Synonyms
Adenylyl cyclase (preferred); Adenylate cyclase; Adenyl cyclase (original); ATP:pyrophosphate lyase; Cyclizing (E.C.4.6.1.1.)
Definition
Adenosine 3′:5′‐monophosphate (cAMP) regulates effects in all eukaryotic cells, principally through activation of cAMP‐dependent protein kinase (PKA), but also through cAMP‐gated ion channels (CNGs) and select guanine nucleotide exchange factors (Epacs) (Fig. 1). Cellular levels of cAMP levels reflect the balance of activities of adenylyl cyclases (AdCy: 5′‐ATP ⎨ cAMP + PPi) and cAMP phosphodiesterases (PDE: cAMP ⎨ 5′‐AMP). Adenylyl cyclases occur throughout the animal kingdom and play diverse roles in cell regulation [1].
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Abbreviations
- Ado:
-
adenosine
- cAMP:
-
adenosine‐3′:5′ monophosphate
- 2′‐d‐Ado:
-
2′‐deoxyadenosine
- 2′‐d‐2‐F‐Ado:
-
2′‐deoxy‐2‐fluoro‐adenosine
- 3′‐d‐Ado:
-
3′‐deoxyadenosine (cordycepin)
- 2′,5′‐dd‐Ado:
-
2′,5′‐dideoxyadenosine
- 2′,3′‐dd‐Ado:
-
2′,3′‐dideoxyadenosine
- 2′,5′‐dd‐2‐F‐Ado:
-
2′,5′‐dideoxy‐2‐fluoro‐adenosine
- 2′,5′‐dd‐2,5′‐di‐F‐Ado:
-
2′,5′‐dideoxy‐5′‐fluoro‐2‐fluoro‐adenosine
- 9‐CP‐Ade:
-
9‐(cyclopentyl)‐adenine
- 9‐THF‐Ade:
-
9‐(tetrahydrofuryl)‐adenine (SQ22,536)
- 9‐Ara‐Ade:
-
9‐(arabinofuranosyl)‐adenine
- 9‐Xyl‐Ade:
-
9‐(xylofuranosyl)‐adenine
- 2′‐d‐Xyl‐Ade:
-
9‐(2‐deoxyxylosyl)‐adenine
- 2′,5′‐dd‐Xyl‐Ade:
-
9‐(2,5‐dideoxyxylosyl)‐adenine
- 2′‐d‐3′‐AMP:
-
2′‐deoxyadenosine‐3′‐monophosphate
- 2′‐d‐3′‐ADP:
-
2′‐deoxyadenosine‐3′‐diphosphate
- 2′‐d‐3′‐ATP:
-
2′‐deoxyadenosine‐3′‐triphosphate
- 2′‐d‐3′‐AMPS:
-
3′‐(thiophosphoryl)‐2′‐deoxyadenosine
- 2′,5′‐dd‐3′‐AMP:
-
2′,5′‐dideoxyadenosine‐3′‐monophosphate
- 2′,5′‐dd‐3′‐ADP:
-
2′,5′‐dideoxyadenosine‐phos‐phate‐3′‐diphosphate
- 2′,5′‐dd‐3′‐ATP:
-
2′,5′‐dideoxyadenosine‐3′‐triphosphate
- 2′,5′‐dd‐3′‐A4P:
-
2′,5′‐dideoxyadenosine‐phos‐phate‐3′‐tetraphosphate
- 2′,5′‐dd‐3′‐AMPS:
-
3′‐(thiophosphoryl)‐2′,5′‐dideoxyadenosine
- 5′‐APP(CH2)P:
-
adenosine 5′‐(β(‐methylene)‐triphosphate
- β‐L‐5′‐ATP:
-
β‐L‐adenosine‐5′‐triphosphate
- β‐L‐2′,3′‐dd‐5′‐ATP:
-
β‐L‐2′,3′‐dideoxyadenosine‐5′‐triphosphate
- PMEA:
-
9‐[(2‐phosphonylmethoxy(ethyl)]‐adenine
- PMEApp:
-
9‐[(2‐diphosphorylphosphonylmethoxy(ethyl)]‐adenine
- PMEAp(NH)p:
-
9‐[(2‐iminodiphosphorylphosphonylmethoxy(ethyl)]‐adenine
- PMPA:
-
9‐[(2‐phosphonylmethoxy)propyl]‐adenine
- PMPApp:
-
9‐[(2‐diphosphorylphosphonylmethoxy(propyl)]‐adenine
- 2′,5′‐dd‐3′‐AMP‐bis(Me‐SATE):
-
2′,5′‐dideoxyadenosine‐3′‐(acetyl‐2‐thioethyl)‐phosphate
- 2′,5′‐dd‐3′‐AMP‐bis(t‐Bu‐SATE):
