Names & Taxonomy
- Uniprot ID:
- P20839
- Entry Name:
- IMDH1_HUMAN
- Status:
- reviewed
- Protein Names:
- Inosine-5'-monophosphate dehydrogenase 1 (IMP dehydrogenase 1) (IMPD 1) (IMPDH 1) (EC 1.1.1.205) (IMPDH-I)
- Gene Names:
- IMPDH1 IMPD1
- Gene Names Primary:
- IMPDH1
- Organism:
- Homo sapiens (Human)
Structure
- Length:
- 514
- Sequence:
- MADYLISGGTGYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY
- Proteomes:
- UP000005640
Subcellular location
- Subcellular Location:
- Cytoplasm
Function
- Function:
- Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.
- Pathway:
- Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
- Catalytic Activity:
- Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH.
- Cofactor:
- COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103;
- Kinetics:
- BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for Inosine 5'-phosphate
- Enzyme Regulation:
- ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH. Subject to product inhibition by XMP and NADH. Also inhibited by ADP.
- Active Site:
- ACT_SITE 331 331 Thioimidate intermediate.
- Cross Reference Drug Bank:
- DB01033 DB00688 DB01024 DB00811
- Gene Ontology Go:
- cell junction
cytoplasm
cytosol
nucleoplasm
nucleus
DNA binding
IMP dehydrogenase activity
metal ion binding
nucleic acid binding
RNA binding
GMP biosynthetic process
lymphocyte proliferation
nucleobase-containing small molecule metabolic process
purine nucleobase metabolic process
purine ribonucleoside monophosphate biosynthetic process
response to cold
retina development in camera-type eye
small molecule metabolic process - Gene Ontology Biological Process:
- GMP biosynthetic process
lymphocyte proliferation
nucleobase-containing small molecule metabolic process
purine nucleobase metabolic process
purine ribonucleoside monophosphate biosynthetic process
response to cold
retina development in camera-type eye
small molecule metabolic process - Gene Ontology Molecular Function:
- DNA binding
IMP dehydrogenase activity
metal ion binding
nucleic acid binding
RNA binding - Gene Ontology Cellular Component:
- cell junction
cytoplasm
cytosol
nucleoplasm
nucleus - Keywords:
- 3D-structure
Alternative splicing
CBS domain
Complete proteome
Cytoplasm
DNA-binding
Direct protein sequencing
Disease mutation
GMP biosynthesis
Leber congenital amaurosis
Metal-binding
NAD
Nucleus
Oxidoreductase
Potassium
Purine biosynthesis
RNA-binding
Reference proteome
Repeat
Retinitis pigmentosa