Reactome | UMPS dimer decarboxylates OMP to UMP

UMPS dimer decarboxylates OMP to UMP

Stable Identifier

R-HSA-73564

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

Synonyms

orotidine 5'-monophosphate => uridine 5'-monophosphate + CO2, decarboxylation of Orotidine 5'-phosphate to form Uridine 5'-phosphate

ReviewStatus

5/5

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The decarboxylation of orotidine 5'-monophosphate (OMP) to form uridine 5'-monophosphate (UMP) is catalyzed by the orotidine 5'-phosphate decarboxylase activity of the bifunctional "uridine monophosphate synthetase (orotate phosphoribosyl transferase and orotidine 5'-decarboxylase)" protein. While purified human protein has not been characterized in detail, the close similarity of the human gene to that encoding the well-studied hamster protein, and the demonstration that mutations in the human gene are associated with failure to convert orotate to UMP in vivo, provide convincing evidence that the human uridine monophosphate synthetase protein indeed catalyzes these two reactions (McClard et al. 1980; Suchi et al. 1997). The active form of the human protein is a dimer (Yablonski et al. 1996; Wittmann et al. 2008).

Literature References

PubMed ID	Title	Journal	Year
6893554	Isolation and initial characterization of the single polypeptide that synthesizes uridine 5'-monophosphate from orotate in Ehrlich ascites carcinoma. Purification by tandem affinity chromatography of uridine-5'-monophosphate synthase McClard, RW, Black, MJ, Livingstone, LR, Jones, ME	Biochemistry	1980
8631878	Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase Yablonski, MJ, Pasek, DA, Han, BD, Jones, ME, Traut, TW	J Biol Chem	1996
9042911	Molecular cloning of the human UMP synthase gene and characterization of point mutations in two hereditary orotic aciduria families Suchi, M, Mizuno, H, Kawai, Y, Tsuboi, T, Sumi, S, Okajima, K, Hodgson, ME, Ogawa, H, Wada, Y	Am J Hum Genet	1997
18184586	Structures of the human orotidine-5'-monophosphate decarboxylase support a covalent mechanism and provide a framework for drug design Wittmann, JG, Heinrich, D, Gasow, K, Frey, A, Diederichsen, U, Rudolph, MG	Structure	2008