CAMP activates cAMP-dependent protein kinase by

bindingregulatory subunits and inducing their release from the

catalyticsubunits.

stimulating itsphosphorylation.

stimulating thedimerization of kinase subunits.

stimulating therelease of a translational inhibitory protein

bound to itsmRNA.

binding regulatory subunits and inducing their release from the catalytic subunits

Explanation:

cAMP molecules diffuse into the cytoplasm where they bind to an allosteric site on a regulatory subunit of a cAMP-dependent protein kinase (protein kinase A, PKA).

-In its inactive form, PKA is a heterotetramer comprised of two subunits namely, regulatory (R) and two catalytic (C) subunits.

-The regulatory subunits normally inhibit the catalytic activity of the enzyme. cAMP binding causes the dissociation of the regulatory subunits, thereby releasing the active catalytic subunits of PKA.

-cAMP stimulates glucose mobilization by activating a protein kinase that adds a phosphate group onto a specific serine residue of the glycogen phosphorylase polypeptide.