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 Lettjournal_title
FEBS lettersauthors
Cecchini DA,Fauré R,Laville E,Potocki-Veronese Gdoi
10.1016/j.febslet.2015.08.012subject
Has Abstractpub_date
2015-10-07 00:00:00pages
3098-106issue
20 Pt Beissn
0014-5793issn
1873-3468pii
S0014-5793(15)00711-5journal_volume
589pub_type
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