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PKA (Protein Kinase A), also known as cAMP-dependent protein kinase, phosphorylates serine or threonine residues in target protein in response to elevated levels of cAMP. Inactive PKA exists as a tetrameric protein composed of two regulatory (R) subunits and two catalytic (C) subunits. Activation occurs when two cAMP molecules bind to each R subunit which causes a conformational change that releases the active C subunits.