Glycerate kinase (EC 2.7.1.31) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from liver and Escherichia coli converts D-glyceric acid to 3-phospho-D-glyceric acid by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). This enzyme is a transferases, specifically one 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. Some related enzymes produce the isomeric 2-phospho-D-glyceric acid.
Structural studies As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1TO6, PDB: 1X3L, and PDB: 2B8N.
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