The gateway to guanine nucleotides: Allosteric regulation of IMP dehydrogenases.
IMP dehydrogenase
allosteric regulation
enzyme filamentation
protein structure and function
purine nucleotide biosynthesis
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
09 2022
09 2022
Historique:
revised:
07
07
2022
received:
03
06
2022
accepted:
19
07
2022
entrez:
30
8
2022
pubmed:
31
8
2022
medline:
3
9
2022
Statut:
ppublish
Résumé
Inosine 5'-monophosphate dehydrogenase (IMPDH) is an evolutionarily conserved enzyme that mediates the first committed step in de novo guanine nucleotide biosynthetic pathway. It is an essential enzyme in purine nucleotide biosynthesis that modulates the metabolic flux at the branch point between adenine and guanine nucleotides. IMPDH plays key roles in cell homeostasis, proliferation, and the immune response, and is the cellular target of several drugs that are widely used for antiviral and immunosuppressive chemotherapy. IMPDH enzyme is tightly regulated at multiple levels, from transcriptional control to allosteric modulation, enzyme filamentation, and posttranslational modifications. Herein, we review recent developments in our understanding of the mechanisms of IMPDH regulation, including all layers of allosteric control that fine-tune the enzyme activity.
Identifiants
pubmed: 36040265
doi: 10.1002/pro.4399
pmc: PMC9375230
doi:
Substances chimiques
Enzyme Inhibitors
0
Guanine Nucleotides
0
Inosine Monophosphate
131-99-7
IMP Dehydrogenase
EC 1.1.1.205
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e4399Informations de copyright
© 2022 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.
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