Dihydroorotase (EC 3.5.2.3, carbamoylaspartic dehydrase, dihydroorotate hydrolase) is an enzyme which converts carbamoyl aspartic acid into 4,5-dihydroorotic acid in the biosynthesis of pyrimidines.[1][2] It forms a multifunctional enzyme with carbamoyl phosphate synthetase and aspartate transcarbamoylase. Dihydroorotase is a zinc metalloenzyme.[3]
| carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase | |||||||
|---|---|---|---|---|---|---|---|
 Dihydroorotase (fragment) dimer, Human | |||||||
| Identifiers | |||||||
| Symbol | CAD | ||||||
| NCBI gene | 790 | ||||||
| HGNC | 1424 | ||||||
| OMIM | 114010 | ||||||
| RefSeq | NM_004341 | ||||||
| UniProt | P27708 | ||||||
| Other data | |||||||
| EC number | 3.5.2.3 | ||||||
| Locus | Chr. 2 p22-p21 | ||||||
| |||||||
See also
editReferences
edit- ^ Cooper C, Wilson DW (1954). "Biosynthesis of pyrimidines". Fed. Proc. 13: 194.
- ^ Lieberman I, Kornberg A (April 1954). "Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. I. Dihydroortic acid, ureidosuccinic acid, and 5-carboxymethylhydantoin" (PDF). The Journal of Biological Chemistry. 207 (2): 911–24. doi:10.1016/S0021-9258(18)65708-4. PMID 13163076.911-24&rft.date=1954-04&rft_id=info:doi/10.1016/S0021-9258(18)65708-4&rft_id=info:pmid/13163076&rft.aulast=Lieberman&rft.aufirst=I&rft.au=Kornberg, A&rft_id=http://www.jbc.org/content/207/2/911.full.pdf&rfr_id=info:sid/en.wikipedia.org:Dihydroorotase" class="Z3988">
- ^ Voet, Donald (2011). Biochemistry. Judith G. Voet. Hoboken, NJ: John Wiley & Sons. ISBN 978-0-470-57095-1. OCLC 690489261.
External links
edit- Dihydroorotase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.5.2.3
