Adenyl cyclase

Adenylate cyclase (also known as adenylyl cyclase, AdC or AC) is an important enzyme in the biochemical process of cellular signaling. It is involved in the conversion of adenosine triphosphate (ATP) to cyclic adenosine monophosphate (cAMP) and pyrophosphate.

Function

Adenylate cyclase is a key player in the G protein-coupled receptor (GPCR) signaling pathway. When a ligand binds to a GPCR, it causes a conformational change in the receptor, which allows it to act as a guanine nucleotide exchange factor (GEF). The GEF activity of the GPCR then activates an associated G protein by exchanging the GDP bound to the G protein for a GTP. The α subunit of the G protein, along with the bound GTP, then dissociates from the β and γ subunits and goes on to activate adenylate cyclase.

Structure

Adenylate cyclase is a membrane-bound enzyme and is found in the cellular membrane. It is a complex protein that has several different domains, including two catalytic domains and a regulatory domain. The catalytic domains are responsible for the enzymatic activity of adenylate cyclase, while the regulatory domain is involved in the activation and inhibition of the enzyme.

Clinical significance

Alterations in the function of adenylate cyclase can lead to a variety of diseases. For example, mutations in the gene encoding for adenylate cyclase can result in congenital adrenal hyperplasia, a condition characterized by an overproduction of androgens. Additionally, abnormal activation of adenylate cyclase can lead to the development of certain types of cancer.

See also

• G protein-coupled receptor
• Adenosine triphosphate
• Cyclic adenosine monophosphate
• Cell signaling