Glycerate kinase

From Wikipedia, the free encyclopedia

In enzymology, a glycerate kinase (EC 2.7.1.31) is an enzyme that catalyzes the chemical reaction

ATP + (R)-glycerate $\rightleftharpoons$ ADP + 3-phospho-(R)-glycerate

Thus, the two substrates of this enzyme are ATP and (R)-glycerate, whereas its two products are ADP and 3-phospho-(R)-glycerate.

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:(R)-glycerate 3-phosphotransferase. Other names in common use include glycerate kinase (phosphorylating), D-glycerate 3-kinase, D-glycerate kinase, glycerate-3-kinase, GK, D-glyceric acid kinase, and ATP:D-glycerate 2-phosphotransferase. This enzyme participates in 3 metabolic pathways: glycine, serine and threonine metabolism, glycerolipid metabolism, and glyoxylate and dicarboxylate metabolism.

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

[edit] Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1TO6, 1X3L, and 2B8N.

[edit] References

IUBMB entry for 2.7.1.31
BRENDA references for 2.7.1.31 (Recommended.)
PubMed references for 2.7.1.31
PubMed Central references for 2.7.1.31
Google Scholar references for 2.7.1.31
Doughty CC, Hayashi JA, Guenther HL (1966). "Purification and properties of D-glycerate 3-kinase from Escherichia coli". J. Biol. Chem. 241: 568–72. PMID 5325263.
ICHIHARA A, GREENBERG DM (1957). "Studies on the purification and properties of D-glyceric acid kinase of liver". J. Biol. Chem. 225: 949–58. PMID 13416296.