Phosphorylation of phosphofructokinase by protein kinase C changes the allosteric properties of the enzyme.
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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D000818:Animals; D001921:Brain / Q000201:enzymology; D003488:Cyanogen Bromide / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D010710:Phosphates / Q000378:metabolism; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C; D011494:Protein Kinases / Q000378:metabolism*; D011817:Rabbits; D051381:Rats; D013237:Stereoisomerism; D013820:Thermolysin / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D010710:Phosphates; D011494:Protein Kinases; D010732:Phosphofructokinase-1; D011493:Protein Kinase C; D014357:Trypsin; D013820:Thermolysin; D003488:Cyanogen Bromide