Expanded Substrate Specificity in D-Amino Acid Transaminases: A Case Study of Transaminase from
D-amino acid
phenylhydrazine
stereoselective amination
structure-function relationships
transaminase
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
10 Nov 2023
10 Nov 2023
Historique:
received:
20
10
2023
revised:
07
11
2023
accepted:
09
11
2023
medline:
27
11
2023
pubmed:
25
11
2023
entrez:
25
11
2023
Statut:
epublish
Résumé
Enzymes with expanded substrate specificity are good starting points for the design of biocatalysts for target reactions. However, the structural basis of the expanded substrate specificity is still elusive, especially in the superfamily of pyridoxal-5'-phosphate-dependent transaminases, which are characterized by a conserved organization of both the active site and functional dimer. Here, we analyze the structure-function relationships in a non-canonical D-amino acid transaminase from
Identifiants
pubmed: 38003383
pii: ijms242216194
doi: 10.3390/ijms242216194
pmc: PMC10671532
pii:
doi:
Substances chimiques
Amino Acids
0
Transaminases
EC 2.6.1.-
Phenethylamines
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Russian Science Foundation
ID : 19_14_00164
Organisme : Ministry of Science and Higher Education of the Russian Federation
ID : no number
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