Gluconokinase
In enzymology, a gluconokinase (EC 2.7.1.12) is an enzyme that catalyzes the chemical reaction
- ATP + D-gluconate ADP + 6-phospho-D-gluconate
gluconokinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.1.12 | ||||||||
CAS no. | 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 | ||||||||
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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.
- SABLE HZ, GUARINO AJ (1952). "Phosphorylation of gluconate in yeast extracts". J. Biol. Chem. 196 (1): 395–402. PMID 12980980.