Ribose 1,5-bisphosphate phosphokinase

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In enzymology, a ribose 1,5-bisphosphate phosphokinase (EC 2.7.4.23) is an enzyme that catalyzes the chemical reaction

ATP + ribose 1,5-bisphosphate ADP + 5-phospho-alpha-D-ribose 1-diphosphate

Thus, the two substrates of this enzyme are ATP and ribose 1,5-bisphosphate, whereas its two products are ADP and 5-phospho-alpha-D-ribose 1-diphosphate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:ribose-1,5-bisphosphate phosphotransferase. Other names in common use include ribose 1,5-bisphosphokinase, and PhnN. This enzyme participates in pentose phosphate pathway.

[edit] References

• IUBMB entry for 2.7.4.23
• BRENDA references for 2.7.4.23 (Recommended.)
• PubMed references for 2.7.4.23
• PubMed Central references for 2.7.4.23
• Google Scholar references for 2.7.4.23
• Hove-Jensen B, Rosenkrantz TJ, Haldimann A, Wanner BL (2003). "Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity (phosphoribosyl diphosphate forming): dual role in phosphonate degradation and NAD biosynthesis pathways". J. Bacteriol. 185: 2793–801. PMID 12700258. 

[edit] External links

• IUBMB entry for 2.7.4.23

• KEGG entry for 2.7.4.23

• BRENDA entry for 2.7.4.23

• NiceZyme view of 2.7.4.23

• EC2PDB: PDB structures for 2.7.4.23

• PRIAM entry for 2.7.4.23

• PUMA2 entry for 2.7.4.23

• IntEnz: Integrated Enzyme entry for 2.7.4.23

• MetaCyc entry for 2.7.4.23

• Atomic-resolution structures of enzymes belonging to this class