Biochemical identification of the catalytic residues of a glycoside hydrolase family 120 β-xylosidase, involved in xylooligosaccharide metabolisation by gut bacteria.

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 Asp(393), Glu(416) and Glu(364) was performed. NMR analysis of the xyloside hydrolysis products, the change of the reaction rate-limiting step for the Glu(416) 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, Glu(416) playing the role of acid/base catalyst and Asp(393) that of nucleophile.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Cecchini DA,Fauré R,Laville E,Potocki-Veronese G

doi

10.1016/j.febslet.2015.08.012

subject

Has Abstract

pub_date

2015-10-07 00:00:00

pages

3098-106

issue

20 Pt B

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(15)00711-5

journal_volume

589

pub_type

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