In enzymology, a diphosphate-purine nucleoside kinase (EC 2.7.1.143) is an enzyme that catalyzes the chemical reaction
diphosphate-purine nucleoside kinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.1.143 | ||||||||
CAS no. | 70356-41-1 | ||||||||
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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- diphosphate + a purine nucleoside phosphate + a purine mononucleotide
Thus, the two substrates of this enzyme are diphosphate and purine nucleoside, whereas its two products are phosphate and purine mononucleotide.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is diphosphate:purine nucleoside phosphotransferase. This enzyme is also called pyrophosphate-purine nucleoside kinase.
References
edit- Tryon VV, Pollack D (1984). "Purine metabolism in Acholeplasma laidlawii B: novel PPi-dependent nucleoside kinase activity". J. Bacteriol. 159 (1): 265–70. PMC 215623. PMID 6330034.
- Tryon VV, Pollack JD (1985). "Distinctions in Mollicutes purine metabolism: pyrophosphate-dependent nucleoside kinase and dependence on guanylate salvage". Int. J. Syst. Bacteriol. 35: 497–501. doi:10.1099/00207713-35-4-497.