Pyrimidine-nucleoside phosphorylase
| pyrimidine-nucleoside phosphorylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.4.2.2 | ||||||||
| CAS number | 9055-35-0 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a pyrimidine-nucleoside phosphorylase (EC 2.4.2.2) is an enzyme that catalyzes the chemical reaction
- a pyrimidine nucleoside + phosphate a pyrimidine base + alpha-D-ribose 1-phosphate
Thus, the two substrates of this enzyme are pyrimidine nucleoside and phosphate, whereas its two products are pyrimidine base 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 pyrimidine-nucleoside:phosphate alpha-D-ribosyltransferase. This enzyme is also called Py-NPase. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1BRW and 2DSJ.
References
- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 237-255.
- Saunders PP, Wilson BA, Saunders GF (1969). "Purification and comparative properties of a pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus". J. Biol. Chem. 244 (13): 3691–7. PMID 4978445.
- Hamamoto T, Noguchi T, Midorikawa Y (1996). "Purification and characterization of purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-2". Biosci. Biotechnol. Biochem. 60 (7): 1179–80. doi:10.1271/bbb.60.1179. PMID 8782414.
This article is issued from Wikipedia - version of the 8/10/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.