Adenylate cyclase activity quantifies the enzymatic process responsible for catalyzing the conversion of adenosine triphosphate (ATP) into cyclic adenosine monophosphate (cAMP). This reaction is a foundational element of cellular signal transduction, particularly for many peptide and protein hormones that cannot directly cross the cell membrane. Clinically, this activity is a measure of a cell’s immediate responsiveness to extracellular hormonal cues. Efficient activity is essential for timely and robust physiological responses.
Origin
The term combines adenylate, referring to the adenosine moiety, and cyclase, indicating the enzyme’s function in forming a cyclic molecule. This enzymatic activity was discovered as a key component of the second messenger system, a breakthrough in understanding how hormones exert their effects inside target cells. It belongs to the broader field of molecular endocrinology and cellular biochemistry. The discovery provided a critical link between external signals and internal cellular machinery.
Mechanism
When a hormone binds to its specific G protein-coupled receptor on the cell surface, the associated G protein is activated. The activated alpha subunit of the G protein then directly stimulates the adenylate cyclase enzyme embedded in the plasma membrane. This stimulation rapidly increases the intracellular concentration of cAMP, which acts as a second messenger to initiate a cascade of protein phosphorylation and subsequent cellular responses. This process ultimately translates the external hormonal signal into an internal physiological action.
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