Because the relative amounts of GPa and GPb largely govern the overall process of glycogen breakdown, it is important to understand the controls on the enzymes that interconvert GPa and GPb. Interconversion of GPa and GPb is accomplished by the enzyme Phosphorylase Kinase , which transfers phosphates from 2 ATPs to GPb to form GPa. Phosphorylase kinase is present in a low activity form and a high activity form. The enzyme can be activated by two mechanisms (see HERE ). First, it can be phosphorylated by Protein Kinase A (PKA). Phosphorylation of phosphorylase kinase ACTIVATES the enzyme. (Recall that PKA is activated by cAMP). Another way to activate the enzyme is with calcium. Remember that calcium is also a second messenger in the cell (in addition to cAMP) and can bind to the protein calmodulin. Calmodulin, it turns out, is a subunit of phosphorylase kinase. Activation of phosphorylase kinase by calcium is VERY important in muscle, which uses the ion to trigger musclular contraction. Thus, the same ion that stimulates muscular contraction also activates phosphorylase kinase, which activates glycogen phosphorylase, which releases G1P from glycogen, which can be used to make ATP to support muscular contraction.
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