3253-22-3Relevant academic research and scientific papers
Total Synthesis of the Chlorinated Indigo-N-Glycosides Akashin A, B and C
Pfretzschner, Alexander T.,Unverzagt, Carlo
supporting information, p. 206 - 229 (2021/03/22)
A total synthesis of the indigo-derived natural products akashin A-C was developed. The key step was the N-glycosylation of soluble N-benzylated-indigos with a suitably protected viosaminyl trichloroacetimidate. This donor was obtained from D-galactose. U
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.
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 (2015/02/18)
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.
