| 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 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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.
- ^ "PDB101: Molecule of the Month: G Proteins". RCSB: PDB-101. Retrieved 24 August 2020.
- ^ Hancock, John (2010). Cell Signaling. pp. 189–195.
- ^ 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.
- ^ 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.