@ARTICLE{Borisova2015115,
author={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.},
title={α-Galactobiosyl units: Thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima},
journal={Carbohydrate Research},
year={2015},
volume={401},
pages={115-121},
doi={10.1016/j.carres.2014.11.003},
note={cited By 5},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84918807980&doi=10.1016%2fj.carres.2014.11.003&partnerID=40&md5=a72be071ed1f9fe275f7d4cc1bf43ce0},
affiliation={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},
abstract={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.},
funding_details={Российский Фонд Фундаментальных Исследований (РФФИ)12-08-00813-a},
}

{"_id":"tQyEwJ6JBQf9zfmK4","bibbaseid":"borisova-ivanen-bobrov-eneyskaya-rychkov-sandgren-kulminskaya-sinnott-etal-galactobiosylunitsthermodynamicsandkineticsoftheirformationbytransglycosylationscatalysedbythegh36galactosidasefromthermotogamaritima-2015","authorIDs":[],"author_short":["Borisova, A.","Ivanen, D.","Bobrov, K.","Eneyskaya, E.","Rychkov, G.","Sandgren, M.","Kulminskaya, A.","Sinnott, M.","Shabalin, K."],"bibdata":{"bibtype":"article","type":"article","author":[{"propositions":[],"lastnames":["Borisova"],"firstnames":["A.S."],"suffixes":[]},{"propositions":[],"lastnames":["Ivanen"],"firstnames":["D.R."],"suffixes":[]},{"propositions":[],"lastnames":["Bobrov"],"firstnames":["K.S."],"suffixes":[]},{"propositions":[],"lastnames":["Eneyskaya"],"firstnames":["E.V."],"suffixes":[]},{"propositions":[],"lastnames":["Rychkov"],"firstnames":["G.N."],"suffixes":[]},{"propositions":[],"lastnames":["Sandgren"],"firstnames":["M."],"suffixes":[]},{"propositions":[],"lastnames":["Kulminskaya"],"firstnames":["A.A."],"suffixes":[]},{"propositions":[],"lastnames":["Sinnott"],"firstnames":["M.L."],"suffixes":[]},{"propositions":[],"lastnames":["Shabalin"],"firstnames":["K.A."],"suffixes":[]}],"title":"α-Galactobiosyl units: Thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima","journal":"Carbohydrate Research","year":"2015","volume":"401","pages":"115-121","doi":"10.1016/j.carres.2014.11.003","note":"cited By 5","url":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-84918807980&doi=10.1016%2fj.carres.2014.11.003&partnerID=40&md5=a72be071ed1f9fe275f7d4cc1bf43ce0","affiliation":"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","abstract":"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.","funding_details":"Российский Фонд Фундаментальных Исследований (РФФИ)12-08-00813-a","bibtex":"@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}","author_short":["Borisova, A.","Ivanen, D.","Bobrov, K.","Eneyskaya, E.","Rychkov, G.","Sandgren, M.","Kulminskaya, A.","Sinnott, M.","Shabalin, K."],"key":"Borisova2015115","id":"Borisova2015115","bibbaseid":"borisova-ivanen-bobrov-eneyskaya-rychkov-sandgren-kulminskaya-sinnott-etal-galactobiosylunitsthermodynamicsandkineticsoftheirformationbytransglycosylationscatalysedbythegh36galactosidasefromthermotogamaritima-2015","role":"author","urls":{"Paper":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-84918807980&doi=10.1016%2fj.carres.2014.11.003&partnerID=40&md5=a72be071ed1f9fe275f7d4cc1bf43ce0"},"metadata":{"authorlinks":{}},"downloads":0},"bibtype":"article","biburl":"https://bio.pnpi.nrcki.ru/wp-content/uploads/2019/12/lmkb_2019_10.txt","creationDate":"2019-11-05T14:32:09.806Z","downloads":0,"keywords":[],"search_terms":["galactobiosyl","units","thermodynamics","kinetics","formation","transglycosylations","catalysed","gh36","galactosidase","thermotoga","maritima","borisova","ivanen","bobrov","eneyskaya","rychkov","sandgren","kulminskaya","sinnott","shabalin"],"title":"α-Galactobiosyl units: Thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima","year":2015,"dataSources":["MohP3xiH36sPcgi5S","y5Lc9ma36AFGThecr","rgjRz8LhiuL9Prc4S"]}