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Pyruvate kinase is an enzyme that plays a crucial role in glycolysis, the process of breaking down glucose for energy. Specifically, it catalyzes the final step of glycolysis, converting phosphoenolpyruvate (PEP) into pyruvate and generating ATP. This reaction is highly exergonic and virtually irreversible under physiological conditions.1

The activity of pyruvate kinase can be regulated. For instance, it is stimulated by fructose 1,6-diphosphate, which is a product of an earlier step in glycolysis. Conversely, its synthesis can be influenced by dietary factors and hormones like insulin, and its concentration can increase significantly in the liver during starvation to support glucose synthesis.23

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