EC 126.96.36.199 - Dihydroorotate dehydrogenase (NAD+)
IntEnz Enzyme Nomenclature
orotate reductase (NADH2)
13516 [IUBMB](S)-dihydroorotate(S)-dihydroorotateName origin: UniProt - CHECKED (C)Formula: C5H5N2O4
Charge: -1ChEBI compound status: CHECKED (C)NAD+NAD(+)Name origin: UniProt - CHECKED (C)Formula: C21H26N7O14P2
Charge: -1ChEBI compound status: CHECKED (C)<=>H+H(+)Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)NADHNADHName origin: UniProt - CHECKED (C)Formula: C21H27N7O14P2
Charge: -2ChEBI compound status: CHECKED (C)
Binds FMN, FAD and a [2Fe-2S] cluster. The enzyme consists of two subunits, an FMN binding catalytic subunit and a FAD and iron-sulfur binding electron transfer subunit . The reaction, which takes place in the cytosol, is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 188.8.131.52) or NADP+ (EC 184.108.40.206) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 220.127.116.11) uses quinone as electron acceptor.
Links to other databases
Purification and properties of dihydroorotic acid dehydrogenase.J. Biol. Chem. 233: 1398-1406 (1958).
Crystalline dihydroorotic dehydrogenase.J. Biol. Chem. 235: 1526-1532 (1960).
Enzymic synthesis and breakdown of a pyrimidine, orotic acid. I. Dihydro-orotic dehydrogenase.Biochim. Biophys. Acta 12: 223-234 (1953).
The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers.J. Biol. Chem. 271: 29359-29365 (1996). [PMID: 8910599]
Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster.Structure 8: 1227-1238 (2000). [PMID: 11188687]
Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits.Arch. Biochem. Biophys. 371: 191-201 (1999). [PMID: 10545205]
Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism.Biochemistry 38: 13129-13137 (1999). [PMID: 10529184]
[EC 18.104.22.168 created 1972, modified 2011]