To the Understanding of Catalysis by D-Amino Acid Transaminases: A Case Study of the Enzyme from
D-amino acids
X-ray analysis
enzymes
structure
substrate-assisted catalysis
transaminase
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
23 Feb 2023
23 Feb 2023
Historique:
received:
31
01
2023
revised:
17
02
2023
accepted:
21
02
2023
entrez:
11
3
2023
pubmed:
12
3
2023
medline:
15
3
2023
Statut:
epublish
Résumé
Pyridoxal-5'-phosphate (PLP)-dependent transaminases are highly efficient biocatalysts for stereoselective amination. D-amino acid transaminases can catalyze stereoselective transamination producing optically pure D-amino acids. The knowledge of substrate binding mode and substrate differentiation mechanism in D-amino acid transaminases comes down to the analysis of the transaminase from
Identifiants
pubmed: 36903355
pii: molecules28052109
doi: 10.3390/molecules28052109
pmc: PMC10003956
pii:
doi:
Substances chimiques
Amino Acids
0
Transaminases
EC 2.6.1.-
Glutamic Acid
3KX376GY7L
Pyridoxal Phosphate
5V5IOJ8338
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Russian Science Foundation
ID : 19-14-00164
Organisme : the Grant of the President of the Russian Federation
ID : MD-1390.2022.1.4
Organisme : Ministry of Science and Higher Education of the Russian Federation
ID : no
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