Adenylyl cyclase

Adenylate cyclase
Adenylate cyclase (calmodulin sensitive) trimer, Bacillus anthracis
Epinephrine binds its receptor, that associates with a heterotrimeric G protein. The G protein associates with adenylyl cyclase, which converts ATP to cAMP, spreading the signal.[1]
Identifiers
EC no.4.6.1.1
CAS no.9012-42-4
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MetaCycmetabolic pathway
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Adenylate cyclase (EC 4.6.1.1, also commonly known as adenyl cyclase and adenylyl cyclase, abbreviated AC) is an enzyme with systematic name ATP diphosphate-lyase (cyclizing; 3′,5′-cyclic-AMP-forming). It catalyzes the following reaction:

ATP = 3′,5′-cyclic AMP + diphosphate

It has key regulatory roles in essentially all cells.[2] It is the most polyphyletic known enzyme: six distinct classes have been described, all catalyzing the same reaction but representing unrelated gene families with no known sequence or structural homology.[3] The best known class of adenylyl cyclases is class III or AC-III (Roman numerals are used for classes). AC-III occurs widely in eukaryotes and has important roles in many human tissues.[4]

All classes of adenylyl cyclase catalyse the conversion of adenosine triphosphate (ATP) to 3',5'-cyclic AMP (cAMP) and pyrophosphate.[4] Magnesium ions are generally required and appear to be closely involved in the enzymatic mechanism. The cAMP produced by AC then serves as a regulatory signal via specific cAMP-binding proteins, either transcription factors, enzymes (e.g., cAMP-dependent kinases), or ion transporters.

Adenylyl cyclase catalyzes the conversion of ATP to 3',5'-cyclic AMP.
  1. ^ "PDB101: Molecule of the Month: G Proteins". RCSB: PDB-101. Retrieved 24 August 2020.
  2. ^ Hancock, John (2010). Cell Signaling. pp. 189–195.
  3. ^ Sadana R, Dessauer CW (February 2009). "Physiological roles for G protein-regulated adenylyl cyclase isoforms: insights from knockout and overexpression studies". Neuro-Signals. 17 (1): 5–22. doi:10.1159/000166277. PMC 2790773. PMID 18948702.
  4. ^ a b Zhang G, Liu Y, Ruoho AE, Hurley JH (March 1997). "Structure of the adenylyl cyclase catalytic core". Nature. 386 (6622): 247–253. Bibcode:1997Natur.386..247Z. doi:10.1038/386247a0. PMID 9069282. S2CID 4329051.