3006-43-7

Upstream product

• 10257-28-0 D-Galactose 
• 3006-41-5 (4aR,7R,8R,8aR)-2-phenylhexahydropyrano[3,2-d][1,3]dioxine-6,7,8-triol 
• 98-88-4 benzoyl chloride 
• 100-52-7 benzaldehyde 
• 83212-64-0 (2R,3R)-2,3-Dihydroxy-3-((2R,4R,5R)-5-hydroxy-2-phenyl-[1,3]dioxan-4-yl)-propionaldehyde 

Downstream Products

• 3253-22-3 1,2,3-tri-O-benzoyl-α-D-galactopyranoside 
• 113544-57-3 1,2,3,4-tetra-O-benzoyl-6-bromo-6-deoxy-β-D-glucopyranose 
• 113544-58-4 1,2,3,4-tetra-O-benzoyl-6-bromo-6-deoxy-α-D-glucopyranose 
• 122240-48-6 O¹,O⁴,O⁶-Triacetyl-O²,O³-dibenzoyl-α-D-glucopyranose 
• 350246-42-3 methyl-(O⁴,O⁶-diacetyl-O²,O³-dibenzoyl-β-D-glucopyranoside) 

Relevant academic research and scientific papers

α-Galactobiosyl units: Thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima

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.