Borisova, Anna S., Ivanen, Dina R., Bobrov, Kirill S., Eneyskaya, Elena V., Rychkov, Georgy N., Sandgren, Mats, Kulminskaya, Anna A., Sinnott, Michael L. and Shabalin1, Konstantin A. (2015) α-Galactobiosyl units: thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima. Carbohydrate Research, 401. pp. 115-121. ISSN 00086215Metadata only available from this repository.
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.
|Subjects:||Q Science > Q Science (General)
Q Science > QD Chemistry
|Schools:||School of Applied Sciences|
|Depositing User:||Sara Taylor|
|Date Deposited:||25 Jun 2015 08:31|
|Last Modified:||25 Jun 2015 08:31|
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