pyrroline-5-carboxylate synthetase |
pyruvate kinase 2 |
60S ribosomal protein L29 |
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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 PKM2 [pyruvate kinase muscle 2; pyruvate kinase M2; also:
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