SUMMARY: The specific activity of pyruvate kinase is high under conditions of glycolysis but low under conditions of gluconeogenesis. Only a single form of the enzyme was detectable, the properties of which resemble in a number of respects those of the allosteric forms of pyruvate kinase. These properties include co-operative interactions with phosphoenolpyruvate (PEP), ATP and fructose 1,6-diphospate. Fructose 1,6-diphosphate (FDP) almost completely reverses the inhibitory effects of ATP.

The decrease in substrate co-operativity in the presence of FDP, the allosteric activator and the increase in ATP co-operativity in the presence of activator suggests the enzyme can be classed as a ‘K-system’ allosteric protein. The regulatory properties of pyruvate kinase (ATP-pyruvate phosphotransferase, EC are discussed in relation to differences in allosteric pyruvate kinases from other sources.


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