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.