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  • Title: Similarity of activation of yeast phosphofructokinase by AMP and fructose-2,6-bisphosphate.
    Author: Nissler K, Otto A, Schellenberger W, Hofmann E.
    Journal: Biochem Biophys Res Commun; 1983 Feb 28; 111(1):294-300. PubMed ID: 6219673.
    Abstract:
    Phosphofructokinase from yeast is effectively activated by AMP and fructose-2,6-bisphosphate by increasing the affinity of the enzyme to fructose-6-phosphate and the maximum activity toward this substrate. The enzyme is activated by AMP and fructose-2, 6-bisphosphate both at high and at low concentrations of ATP. The half maximum stimulation concentrations of AMP and fructose-2, 6-bisphosphate are about 200 microM and 2 microM, respectively. At saturating concentrations of AMP and fructose-2, 6-bisphosphate similar maximum activities were observed in the dependence of enzyme activity on the concentrations of fructose-6-phosphate. The fructose-6-phosphate affinity is more enhanced by fructose-2, 6-bisphosphate than by AMP.
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