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Phosphofructokinase (PFK) is a fundamental enzyme in the glycolytic pathway. As the name suggests, the enzyme acts on the intermediate compound 'phosphofructose'; its proper name being fructose-6-phosphate. The suffix 'kinase' indicates its function as a phosphorylator. The product of this enzyme-subtrate interaction is fructose 1,6 bisphosphate, which subsequently is hydrolysed to glyceralaldehyde 3 phosphate and dihydroxyacetone phosphate[1].

PFK is an allosteric enzyme; meaning that its action is regulated by activator and inhibitor effector molecules; in this case AMP and ATP respectively.

Phosphofructokinase has antagonistic action with the enzyme Fructose 1,6-bisphosphatase; a dephosphorylator[2].


  1. Phosphofructokinase - an overview | ScienceDirect Topics [Internet]. 2017 [cited 3 December 2017]. Available from:
  2. Berg J, Tymoczko J, Stryer L, Clarke N. Biochemistry. New York: W.H. Freeman; 2002.
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