Interplay of structural preorganization and conformational sampling in UDP-glucuronic acid 4-epimerase catalysis.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
08 May 2024
08 May 2024
Historique:
received:
20
12
2023
accepted:
26
04
2024
medline:
9
5
2024
pubmed:
9
5
2024
entrez:
8
5
2024
Statut:
epublish
Résumé
Understanding enzyme catalysis as connected to protein motions is a major challenge. Here, based on temperature kinetic studies combined with isotope effect measurements, we obtain energetic description of C-H activation in NAD-dependent UDP-glucuronic acid C4 epimerase. Approach from the ensemble-averaged ground state (GS) to the transition state-like reactive conformation (TSRC) involves, alongside uptake of heat (
Identifiants
pubmed: 38719841
doi: 10.1038/s41467-024-48281-6
pii: 10.1038/s41467-024-48281-6
doi:
Substances chimiques
Carbohydrate Epimerases
EC 5.1.3.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3897Subventions
Organisme : Austrian Science Fund (Fonds zur Förderung der Wissenschaftlichen Forschung)
ID : I 3247
Informations de copyright
© 2024. The Author(s).
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