Ribose 1,5-bisphosphate phosphokinase

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
Ribose 1,5-bisphosphate phosphokinase
Identifiers
EC no.2.7.4.23
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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.

References

    • 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 (9): 2793–801. doi:10.1128/JB.185.9.2793-2801.2003. PMC 154390. PMID 12700258.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.