Improving the Thermostability and Activity of Transaminase From
amine transaminase
enzyme thermal stability system
molecular dynamics simulations
site-directed mutagenesis
thermostability
Journal
Frontiers in chemistry
ISSN: 2296-2646
Titre abrégé: Front Chem
Pays: Switzerland
ID NLM: 101627988
Informations de publication
Date de publication:
2021
2021
Historique:
received:
05
02
2021
accepted:
23
03
2021
entrez:
3
5
2021
pubmed:
4
5
2021
medline:
4
5
2021
Statut:
epublish
Résumé
Transaminases that promote the amination of ketones into amines are an emerging class of biocatalysts for preparing a series of drugs and their intermediates. One of the main limitations of (
Identifiants
pubmed: 33937200
doi: 10.3389/fchem.2021.664156
pmc: PMC8081293
doi:
Types de publication
Journal Article
Langues
eng
Pagination
664156Informations de copyright
Copyright © 2021 Cao, Fan, Lv, Wang, Li, Hu, Zhao, Chen, Huang and Mei.
Déclaration de conflit d'intérêts
H-BC was employed by the company Enzymaster (Ningbo) Bio-Engineering. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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