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  • Title: Kinetic effects of fructose-1,6-bisphosphate on yeast phosphofructokinase.
    Author: Otto A, Przybylski F, Nissler K, Schellenberger W, Hofmann E.
    Journal: Biomed Biochim Acta; 1986; 45(7):865-75. PubMed ID: 2947575.
    Abstract:
    Yeast phosphofructokinase is known to be effectively activated by fructose-2,6-bisphosphate and AMP. In the absence of the two effectors, fructose-1,6-bisphosphate activates or inhibits the enzyme according to the concentrations of the substrates and of inorganic phosphate. At cellular concentrations of the substrates, however, the effects of fructose-1,6-bisphosphate are negligible. Whereas the activation of the enzyme by AMP is not affected by fructose-1,6-bisphosphate, the latter was found to diminish strongly the activity of the fructose-2,6-bisphosphate-activated enzyme. Inorganic phosphate amplifies the activating effect of fructose-2,6-bisphosphate and augments also the deactivation of the fructose-2,6-bisphosphate-activated enzyme. The deactivating action of fructose-1,6-bisphosphate with respect to fructose-2,6-bisphosphate dominates at low concentrations of fructose-6-phosphate and high levels of ATP and might be of regulatory significance.
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