Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. Protein kinase A (PKA) refers to a family of enzymes whose activity is dependent on the level of cyclic AMP (cAMP) in the cell, in cell biology. PKA is also known as cAMP-dependent protein kinase EC 2.7.11.11). Protein kinase A has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism. It should neither be confused with AMP-activated protein kinase - which, although being of similar nature, may have opposite effects - nor be confused with Cdks (cyclin-dependent kinases). Each PKA is a holoenzyme that consists of two regulatory and two catalytic subunits. Under low levels of cAMP, the holoenzyme remains intact and is catalytically inactive. When the concentration of cAMP rises (e.g., activation of adenylate cyclases by G protein-coupled receptors coupled to Gs, inhibition of phosphodiesterases that degrade cAMP), cAMP binds to the two binding sites on the regulatory subunits, which leads to the release of the catalytic subunits.

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