Adenyl Cyclase

Structure and Function

Adenyl cyclase is a trans membrane protein that catalyzes the breakdown of ATP into 3',5' cyclic AMP (also known as cAMP). Adenylate cyclase is activated by G-proteins, such as the A2A receptor, upstream in the signal. Upon uptake of caffeine into a cell, adenylate cyclase is up regulated resulting in increased synthesis of cAMP from ATP. This results in an overall increase of cAMP in the cell.[1]


Figure 1: The reaction catalyzed by adenyl cyclase. Adenosine triphosphate (ATP) is converted into cyclic adenosine monophosphate (cAMP). Pyrophosphate is the leaving group. Figure created by David Kuang


3',5' cyclic AMP is an important secondary messenger in many transduction pathways. It affects the regulation of homeostasis for many physiological functions including: memory, learning, heart contraction, respiration and lipolysis. cAMP activates protein kinase A and subsequently activates a series of cascading effects that leads to increased lipolysis resulting in increased free fatty acids. cAMP is degraded into 5'-AMP by phosphodiesterases to balance the concentration of cAMP in cells. Increasing the concentration of cAMP has important metabolic effects.[2]

Pathway 1
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  1. ^ Pavan,B., Biondi,C. and Dalpiaz, A. (2009). Drug Discovery Today. 14,982-991.
  2. ^ J.L. Wang et al. (2007). A conformational transition in the adenylyl cyclase catalytic site yields different binding modes for ribosyl-modified and unmodified nucleotide inhibitors. Bioorganic & Medicinal Chemistry. 15, 2993-3002.