Biology:Uridine phosphorylase
| uridine phosphorylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.4.2.3 | ||||||||
| CAS number | 9030-22-2 | ||||||||
| 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 uridine phosphorylase (EC 2.4.2.3) is an enzyme that catalyzes the chemical reaction
- uridine + phosphate [math]\displaystyle{ \rightleftharpoons }[/math] uracil + alpha-D-ribose 1-phosphate
Thus, the two substrates of this enzyme are uridine and phosphate, whereas its two products are uracil and alpha-D-ribose 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is uridine:phosphate alpha-D-ribosyltransferase. Other names in common use include pyrimidine phosphorylase, UrdPase, UPH, and UPase. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, 27 structures have been solved for this class of enzymes, with PDB accession codes 1K3F, 1LX7, 1RXC, 1RXS, 1RXU, 1RXY, 1RYZ, 1SJ9, 1SQ6, 1T0U, 1TGV, 1TGY, 1U1C, 1U1D, 1U1E, 1U1F, 1U1G, 1Y1Q, 1Y1R, 1Y1S, 1Y1T, 1ZL2, 2HN9, 2HRD, 2HSW, 2HWU, and 2I8A.
References
- CANELLAKIS ES (1957). "Pyrimidine metabolism. II. Enzymatic pathways of uracil anabolism". J. Biol. Chem. 227 (1): 329–38. doi:10.1016/S0021-9258(18)70818-1. PMID 13449076.
- "Bacterial uracil riboside phosphorylase". Arch. Biochem. Biophys. 40 (1): 42–9. 1952. doi:10.1016/0003-9861(52)90071-4. PMID 12997187.
- "Uridine and deoxyuridine phosphorylases from Ehrlich ascites tumor". Biochim. Biophys. Acta 51 (1): 138–147. 1961. doi:10.1016/0006-3002(61)91024-1. PMID 13737038.
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