| Orotate phosphoribosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 S. cerevisiae orotate phosphoribosyl transferase bound to its substrates. From PDB file 2PS1.[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 2.4.2.10 | ||||||||
| CAS no. | 9030-25-5 | ||||||||
| 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 | ||||||||
| |||||||||
Orotate phosphoribosyltransferase (OPRTase) or orotic acid phosphoribosyltransferase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the formation of orotidine 5'-monophosphate (OMP) from orotate and phosphoribosyl pyrophosphate.[1] In yeast and bacteria, orotate phosphoribosyltransferase is an independent enzyme with a unique gene coding for the protein, whereas in mammals and other multicellular organisms, the catalytic function is carried out by a domain of the bifunctional enzyme UMP synthase (UMPS).[2]
- ^ a b González-Segura L, Witte JF, McClard RW, Hurley TD (December 2007). "Ternary complex formation and induced asymmetry in orotate phosphoribosyltransferase". Biochemistry. 46 (49): 14075–86. doi:10.1021/bi701023z. PMID 18020427.
- ^ Yablonski MJ, Pasek DA, Han BD, Jones ME, Traut TW (May 1996). "Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase". The Journal of Biological Chemistry. 271 (18): 10704–8. doi:10.1074/jbc.271.18.10704. PMID 8631878.