Phosphofructokinase is the principal regulatory enzyme for glycolysis. Gene duplication plus fusion have doubled the size of the eukaryotic enzyme. The smaller enzyme in microbes has versions that may use ATP, ADP, or pyrophosphate as the phosphate donor. These enzymes are normally inhibited by phosphoenolpyruvate and activated by AMP. The larger enzyme uses ATP, and has additional regulatory sites. A special site for fructose-2,6-bisphosphate has resulted in this activator being obligatory for many versions of the enzyme. The larger enzyme is also activated by ADP/AMP, and inhibited by ATP, and citrate.
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© 2008 Springer Science+Business Media, LLC
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(2008). Phosphofructokinase. In: Allosteric Regulatory Enzymes. Springer, Boston, MA. https://doi.org/10.1007/978-0-387-72891-9_8
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DOI: https://doi.org/10.1007/978-0-387-72891-9_8
Publisher Name: Springer, Boston, MA
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