Gluconokinase

From Wikipedia, the free encyclopedia

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

ATP + D-gluconate $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 2.7.1.12
BRENDA references for 2.7.1.12 (Recommended.)
PubMed references for 2.7.1.12
PubMed Central references for 2.7.1.12
Google Scholar references for 2.7.1.12
COHEN SS (1951). "Gluconokinase and the oxidative path of glucose-6-phosphate utilization". J. Biol. Chem. 189: 617–28. PMID 14832279.
LEDER IG (1957). "Hog kidney gluconokinase". J. Biol. Chem. 225: 125–36. PMID 13416223.
Narrod SA and Wood WA (1956). "Carbohydrate oxidation by Pseudomonas fluorescens. V. Evidence for gluconokinase and 2-ketogluconokinase". J. Biol. Chem. 220: 45–55.
SABLE HZ, GUARINO AJ (1952). "Phosphorylation of gluconate in yeast extracts". J. Biol. Chem. 196: 395–402. PMID 12980980.