Glycerol-3-Phosphate Dehydrogenase: The K120 and K204 Side Chains Define an Oxyanion Hole at the Enzyme Active Site.


Journal

Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623

Informations de publication

Date de publication:
17 05 2022
Historique:
pubmed: 4 5 2022
medline: 20 5 2022
entrez: 3 5 2022
Statut: ppublish

Résumé

The cationic K120 and K204 side chains lie close to the C-2 carbonyl group of substrate dihydroxyacetone phosphate (DHAP) at the active site of glycerol-3-phosphate dehydrogenase (GPDH), and the K120 side chain is also positioned to form a hydrogen bond to the C-1 hydroxyl of DHAP. The kinetic parameters for unactivated and phosphite dianion-activated GPDH-catalyzed reduction of glycolaldehyde and acetaldehyde (AcA) show that the transition state for the former reaction is stabilized by

Identifiants

pubmed: 35502876
doi: 10.1021/acs.biochem.2c00053
pmc: PMC9119304
doi:

Substances chimiques

Dihydroxyacetone Phosphate 57-04-5
Glycerolphosphate Dehydrogenase EC 1.1.-

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

856-867

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM116921
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM134881
Pays : United States

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Auteurs

Judith R Cristobal (JR)

Department of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, United States.

John P Richard (JP)

Department of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, United States.

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Classifications MeSH