A number of inactive tetrameric PKA holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. When cAMP binds to two specific binding sites on the regulatory subunits, these undergo a conformational change that causes the dissociation of a dimer of regulatory subunits bound to four cAMP from two monomeric, catalytically active PKA subunits.
|Compartment||plasma membrane , cytosol|
|GO Biological Process||activation of protein kinase A activity (0034199)|
|2165385||cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes||Annu Rev Biochem||1990|