Journal
PROTEIN SCIENCE
Volume 31, Issue 9, Pages -Publisher
WILEY
DOI: 10.1002/pro.4399
Keywords
allosteric regulation; enzyme filamentation; IMP dehydrogenase; protein structure and function; purine nucleotide biosynthesis
Categories
Funding
- Spanish Ministerio de Ciencia e Innovacion-FEDER-Fondo Social Europeo [PID2019-109671GB-I00, PID2020-118200RB-I00]
- Junta de Castilla y Leon
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This article reviews recent developments in understanding the mechanisms of IMPDH regulation, including all layers of allosteric control that fine-tune enzyme activity.
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.
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