@Article{Borisova2015a,
  author          = {Borisova, Anna S. and Ivanen, Dina R. and Bobrov, Kirill S. and Eneyskaya, Elena V. and Rychkov, Georgy N. and Sandgren, Mats and Kulminskaya, Anna A. and Sinnott, Michael L. and Shabalin, Konstantin A.},
  journal         = {Carbohydrate research},
  title           = {α-Galactobiosyl units: thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima.},
  year            = {2015},
  issn            = {1873-426X},
  month           = jan,
  pages           = {115--121},
  volume          = {401},
  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.},
  chemicals       = {Disaccharides, 6-O-galactopyranosylgalactose, alpha-Galactosidase},
  citation-subset = {IM},
  completed       = {2015-09-04},
  country         = {Netherlands},
  doi             = {10.1016/j.carres.2014.11.003},
  issn-linking    = {0008-6215},
  keywords        = {Biocatalysis; Disaccharides, chemistry, metabolism; Glycosylation; Hydrolysis; Kinetics; Stereoisomerism; Substrate Specificity; Thermotoga maritima, enzymology; alpha-Galactosidase, metabolism; Free energy differences; Kinetics; Regioselectivity; Thermotoga maritima; Transglycosylation; α-Galactosidase},
  nlm-id          = {0043535},
  owner           = {NLM},
  pii             = {S0008-6215(14)00419-4},
  pmid            = {25486100},
  pubmodel        = {Print-Electronic},
  pubstate        = {ppublish},
  revised         = {2014-12-29},
}

{"_id":"tQyEwJ6JBQf9zfmK4","bibbaseid":"borisova-ivanen-bobrov-eneyskaya-rychkov-sandgren-kulminskaya-sinnott-etal-galactobiosylunitsthermodynamicsandkineticsoftheirformationbytransglycosylationscatalysedbythegh36galactosidasefromthermotogamaritima-2015","authorIDs":[],"author_short":["Borisova, A. S.","Ivanen, D. R.","Bobrov, K. S.","Eneyskaya, E. V.","Rychkov, G. N.","Sandgren, M.","Kulminskaya, A. A.","Sinnott, M. L.","Shabalin, K. A."],"bibdata":{"bibtype":"article","type":"article","author":[{"propositions":[],"lastnames":["Borisova"],"firstnames":["Anna","S."],"suffixes":[]},{"propositions":[],"lastnames":["Ivanen"],"firstnames":["Dina","R."],"suffixes":[]},{"propositions":[],"lastnames":["Bobrov"],"firstnames":["Kirill","S."],"suffixes":[]},{"propositions":[],"lastnames":["Eneyskaya"],"firstnames":["Elena","V."],"suffixes":[]},{"propositions":[],"lastnames":["Rychkov"],"firstnames":["Georgy","N."],"suffixes":[]},{"propositions":[],"lastnames":["Sandgren"],"firstnames":["Mats"],"suffixes":[]},{"propositions":[],"lastnames":["Kulminskaya"],"firstnames":["Anna","A."],"suffixes":[]},{"propositions":[],"lastnames":["Sinnott"],"firstnames":["Michael","L."],"suffixes":[]},{"propositions":[],"lastnames":["Shabalin"],"firstnames":["Konstantin","A."],"suffixes":[]}],"journal":"Carbohydrate research","title":"α-Galactobiosyl units: thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima.","year":"2015","issn":"1873-426X","month":"January","pages":"115–121","volume":"401","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.","chemicals":"Disaccharides, 6-O-galactopyranosylgalactose, alpha-Galactosidase","citation-subset":"IM","completed":"2015-09-04","country":"Netherlands","doi":"10.1016/j.carres.2014.11.003","issn-linking":"0008-6215","keywords":"Biocatalysis; Disaccharides, chemistry, metabolism; Glycosylation; Hydrolysis; Kinetics; Stereoisomerism; Substrate Specificity; Thermotoga maritima, enzymology; alpha-Galactosidase, metabolism; Free energy differences; Kinetics; Regioselectivity; Thermotoga maritima; Transglycosylation; α-Galactosidase","nlm-id":"0043535","owner":"NLM","pii":"S0008-6215(14)00419-4","pmid":"25486100","pubmodel":"Print-Electronic","pubstate":"ppublish","revised":"2014-12-29","bibtex":"@Article{Borisova2015a,\n author = {Borisova, Anna S. and Ivanen, Dina R. and Bobrov, Kirill S. and Eneyskaya, Elena V. and Rychkov, Georgy N. and Sandgren, Mats and Kulminskaya, Anna A. and Sinnott, Michael L. and Shabalin, Konstantin A.},\n journal = {Carbohydrate research},\n title = {α-Galactobiosyl units: thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima.},\n year = {2015},\n issn = {1873-426X},\n month = jan,\n pages = {115--121},\n volume = {401},\n 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.},\n chemicals = {Disaccharides, 6-O-galactopyranosylgalactose, alpha-Galactosidase},\n citation-subset = {IM},\n completed = {2015-09-04},\n country = {Netherlands},\n doi = {10.1016/j.carres.2014.11.003},\n issn-linking = {0008-6215},\n keywords = {Biocatalysis; Disaccharides, chemistry, metabolism; Glycosylation; Hydrolysis; Kinetics; Stereoisomerism; Substrate Specificity; Thermotoga maritima, enzymology; alpha-Galactosidase, metabolism; Free energy differences; Kinetics; Regioselectivity; Thermotoga maritima; Transglycosylation; α-Galactosidase},\n nlm-id = {0043535},\n owner = {NLM},\n pii = {S0008-6215(14)00419-4},\n pmid = {25486100},\n pubmodel = {Print-Electronic},\n pubstate = {ppublish},\n revised = {2014-12-29},\n}\n\n","author_short":["Borisova, A. S.","Ivanen, D. R.","Bobrov, K. S.","Eneyskaya, E. V.","Rychkov, G. N.","Sandgren, M.","Kulminskaya, A. A.","Sinnott, M. L.","Shabalin, K. A."],"key":"Borisova2015a","id":"Borisova2015a","bibbaseid":"borisova-ivanen-bobrov-eneyskaya-rychkov-sandgren-kulminskaya-sinnott-etal-galactobiosylunitsthermodynamicsandkineticsoftheirformationbytransglycosylationscatalysedbythegh36galactosidasefromthermotogamaritima-2015","role":"author","urls":{},"keyword":["Biocatalysis; Disaccharides","chemistry","metabolism; Glycosylation; Hydrolysis; Kinetics; Stereoisomerism; Substrate Specificity; Thermotoga maritima","enzymology; alpha-Galactosidase","metabolism; Free energy differences; Kinetics; Regioselectivity; Thermotoga maritima; Transglycosylation; α-Galactosidase"],"metadata":{"authorlinks":{}},"downloads":0},"bibtype":"article","biburl":"https://bio.pnpi.nrcki.ru/wp-content/uploads/2024/02/lbt.txt","creationDate":"2019-11-05T14:32:09.806Z","downloads":0,"keywords":["biocatalysis; disaccharides","chemistry","metabolism; glycosylation; hydrolysis; kinetics; stereoisomerism; substrate specificity; thermotoga maritima","enzymology; alpha-galactosidase","metabolism; free energy differences; kinetics; regioselectivity; thermotoga maritima; transglycosylation; α-galactosidase"],"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":["rgjRz8LhiuL9Prc4S","MohP3xiH36sPcgi5S","y5Lc9ma36AFGThecr"]}