187394-28-1Relevant articles and documents
Chemical and enzymatic synthesis of glycoconjugates 5: One-pot regioselective synthesis of bioactive galactobiosides using a clonezyme(TM) thermophilic glycosidase library
Li, Jun,Robertson, Dan E.,Short, Jay M.,Wang, Peng George
, p. 35 - 38 (1999)
Enzymatic synthesis of galactobiosides using a versatile CLONEZYME(TM) thermostable glycosidase library was studied. One-pot transglycosylation reactions were demonstrated to synthesize β(1→4), β(1→6), and α(1→6) disaccharide sequences with high regiosele
Semi-rational approach for converting a GH36 α-glycosidase into an α-transglycosidase
Teze, David,Daligault, Franck,Ferrières, Vincent,Sanejouand, Yves-Henri,Tellier, Charles
, p. 420 - 427 (2015)
A large number of retaining glycosidases catalyze both hydrolysis and transglycosylation reactions. In order to use them as catalysts for oligosaccharide synthesis, the balance between these two competing reactions has to be shifted toward transglycosylat
Preparation of α-galactooligoglycosides by cell walls from Cryptococcus laurentii using a novel α-galactosyl donor
Mastihuba, Vladimír,Mastihubová, Mária,Belák, Miroslav,Dudíková, Jana,Potocká, Elena Karni?ová,Petru?, Ladislav
, p. 1089 - 1094 (2017/10/05)
The cell walls of an acapsular strain of the yeast Cryptococcus laurentii catalyze the regioselective formation of α-galactooligosaccharides through self-condensation of 4-nitrophenyl α-D-galactopyranoside and of a novel activated α-galactosyl donor 2,2,2-trifluoroethyl α-D-galactopyranoside. The latter substance can be easily prepared by several methods and is highly soluble in water and therefore can be used in higher initial concentrations suppressing secondary product hydrolysis. The preparative reaction catalyzed by cell walls provided 17.4% and 2% of corresponding 2,2,2-trifluoroethyl galactobioside and galactotrioside, respectively, while the reaction with 4-nitrophenyl α-D-galactopyranoside provided the corresponding 4-nitrophenyl galactobioside and galactotrioside in 6.6 and 2.5% yields, respectively. The reactions proceeded with strict α-(1 → 6)-regioselectivity.
α-Galactobiosyl units: Thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima
Borisova, Anna S.,Ivanen, Dina R.,Bobrov, Kirill S.,Eneyskaya, Elena V.,Rychkov, Georgy N.,Sandgren, Mats,Kulminskaya, Anna A.,Sinnott, Michael L.,Shabalin, Konstantin A.
supporting information, p. 115 - 121 (2015/02/19)
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.
