A cold-active esterase enhances mesophilic properties through Mn
GDSx esterases
cold adaptation
enzyme stability
psychrophilic enzymes
temperature adaptation
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
05 2023
05 2023
Historique:
revised:
20
09
2022
received:
21
06
2022
accepted:
19
10
2022
medline:
4
5
2023
pubmed:
22
10
2022
entrez:
21
10
2022
Statut:
ppublish
Résumé
A key aspect of adaptation to cold environments is the production of cold-active enzymes by psychrophilic organisms. These enzymes not only have high activity at low temperatures, but also exhibit remarkable structural flexibility and thermolability. In this context, the role of metal ions has been little explored, and the few available studies seem to suggest that metal binding counteracts structural flexibility. This article reports an investigation into the role of the binding of manganese ion (Mn
Substances chimiques
Esterases
EC 3.1.-
Ions
0
Banques de données
RefSeq
['WP_100636456.1']
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
2394-2411Informations de copyright
© 2022 Federation of European Biochemical Societies.
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