Utilization of Cofactor Binding Energy for Enzyme Catalysis: Formate Dehydrogenase-Catalyzed Reactions of the Whole NAD Cofactor and Cofactor Pieces.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
01 08 2023
01 08 2023
Historique:
pmc-release:
18
07
2024
medline:
7
8
2023
pubmed:
18
7
2023
entrez:
18
7
2023
Statut:
ppublish
Résumé
The pressure to optimize enzymatic rate accelerations has driven the evolution of the induced-fit mechanism for enzyme catalysts where the binding interactions of nonreacting phosphodianion or adenosyl substrate pieces drive enzyme conformational changes to form protein substrate cages that are activated for catalysis. We report the results of experiments to test the hypothesis that utilization of the binding energy of the adenosine 5'-diphosphate ribose (ADP-ribose) fragment of the NAD cofactor to drive a protein conformational change activates
Identifiants
pubmed: 37463347
doi: 10.1021/acs.biochem.3c00290
pmc: PMC10399567
doi:
Substances chimiques
NAD
0U46U6E8UK
Formate Dehydrogenases
EC 1.17.1.9
Ribose
681HV46001
Anions
0
Phosphates
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
2314-2324Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM134881
Pays : United States
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