Studying the Role of a Single Mutation of a Family 11 Glycoside Hydrolase Using High-Resolution X-ray Crystallography.
Electrostatics
General acid/base catalysis
Glycoside hydrolase
Mutagenesis
X-ray crystallography
pH-dependent activity
Journal
The protein journal
ISSN: 1875-8355
Titre abrégé: Protein J
Pays: Netherlands
ID NLM: 101212092
Informations de publication
Date de publication:
12 2020
12 2020
Historique:
accepted:
26
10
2020
pubmed:
1
11
2020
medline:
7
2
2021
entrez:
31
10
2020
Statut:
ppublish
Résumé
XynII is a family 11 glycoside hydrolase that uses the retaining mechanism for catalysis. In the active site, E177 works as the acid/base and E86 works as the nucleophile. Mutating an uncharged residue (N44) to an acidic residue (D) near E177 decreases the enzyme's optimal pH by ~ 1.0 unit. D44 was previously suggested to be a second proton carrier for catalysis. To test this hypothesis, we abolished the activity of E177 by mutating it to be Q, and mutated N44 to be D or E. These double mutants have dramatically decreased activities. Our high-resolution crystallographic structures and the microscopic pK
Identifiants
pubmed: 33128114
doi: 10.1007/s10930-020-09938-5
pii: 10.1007/s10930-020-09938-5
doi:
Substances chimiques
Fungal Proteins
0
Glycoside Hydrolases
EC 3.2.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
671-680Références
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