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Glycerate kinase : ウィキペディア英語版 | Glycerate kinase
In enzymology, a glycerate kinase () is an enzyme that catalyzes the chemical reaction :ATP + (R)-glycerate 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: serine/glycine/threonine metabolism, glycerolipid metabolism, and glyoxylate-dicarboxylate metabolism. ==Structural studies==
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
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