Biology:Orotate reductase (NADH)
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Short description: Class of enzymes
| orotate reductase (NADH) | |||||||||
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| Identifiers | |||||||||
| EC number | 1.3.1.14 | ||||||||
| CAS number | 37255-26-8 | ||||||||
| 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 / QuickGO | ||||||||
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In enzymology, an orotate reductase (NADH) (EC 1.3.1.14) is an enzyme that catalyzes the chemical reaction
- (S)-dihydroorotate + NAD+ [math]\displaystyle{ \rightleftharpoons }[/math] orotate + NADH + H+
Thus, the two substrates of this enzyme are (S)-dihydroorotate and NAD+, whereas its 3 products are orotate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-dihydroorotate:NAD+ oxidoreductase. This enzyme is also called orotate reductase (NADH). This enzyme participates in pyrimidine metabolism. It has 2 cofactors: FAD, and FMN.
References
- "Purification and properties of dihydro-orotic dehydrogenase". J. Biol. Chem. 233 (6): 1398–406. 1958. PMID 13610849.
- "Crystalline dihydroorotic dehydrogenase". J. Biol. Chem. 235: 1526–32. 1960. PMID 13825167.
- "Enzymic synthesis and breakdown of a pyrimidine, orotic acid. I Dihydro-orotic dehydrogenase". Biochim. Biophys. Acta 12 (1–2): 223–34. 1953. doi:10.1016/0006-3002(53)90141-3. PMID 13115431.
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