Glycerol 3-Phosphate Dehydrogenase: Role of the Protein Conformational Change in Activation of a Readily Reversible Enzyme-Catalyzed Hydride Transfer Reaction.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
16 Apr 2024
16 Apr 2024
Historique:
pmc-release:
28
03
2025
medline:
17
4
2024
pubmed:
28
3
2024
entrez:
28
3
2024
Statut:
ppublish
Résumé
Kinetic parameters are reported for glycerol 3-phosphate dehydrogenase (GPDH)-catalyzed hydride transfer from the whole substrate glycerol 3-phosphate (G3P) or truncated substrate ethylene glycol (EtG) to NAD, and for activation of the hydride transfer reaction of EtG by phosphite dianion. These kinetic parameters were combined with parameters for enzyme-catalyzed hydride transfer in the microscopic reverse direction to give the reaction equilibrium constants
Identifiants
pubmed: 38546289
doi: 10.1021/acs.biochem.3c00702
pmc: PMC11025551
doi:
Substances chimiques
Glycerolphosphate Dehydrogenase
EC 1.1.-
alpha-glycerophosphoric acid
9NTI6P3O4X
Phosphites
0
NAD
0U46U6E8UK
Glycerophosphates
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1016-1025Références
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