Enhancement in the catalytic efficiency of D-amino acid oxidase from Glutamicibacter protophormiae by multiple amino acid substitutions.
Active-site lid
Catalytic efficiency
D-amino acid oxidase
Glutamicibacter protophormia
Triple-point mutant
Journal
Enzyme and microbial technology
ISSN: 1879-0909
Titre abrégé: Enzyme Microb Technol
Pays: United States
ID NLM: 8003761
Informations de publication
Date de publication:
May 2023
May 2023
Historique:
received:
21
10
2022
revised:
16
01
2023
accepted:
27
02
2023
medline:
11
4
2023
pubmed:
9
3
2023
entrez:
8
3
2023
Statut:
ppublish
Résumé
D-Amino acid oxidase (DAAO) is an imperative oxidoreductase that oxidizes D-amino acids to corresponding keto acids, producing ammonia and hydrogen peroxide. Previously, based on the sequence alignment of DAAO from Glutamicibacter protophormiae (GpDAAO-1) and (GpDAAO-2), 4 residues (E115, N119, T256, T286) at the surface regions of GpDAAO-2, were subjected to site-directed mutagenesis and achieved 4 single-point mutants with enhanced catalytic efficiency (k
Identifiants
pubmed: 36889103
pii: S0141-0229(23)00032-7
doi: 10.1016/j.enzmictec.2023.110224
pii:
doi:
Substances chimiques
Amino Acids
0
D-Amino-Acid Oxidase
EC 1.4.3.3
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
110224Informations de copyright
Copyright © 2023 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare no conflict of interest regarding the data presented in the manuscript.