Ribulokinase
| ribulokinase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 2.7.1.16 | ||||||
| CAS number | 9030-57-3 | ||||||
| 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 ribulokinase (EC 2.7.1.16) is an enzyme that catalyzes the chemical reaction
- ATP + L(or D)-ribulose
ADP + L(or D)-ribulose 5-phosphate
The 3 substrates of this enzyme are ATP, L-ribulose, and D-ribulose, whereas its 3 products are ADP, L-ribulose 5-phosphate, and D-ribulose 5-phosphate.
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:L(or D)-ribulose 5-phosphotransferase. Other names in common use include ribulokinase (phosphorylating), and L-ribulokinase. This enzyme participates in pentose and glucuronate interconversions.
References
- BURMA DP, HORECKER BL (1958). "Pentose fermentation by Lactobacillus plantarum. III. Ribulokinase". J. Biol. Chem. 231 (2): 1039–51. PMID 13539035.
- Lee N, Bendet I (1967). "Crystalline L-ribulokinase from Escherichia coli". J. Biol. Chem. 242 (9): 2043–50. PMID 5336963.
- Simpson FJ, Wolin MJ and Wood WA (1958). "Degradation of L-arabinose by Aerobacter aerogenes. I. A pathway involving phosphorylated intermediates". J. Biol. Chem. 230 (1): 457–472. PMID 13502414.