Glycerate 2-kinase (, D-glycerate-2-kinase, glycerate kinase (2-phosphoglycerate forming), ATP:(R)-glycerate 2-phosphotransferase) is an enzyme with systematic name ATP:D-glycerate 2-phosphotransferase. It catalyses the following chemical reaction
The enzyme first characterised from Hyphomicrobium methylovorum converts D-glyceric acid to 2-phospho-D-glyceric acid by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). It has been found in many other organisms, including Escherichia coli, Thermoplasma acidophilum, Pyrococcus horikoshii,, Picrophilus torridus, and Sulfolobus tokodaii.
Glycerate 2-kinase is a key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea.
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