Phosphoribulokinase

From Wikipedia, the free encyclopedia

In enzymology, a phosphoribulokinase (EC 2.7.1.19) is an enzyme that catalyzes the chemical reaction

ATP + D-ribulose 5-phosphate $\rightleftharpoons$ ADP + D-ribulose 1,5-bisphosphate

Thus, the two substrates of this enzyme are ATP and D-ribulose 5-phosphate, whereas its two products are ADP and D-ribulose 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-ribulose-5-phosphate 1-phosphotransferase. Other names in common use include phosphopentokinase, ribulose-5-phosphate kinase, phosphopentokinase, phosphoribulokinase (phosphorylating), 5-phosphoribulose kinase, ribulose phosphate kinase, PKK, PRuK, and PRK. This enzyme participates in carbon fixation.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1A7J.

[edit] References

IUBMB entry for 2.7.1.19
BRENDA references for 2.7.1.19 (Recommended.)
PubMed references for 2.7.1.19
PubMed Central references for 2.7.1.19
Google Scholar references for 2.7.1.19
HURWITZ J, WEISSBACH A, HORECKER BL, SMYRNIOTIS PZ (1956). "Spinach phosphoribulokinase". J. Biol. Chem. 218: 769–83. PMID 13295229.
JAKOBY WB, BRUMMOND DO, OCHOA S (1956). "Formation of 3-phosphoglyceric acid by carbon dioxide fixation with spinach leaf enzymes". J. Biol. Chem. 218: 811–22. PMID 13295232.