthases to include those capable of synthesising structurally homogenenous xyloglucans for applications. © The Royal Society of Chemistry.","correspondence_address1":"Brumer, H.; School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91, Stockholm, Sweden; email: harry@biotech.kth.se","publisher":"Royal Society of Chemistry","issn":"14770520","coden":"OBCRA","language":"English","abbrev_source_title":"Org. Biomol. Chem.","document_type":"Article","source":"Scopus","bibtex":"@ARTICLE{Piens20073971,\r\nauthor={Piens, K. and Henriksson, A.-M. and Gullfot, F. and Lopez, M. and Fauré, R. and Ibatullin, F.M. and Teeri, T.T. and Driguez, H. and Brumer, H.},\r\ntitle={Glycosynthase activity of hybrid aspen xyloglucan endo-transglycosylase PttXET16-34 nucleophile mutants},\r\njournal={Organic and Biomolecular Chemistry},\r\nyear={2007},\r\nvolume={5},\r\nnumber={24},\r\npages={3971-3978},\r\ndoi={10.1039/b714570e},\r\nnote={cited By 20},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-36749095084&doi=10.1039%2fb714570e&partnerID=40&md5=2db6d80ea903a5f97675e2ec94acd10b},\r\naffiliation={School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91, Stockholm, Sweden; Laboratory for Protein Biochemistry and Biomolecular Engineering, Department of Biochemistry, Physiology and Microbiology, Ghent University, K.L.-Ledeganckstraat 35, 9000, Ghent, Belgium; Centre de Recherches sur les Macromolécules Végé tales, (CERMAV-CNRS), B.P. 53, F-38041, Grenoble cedex 9, France; Joseph Fourier University, France; Institut de Chimie Moléculaire de Grenoble FR-CNRS 2607, France},\r\nabstract={Glycosynthases are active-site mutants of glycoside hydrolases that catalyse glycosyl transfer using suitable activated donor substrates without competing product hydrolysis (S. M. Hancock, M. D. Vaughan and S. G. Withers, Curr. Opin. Chem. Biol., 2006, 10, 509-519). Site-directed mutagenesis of the catalytic nucleophile, Glu-85, of a Populus tremula x tremuloides xyloglucan endo-transglycosylase (PttXET16-34, EC 2.4.1.207) into alanine, glycine, and serine yielded enzymes with glycosynthase activity. Product analysis indicated that PttXET16-34 E85A in particular was able to catalyse regio- and stereospecific homo- and hetero-condensations of α-xylogluco- oligosaccharyl fluoride donors XXXGαF and XLLGαF to produce xyloglucans with regular sidechain substitution patterns. This substrate promiscuity contrasts that of the Humicola insolens Cel7B E197A glycosynthase, which was not able to polymerise the di-galactosylated substrate XLLGαF. The production of the PttXET16-34 E85A xyloglucosynthase thus expands the repertoire of glycosynthases to include those capable of synthesising structurally homogenenous xyloglucans for applications. © The Royal Society of Chemistry.},\r\ncorrespondence_address1={Brumer, H.; School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91, Stockholm, Sweden; email: harry@biotech.kth.se},\r\npublisher={Royal Society of Chemistry},\r\nissn={14770520},\r\ncoden={OBCRA},\r\nlanguage={English},\r\nabbrev_source_title={Org. Biomol. Chem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n","author_short":["Piens, K.","Henriksson, A.","Gullfot, F.","Lopez, M.","Fauré, R.","Ibatullin, F.","Teeri, T.","Driguez, H.","Brumer, H."],"key":"Piens20073971","id":"Piens20073971","bibbaseid":"piens-henriksson-gullfot-lopez-faur-ibatullin-teeri-driguez-etal-glycosynthaseactivityofhybridaspenxyloglucanendotransglycosylasepttxet1634nucleophilemutants-2007","role":"author","urls":{"Paper":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-36749095084&doi=10.1039%2fb714570e&partnerID=40&md5=2db6d80ea903a5f97675e2ec94acd10b"},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bio.pnpi.nrcki.ru/wp-content/uploads/2019/12/lbmx_2019_10.txt","dataSources":["5udpPf7ooeTjMNNMd"],"keywords":[],"search_terms":["glycosynthase","activity","hybrid","aspen","xyloglucan","endo","transglycosylase","pttxet16","nucleophile","mutants","piens","henriksson","gullfot","lopez","fauré","ibatullin","teeri","driguez","brumer"],"title":"Glycosynthase activity of hybrid aspen xyloglucan endo-transglycosylase PttXET16-34 nucleophile mutants","year":2007}