Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10869872 | FEBS Letters | 2015 | 9 Pages |
Abstract
The β-xylosidase B from Bifidobacterium adolescentis ATCC15703 belongs to the newly characterized family 120 of glycoside hydrolases. In order to investigate its catalytic mechanism, an extensive kinetic study of the wild-type enzyme and mutants targeting the three highly conserved residues Asp393, Glu416 and Glu364 was performed. NMR analysis of the xyloside hydrolysis products, the change of the reaction rate-limiting step for the Glu416 mutants, the pH dependency of E416A activity and its chemical rescue allowed to demonstrate that this GH120 enzyme uses a retaining mechanism of glycoside hydrolysis, Glu416 playing the role of acid/base catalyst and Asp393 that of nucleophile.
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Authors
Davide A. Cecchini, Régis Fauré, Elisabeth Laville, Gabrielle Potocki-Veronese,