Phosphoribulokinase
phosphoribulokinase | |||||||||
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Identifiers | |||||||||
EC number | 2.7.1.19 | ||||||||
CAS number | 9030-60-8 | ||||||||
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 / EGO | ||||||||
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In enzymology, a phosphoribulokinase (EC 2.7.1.19) is an enzyme that catalyzes the chemical reaction
- ATP + D-ribulose 5-phosphate 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.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1A7J.
References
- HURWITZ J, WEISSBACH A, HORECKER BL, SMYRNIOTIS PZ (1956). "Spinach phosphoribulokinase". J. Biol. Chem. 218 (2): 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 (2): 811–22. PMID 13295232.