IMP dehydrogenase
| IMP dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Structure of IMPDH[1]
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| Identifiers | |||||||||
| EC number | 1.1.1.205 | ||||||||
| CAS number | Template:CAS | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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IMP dehydrogenase EC 1.1.1.205 (Inosine-5'-monophosphate dehydrogenase) (Inosinic acid dehydrogenaseis) (IMPDH) an enzyme that converts inosine monophosphate to xanthosine monophosphate:[2][3][4][5]
- inosine 5'-phosphate + NAD+ + H2O
xanthosine 5'-phosphate + NADH + H+
It catalyzes the rate-limiting reaction of de novo GTP biosynthesis.[6]
IMP dehydrogenase is associated with cell proliferation and is a possible target for cancer chemotherapy. Mammalian and bacterial IMPDHs are tetramers of identical chains. There are two IMP dehydrogenase isozymes in humans.[7] IMP dehydrogenase nearly always contains a long insertion that has two CBS domains within it.
The structure of this enzyme is composed of a TIM barrel domain with two CBS domains inserted within a loop.[1][4]
It is inhibited by Mycophenolic acid, ribavirin, and 6TGMP (6-thioguanine monophosphate). 6TGMP inhibition prevents purine interconversion and thus the synthesis of purine nucleotides.
Examples
Humans express the following two IMP dehydrogenase isozymes:
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See also
References
- ↑ 1.0 1.1 Lua error in package.lua at line 80: module 'strict' not found.
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- ↑ 4.0 4.1 Lua error in package.lua at line 80: module 'strict' not found.
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Further reading
- Lua error in package.lua at line 80: module 'strict' not found.
This article incorporates text from the public domain Pfam and InterPro IPR001093
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