Pyruvate Kinase (PK)

Pyruvate kinase is a key enzyme in cellular metabolism, specifically catalyzing the final step of glycolysis. It facilitates the transfer of a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), resulting in the production of one molecule each of pyruvate and adenosine triphosphate (ATP). This reaction is irreversible and crucial for controlling metabolic flux and ATP generation within cells. There are four main tissue-specific isozymes in mammals: PKM1, PKM2, PKL, and PKR. The M2 isoform (PKM2) is especially notable for its role in both normal proliferating cells and cancer cells, where it supports anabolic metabolism and can regulate gene expression as well as cell cycle progression through non-canonical protein kinase activity. Mutations or dysregulation of pyruvate kinase can lead to various diseases, including pyruvate kinase deficiency causing hemolytic anemia and overexpression/altered function (especially involving PKM2) being associated with cancer progression.

Other names

Pyruvic Kinase

Inhibition of pyruvate kinase activity