What is an effect of camp-dependent protein kinase (pka) inactivation of the liver isozyme but not the muscle isozyme?

The rate of glucogenesis and lipogenesis would drastically reduce. Protein kinase A acts to phosphorylate many enzymes important in metabolism. In the liver, protein kinase A phosphorylates acetyl-CoA carboxylase and pyruvate dehydrogenase. Such covalent modification has an inhibitory effect on these enzymes, thus inhibiting lipogenesis and promoting net gluconeogenesis. Insulin, on the other hand, decreases the level of phosphorylation of these enzymes, which instead promotes lipogenesis. Recall that gluconeogenesis does not occur in myocytes (muscle cells). Adrenaline and glucagon affect the activity of protein kinase A by changing the levels of cAMP in a cell via the G-protein mechanism, using adenylate cyclase.