Dihydroorotate dehydrogenase
From Wikipedia, the free encyclopedia
| Dihydroorotate dehydrogenase fom E. coli | ||
| Identifiers | ||
|---|---|---|
| Symbol | DHO_dh | |
| Pfam | PF01180 | |
| InterPro | IPR001295 | |
| PROSITE | PDOC00708 | |
| SCOP | 1dor | |
| OPM family | 59 | |
| OPM protein | 1uum | |
| Available PDB structures:
1f76A:47-336 1uumA:77-377 1uuoA:77-377 1d3gA:77-377 1d3hA:77-377 2b0mA:77-377 1lx3A:49-334 1tv5A:207-550 1ep3A:6-291 1ep2A:6-291 1ep1A:6-291 1h7xA:532-838 1gteA:532-838 1h7wB:532-838 1gthA:532-838 1gt8A:532-838 1jueA:1-293 1jrbA:1-293 1jubA:1-293 1jqxA:1-293 1jrcB:1-293 2dorA:1-293 1nfcA:1-293 1jqvB:1-293 1ovdB:1-293 1dorA:1-293 2b4gD:2-294 |
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Human dihydroorotate dehydrogenase
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| Identifiers | |
| Symbol | DHODH |
| Entrez | 1723 |
| HUGO | 2867 |
| OMIM | 126064 |
| PDB | 1D3G |
| RefSeq | NM_001361 |
| UniProt | Q02127 |
| Other data | |
| EC number | 1.3.3.1 |
| Locus | Chr. 16 q22 |
Dihydroorotate dehydrogenase (EC 1.3.3.1) is an enzyme that catalyzes the fourth step in the de novo biosynthesis of pyrimidine. It converts dihydroorotate to orotate:
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Orotic acid. Note the double bond in the ring. |
Dihydroorotate dehydrogenase is a ubiquitous FAD flavoprotein. In bacteria (gene pyrD), it is located on the inner side of the cytosolic membrane. In some yeasts, such as in Saccharomyces cerevisiae (gene URA1), it is a cytosolic protein while in other eukaryotes it is found in the mitochondria[1].
Contents |
[edit] Human proteins containing this domain
DHODH; DPYD;
[edit] References
- ^ Lacroute F, Thomas D, Nagy M (1992). "Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts". Proc. Natl. Acad. Sci. U.S.A. 89 (19): 8966–8970. doi:. PMID 1409592.
[edit] Further reading
- [1]. The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function. Rowland P, Bjornberg O, Nielsen FS, Jensen KF, Larsen S; Protein Sci 1998;7:1269-1279. PubMed
[edit] External links
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This article includes text from the public domain Pfam and InterPro IPR001295

