pyruvate kinase

Pyruvate kinase (also: ATP-pyruvate phosphotransferase, EC2.7.1.40) is a glycolytic enzyme that generates ATP by catalyzing the transfer of a phosphoryl group from phosphoenolpyruvate to ADP (Cardenas, 1982; Imamura and Tanaka, 1982; Ikeda and Noguchi, 1998). The majority of pyruvate kinase exists as tetramer and is dissociated into monomeric forms within minutes after cells are deprived of glucose, thus shutting off the glycolytic pathway. Fructose-1,6-bisphosphate is the metabolite in the glycolytic pathway that regulates pyruvate kinase activity (Ashizawa et al, 1991).

Pyruvate kinase is a tetrameric enzyme with subunits encoded by two different genes (Tsutsumi et al, 1988). The structure of the gene has been described by Takenaka et al (1991).

The PKM2 [pyruvate kinase muscle 2 ... ... ... ...
 
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Entry last modified: November 2014