The gateway to guanine nucleotides: Allosteric regulation of IMP dehydrogenases

被引：17
作者：
Buey, Ruben M. [1 ]
Fernandez-Justel, David [1 ]
Jimenez, Alberto [1 ]
Revuelta, Jose L. [1 ]
机构：
[1] Univ Salamanca, Dept Genet & Microbiol, Metab Engn Grp, Salamanca, Spain
来源：
PROTEIN SCIENCE | 2022年 / 31卷 / 09期
关键词：
allosteric regulation; enzyme filamentation; IMP dehydrogenase; protein structure and function; purine nucleotide biosynthesis; INOSINE 5'-MONOPHOSPHATE DEHYDROGENASE; DOMINANT RETINITIS-PIGMENTOSA; MONOPHOSPHATE DEHYDROGENASE; 5-MONOPHOSPHATE DEHYDROGENASE; BINDING; MUTATIONS; DISEASE; GENE; CYCLOPHILIN; METABOLISM;
D O I：
10.1002/pro.4399
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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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页数：16
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