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α-Galactobiosyl units: thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima.
- Source :
-
Carbohydrate Research . Jan2015, Vol. 401, p115-121. 7p. - Publication Year :
- 2015
-
Abstract
- Broad regioselectivity of α-galactosidase from Thermotoga maritima ( Tm Gal36A) 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 p NP-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 (ΔΔ G ‡ 0 values were equal 5.34 ± 0.85 kJ/mol) and between 1,6-linkage and 1,3-linkage (ΔΔ G ‡ 0 = 1.46 ± 0.23 kJ/mol) in p NP-galactobiosides over the course of the reaction catalysed by Tm Gal36A. Using the free energy difference for formation and hydrolysis of glycosidic linkages (ΔΔ G ‡ F − ΔΔ G ‡ 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00086215
- Volume :
- 401
- Database :
- Academic Search Index
- Journal :
- Carbohydrate Research
- Publication Type :
- Academic Journal
- Accession number :
- 100155835
- Full Text :
- https://doi.org/10.1016/j.carres.2014.11.003