-
2′,5′‐dideoxyadenosine‐3′‐(pivaloyl‐2‐thioethyl)‐phosphate
- 2′,5′‐dd‐3′‐AMP‐bis(Ph‐SATE):
-
2′,5′‐dideoxyadenosine‐3′‐(phenyl‐2‐thioethyl)‐phosphate
- 2′,5′‐dd‐2F‐Ado‐3′‐P‐bis(Me‐SATE):
-
2′,5′‐dd‐2‐fluoro‐adenosine‐3′‐(acetyl‐2‐thioethyl)‐phosphate
- MANT‐5′‐GTPγS:
-
3′‐(2′)‐O‐N‐methylanthraniloyl‐guanosine‐5′‐[γ‐thio]triphosphate
- MANT‐5′‐ITPγS:
-
3′‐(2′)‐O‐N‐methylanthraniloyl‐inosine‐5′[γ‐thio]triphosphate
- MANT‐5′ATP:
-
3′‐(2′)‐O‐N‐methylanthraniloyl‐5′‐ATP
- MANT‐5′GTP:
-
3′‐(2′)‐O‐N‐methylanthraniloyl‐5′‐GTP
- 3′‐MANT‐2′‐d‐5′‐ATP:
-
3′‐O‐N‐methylanthraniloyl‐2′‐deoxy‐5′‐ATP
- 3′‐7M4AMC‐2′‐d‐5′‐ATP:
-
3′‐(7‐methoxy‐4‐aminomethylcoumarinn)‐2′‐deoxy‐5′‐ATP
- 3′‐Dansyl‐2′‐d‐5′‐ATP:
-
3′‐(dansyl)‐2′‐deoxy‐5′‐ATP
- 2′,5′‐dd‐3′‐ADP‐(β‐7M4AMC):
-
2′,5′‐dideoxyadenosine‐{β‐(7‐methoxy‐4‐aminomethyl‐coumarin)}‐3′‐diphosphate
- 2′,5′‐dd‐3′‐ATP‐(γ‐7M4AMC):
-
2′,5′‐dideoxyadenosine‐{γ‐(7‐methoxy‐4‐aminomethyl‐coumarin)}‐3′‐triphosphate
- 2′,5′‐dd‐3′‐ATP‐(γ‐7A4AMC):
-
2′,5′‐dideoxyadenosine‐{γ‐(7‐amino‐4‐aminomethyl‐coumarin)}‐3′‐triphosphate
References
Hanoune J, Defer N (2001) Regulation and role of adenylyl cyclase isoforms. Annu Rev Pharmacol Toxicol 41:145–174
Linder JU, Schultz JE (2003) The Class III adenylyl cyclases: multi‐purpose signalling modules. Cell Signal 15:1081–1089
Tesmer JJG, Sunahara RK, Johnson RA et al (1999) Two‐metal‐ion catalysis in adenylyl cyclase. Science 285:756–760
Shoshani I, Boudou V, Pierra C et al (1999) Enzymatic synthesis of unlabeled and [β‐32P]‐labeled β‐L‐2′,3′‐dideoxyadenosine‐5′‐triphosphate as a potent inhibitor of adenylyl cyclases and its use as reversible binding ligand. J Biol Chem 274:34735–34741
Désaubry L, Shoshani I, Johnson RA (1996) Inhibition of adenylyl cyclase by a family of newly synthesized adenine nucleoside 3′‐polyphosphates. J Biol Chem 271:14028–14034
Gille A, Seifert R (2003) 2′(3′)‐O‐(N‐methylanthraniloyl)‐substituted GTP analogs: a novel class of potent competitive adenylyl cyclase inhibitors. J Biol Chem 278:12672–12679
Laux WHG, Pande P, Shoshani I et al (2004) Pro‐nucleotide inhibitors of adenylyl cyclases in intact cells. J Biol Chem 279:13317–13332
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Johnson, R.A. (2008). Adenylyl Cyclases. In: Offermanns, S., Rosenthal, W. (eds) Encyclopedia of Molecular Pharmacology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-38918-7_3
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DOI: https://doi.org/10.1007/978-3-540-38918-7_3
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