Glycerate kinase

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

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

or

ATP + (R)-glycerate ${\displaystyle \rightleftharpoons }$ ADP + 2-phospho-(R)-glycerate

Thus, the two substrates of this enzyme are ATP and (R)-glycerate, whereas its two products are ADP and either 3-phospho-(R)-glycerate or 2-phospho-(R)-glycerate.^[1]

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: serine/glycine/threonine metabolism, glycerolipid metabolism, and glyoxylate-dicarboxylate metabolism.

This enzyme had been thought to produce 3-phosphoglycerate, but some glycerate kinases produce 2-phosphoglycerate instead.^[1]

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

• Doughty CC, Hayashi JA, Guenther HL (1966). "Purification and properties of D-glycerate 3-kinase from Escherichia coli". J. Biol. Chem. 241 (3): 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 (2): 949–58. PMID 13416296.