CAMP activates cAMP-dependent protein kinase by

Biology

1 answer:

Leya [2.2K]3 years ago

4 0

Answer:

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.

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