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Additional recommended knowledge
There are nine known adenylate cyclases in mammals:
Adenylate cyclase catalyzes the conversion of ATP to 3',5'-cyclic AMP (cAMP) and pyrophosphate.
cAMP is an important molecule in eukaryotic signal transduction, a so-called second messenger. Adenylate cyclase can be activated or inhibited by G proteins, which are coupled to membrane receptors and thus can respond to hormonal or other stimuli.
Adenylyl cyclase is a transmembrane protein. It passes through the plasma membrane twelve times.
The important parts for its function are located in the cytoplasm and can be subdivided into the N-terminus, C1a, C1b, C2a and C2b.
The C1 region exists between transmembrane helices six and seven and the C2 region follows transmembrane helix 12.
The C1a and C2a domains form a catalytic dimer where ATP binds and is converted to cAMP.
Adenylate cyclase is stimulated by G proteins, and by forskolin, as well as other class-specific substrates:
In neurons, adenylate cyclases are located next to calcium ion channels for faster reaction to Ca2+ influx; they are suspected of playing an important role in learning processes. This is supported by the fact that adenylate cyclases are coincidence detectors, meaning that they are only activated by several different signals occurring together.
Categories: EC 4.6.1 | Cell signaling | Signal transduction
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Adenylate_cyclase". A list of authors is available in Wikipedia.|