Phosphorylation of purified bovine heart and rat liver 6-phosphofructo-2-kinase by protein kinase C and comparison of the fructose-2,6-bisphosphatase activity of the two enzymes.
Purified bovine heart 6-phosphofructo-2-kinase can be phosphorylated in the presence of protein kinase C and dephosphorylated by alkaline phosphatase; changes in phosphorylation state have no effect on enzyme activity. By contrast, the rat liver enzyme is a poor substrate for protein kinase C. Unlike the liver enzyme, which is bifunctional and is phosphorylated by fructose 2,6-[2-32P]bisphosphate, the heart enzyme contains 10 times less fructose 2,6-bisphosphatase activity and is phosphorylated at a slower rate and to a lesser extent than the liver enzyme. Both rat liver and bovine heart enzymes catalyse a similar exchange reaction between [U-14C]ADP and ATP.
D000818:Animals; D002417:Cattle; D007527:Isoenzymes / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology*; D025481:Phosphofructokinase-2; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D010766:Phosphorylation; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000378:metabolism*; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats
D007527:Isoenzymes; D017853:Phosphotransferases (Alcohol Group Acceptor); D025481:Phosphofructokinase-2; D011493:Protein Kinase C; D010744:Phosphoric Monoester Hydrolases