Modeling the Role of a Flexible Loop and Active Site Side Chains in Hydride Transfer Catalyzed by Glycerol-3-phosphate Dehydrogenase.
Journal
ACS catalysis
ISSN: 2155-5435
Titre abrégé: ACS Catal
Pays: United States
ID NLM: 101562209
Informations de publication
Date de publication:
02 Oct 2020
02 Oct 2020
Historique:
received:
23
06
2020
revised:
31
08
2020
entrez:
12
10
2020
pubmed:
13
10
2020
medline:
13
10
2020
Statut:
ppublish
Résumé
Glycerol-3-phosphate dehydrogenase is a biomedically important enzyme that plays a crucial role in lipid biosynthesis. It is activated by a ligand-gated conformational change that is necessary for the enzyme to reach a catalytically competent conformation capable of efficient transition-state stabilization. While the human form (
Identifiants
pubmed: 33042609
doi: 10.1021/acscatal.0c02757
pmc: PMC7536716
doi:
Types de publication
Journal Article
Langues
eng
Pagination
11253-11267Subventions
Organisme : NIAID NIH HHS
ID : R01 AI116998
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM116921
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM134881
Pays : United States
Déclaration de conflit d'intérêts
The authors declare no competing financial interest.
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