The Uncommon Active Site of D-Amino Acid Transaminase from
D-amino acid transaminase
X-ray analysis
arginine residues
enzyme catalysis
sequence-structure-function relationships
substrate specificity
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
20 Aug 2021
20 Aug 2021
Historique:
received:
23
07
2021
revised:
16
08
2021
accepted:
17
08
2021
entrez:
27
8
2021
pubmed:
28
8
2021
medline:
23
9
2021
Statut:
epublish
Résumé
Among industrially important pyridoxal-5'-phosphate (PLP)-dependent transaminases of fold type IV D-amino acid transaminases are the least studied. However, the development of cascade enzymatic processes, including the synthesis of D-amino acids, renewed interest in their study. Here, we describe the identification, biochemical and structural characterization of a new D-amino acid transaminase from
Identifiants
pubmed: 34443642
pii: molecules26165053
doi: 10.3390/molecules26165053
pmc: PMC8401098
pii:
doi:
Substances chimiques
Amino Acids
0
Bacterial Proteins
0
Pyridoxal Phosphate
5V5IOJ8338
Transaminases
EC 2.6.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Russian Science Foundation
ID : 19-14-00164
Organisme : Russian Foundation for Basic Research
ID : 18-29-13006
Organisme : Ministry of Science and Higher Education of the Russian Federation
ID : 2021
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