Phosphoribokinase
From Wikipedia, the free encyclopedia
In enzymology, a phosphoribokinase (EC 2.7.1.18) is an enzyme that catalyzes the chemical reaction
- ATP + D-ribose 5-phosphate
ADP + D-ribose 1,5-bisphosphate
Thus, the two substrates of this enzyme are ATP and D-ribose 5-phosphate, whereas its two products are ADP and D-ribose 1,5-bisphosphate.
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 ATP:D-ribose-5-phosphate 1-phosphotransferase. This enzyme is also called phosphoribokinase (phosphorylating).
[edit] References
- IUBMB entry for 2.7.1.18
- BRENDA references for 2.7.1.18 (Recommended.)
- PubMed references for 2.7.1.18
- PubMed Central references for 2.7.1.18
- Google Scholar references for 2.7.1.18
- Krebs EG (1966). "Phosphorylase b kinase from rabbit muscle". Methods Enzymol. 8: 543–546.
- Scarano E (1953). "Quoted by H.M. Kalckar The role of phosphoglycosyl compounds in the biosynthesis of nucleosides and nucleotides". Biochim. Biophys. Acta 12: 250–264. doi:.
[edit] External links
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- The CAS registry number for this enzyme class is 9030-59-5.

