Pyruvate Kinase

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Pyruvate Kinase is the enzyme that catalyses the final stage in glycolysis, changing phosphoenolpyruvate to pyruvate, phosphorylating a molecule of ADP to ATP in the process[1].

This reaction is irreversible in nature due to the large negative free energy change of -17kJmol-1[2].

ATP, a product of the reaction, allosterically inhibits the enzyme, as does the amino acid alanine, slowing the rate of the reaction. The rate of the reaction can be increased by the presence of Fructose 1,6-bisphosphate, a molecule found in the earlier stages of glycolysis[3].

References

  1. ↑ Berg et al. 2007. Biochemistry. New York. W. H. Freeman and Company. p456
  2. ↑ Berg et al. 2007. Biochemistry. New York. W. H. Freeman and Compang. p460
  3. ↑ Berg et al. 2007. Biochemistry. New York. W. H. Freeman and Company. p456
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