Biology:Gluconokinase
| gluconokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Gluconokinase homodimer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC number | 2.7.1.12 | ||||||||
| CAS number | 9030-55-1 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
In enzymology, a gluconokinase (EC 2.7.1.12) is an enzyme that catalyzes the chemical reaction
- ATP + D-gluconate [math]\displaystyle{ \rightleftharpoons }[/math] ADP + 6-phospho-D-gluconate
Thus, the two substrates of this enzyme are ATP and D-gluconate, whereas its two products are ADP and 6-phospho-D-gluconate.
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-gluconate 6-phosphotransferase. Other names in common use include gluconokinase (phosphorylating), and gluconate kinase. This enzyme participates in pentose phosphate pathway.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1KNQ, 1KO1, 1KO4, 1KO5, 1KO8, and 1KOF.
References
- COHEN SS (1951). "Gluconokinase and the oxidative path of glucose-6-phosphate utilization". J. Biol. Chem. 189 (2): 617–28. PMID 14832279.
- LEDER IG (1957). "Hog kidney gluconokinase". J. Biol. Chem. 225 (1): 125–36. PMID 13416223.
- Narrod SA; Wood WA (1956). "Carbohydrate oxidation by Pseudomonas fluorescens. V. Evidence for gluconokinase and 2-ketogluconokinase". J. Biol. Chem. 220 (1): 45–55. PMID 13319325.
- "Phosphorylation of gluconate in yeast extracts". J. Biol. Chem. 196 (1): 395–402. 1952. PMID 12980980.
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