Xanthine phosphoribosyltransferase
| Xanthine phosphoribosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.2.22 | ||||||||
| CAS no. | 9023-10-3 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Xanthine phosphoribosyltransferase (EC 2.4.2.22) is an enzyme that catalyzes the phosphorolysis reaction
The two substrates of this enzyme characterised from Lactobacillus casei are xanthosine monophosphate and pyrophosphate (PPi). Its products are phosphoribosyl pyrophosphate and xanthine.[1]
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is XMP:diphosphate 5-phospho-alpha-D-ribosyltransferase. Other names in common use include Xan phosphoribosyltransferase, xanthosine 5'-phosphate pyrophosphorylase, xanthylate pyrophosphorylase, xanthylic pyrophosphorylase, XMP pyrophosphorylase, 5-phospho-alpha-D-ribose-1-diphosphate:xanthine, phospho-D-ribosyltransferase, 9-(5-phospho-beta-D-ribosyl)xanthine:diphosphate, and 5-phospho-alpha-D-ribosyltransferase.[2]
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1A95, PDB: 1A96, PDB: 1A97, PDB: 1A98, PDB: 1NUL, and PDB: 2FXV.
References
- ↑ Krenitsky TA, Neil SM, Miller RL (1970). "Guanine and xanthine phosphoribosyltransfer activities of Lactobacillus casei and Escherichia coli. Their relationship to hypoxanthine and adenine phosphoribosyltransfer activities" (pdf). J. Biol. Chem. 245 (10): 2605–11. doi:10.1016/S0021-9258(18)63113-8. PMID 4910918.
- ↑ Enzyme 2.4.2.22 at KEGG Pathway Database.