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  • Title: Phosphorylation of phosphofructokinase by protein kinase C changes the allosteric properties of the enzyme.
    Author: Hofer HW, Schlatter S, Graefe M.
    Journal: Biochem Biophys Res Commun; 1985 Jun 28; 129(3):892-7. PubMed ID: 3160350.
    Abstract:
    The Ca2+- and phospholipid-dependent protein kinase C from rat brain phosphorylates rabbit muscle phosphofructokinase at the same trypsin-labile site as cyclic AMP-dependent protein kinase. However, protein kinase C also effectively phosphorylates one or more separate sites. Incubation of phosphofructokinase in the presence of protein kinase C, phospholipids, Ca2+, and ATP appears to affect the allosteric properties of phosphofructokinase by shifting the fructose 6-phosphate saturation curve to lower substrate concentrations in a time-dependent manner and decreasing cooperativity of the enzyme.
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