Structural and functional analysis of hyper-thermostable ancestral L-amino acid oxidase that can convert Trp derivatives to D-forms by chemoenzymatic reaction.
Journal
Communications chemistry
ISSN: 2399-3669
Titre abrégé: Commun Chem
Pays: England
ID NLM: 101725670
Informations de publication
Date de publication:
22 Sep 2023
22 Sep 2023
Historique:
received:
22
05
2023
accepted:
12
09
2023
medline:
22
9
2023
pubmed:
22
9
2023
entrez:
22
9
2023
Statut:
epublish
Résumé
Production of D-amino acids (D-AAs) on a large-scale enables to provide precursors of peptide therapeutics. In this study, we designed a novel L-amino acid oxidase, HTAncLAAO2, by ancestral sequence reconstruction, exhibiting high thermostability and long-term stability. The crystal structure of HTAncLAAO2 was determined at 2.2 Å by X-ray crystallography, revealing that the enzyme has an octameric form like a "ninja-star" feature. Enzymatic property analysis demonstrated that HTAncLAAO2 exhibits three-order larger k
Identifiants
pubmed: 37737277
doi: 10.1038/s42004-023-01005-1
pii: 10.1038/s42004-023-01005-1
pmc: PMC10517122
doi:
Types de publication
Journal Article
Langues
eng
Pagination
200Subventions
Organisme : MEXT | Japan Society for the Promotion of Science (JSPS)
ID : 18K14391
Organisme : MEXT | Japan Society for the Promotion of Science (JSPS)
ID : 21K05395
Organisme : MEXT | JST | Precursory Research for Embryonic Science and Technology (PRESTO)
ID : JPMJPR20AB
Informations de copyright
© 2023. Springer Nature Limited.
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