Computational Design of Nitrile Hydratase from
NHase
bioengineering
catalytic activity
molecular dynamics
nitrile hydratase
rational design
thermostability
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
19 Oct 2020
19 Oct 2020
Historique:
received:
21
09
2020
revised:
08
10
2020
accepted:
16
10
2020
entrez:
22
10
2020
pubmed:
23
10
2020
medline:
27
3
2021
Statut:
epublish
Résumé
High thermostability and catalytic activity are key properties for nitrile hydratase (NHase, EC 4.2.1.84) as a well-industrialized catalyst. In this study, rational design was applied to tailor the thermostability of NHase from
Identifiants
pubmed: 33086715
pii: molecules25204806
doi: 10.3390/molecules25204806
pmc: PMC7587978
pii:
doi:
Substances chimiques
Hydro-Lyases
EC 4.2.1.-
nitrile hydratase
EC 4.2.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
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