gluconokinase
Gluconokinase homodimer, E.Coli
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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a gluconokinase (EC 2.7.1.12) is an enzyme that catalyzes the chemical reaction

ATP + D-gluconate ${\displaystyle \rightleftharpoons }$ 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.

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.

• COHEN SS (1951). "Gluconokinase and the oxidative path of glucose-6-phosphate utilization". J. Biol. Chem. 189 (2): 617–28. doi:10.1016/S0021-9258(18)44878-8. PMID 14832279.
• LEDER IG (1957). "Hog kidney gluconokinase". J. Biol. Chem. 225 (1): 125–36. doi:10.1016/S0021-9258(18)64915-4. 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. doi:10.1016/S0021-9258(18)65331-1. PMID 13319325.
• SABLE HZ, GUARINO AJ (1952). "Phosphorylation of gluconate in yeast extracts". J. Biol. Chem. 196 (1): 395–402. doi:10.1016/S0021-9258(18)55743-4. PMID 12980980.