cAMPmolekyylin

cAMPmolekyylin, or cyclic adenosine monophosphate, is a crucial second messenger in cellular signal transduction. It is derived from adenosine triphosphate (ATP) through the action of adenylyl cyclase enzymes. Adenylyl cyclase catalyzes the removal of two phosphate groups from ATP and then forms a cyclic bond between the remaining phosphate and the adenosine moiety. The breakdown of cAMP is facilitated by phosphodiesterase enzymes, which hydrolyze the cyclic bond, converting it back to adenosine monophosphate (AMP).

The primary role of cAMP is to activate protein kinase A (PKA). When cAMP levels rise within a cell, it binds to the regulatory subunits of PKA, causing a conformational change that releases the active catalytic subunits. These activated catalytic subunits can then phosphorylate a wide range of target proteins, altering their activity and thereby influencing various cellular processes. These processes include metabolism, gene expression, ion channel function, and cell growth. The rapid and reversible nature of cAMP signaling allows cells to respond quickly to external stimuli. Different cell types and signaling pathways utilize cAMP to mediate diverse physiological responses, making it a versatile and essential signaling molecule.