Evolving ω-amine transaminase
binding free energy-guided
evolution
non-natural substrates
virtual screening
ω-amine transaminase
Journal
Applied and environmental microbiology
ISSN: 1098-5336
Titre abrégé: Appl Environ Microbiol
Pays: United States
ID NLM: 7605801
Informations de publication
Date de publication:
12 Jun 2024
12 Jun 2024
Historique:
medline:
12
6
2024
pubmed:
12
6
2024
entrez:
12
6
2024
Statut:
aheadofprint
Résumé
In the field of chiral amine synthesis, ω-amine transaminase (ω-ATA) is one of the most established enzymes capable of asymmetric amination under optimal conditions. However, the applicability of ω-ATA toward more non-natural complex molecules remains limited due to its low transamination activity, thermostability, and narrow substrate scope. Here, by employing a combined approach of computational virtual screening strategy and combinatorial active-site saturation test/iterative saturation mutagenesis strategy, we have constructed the best variant M14C3-V5 (M14C3-V62A-V116S-E117I-L118I-V147F) with improved ω-ATA from
Identifiants
pubmed: 38864627
doi: 10.1128/aem.00543-24
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM