Ligand 3',5'-cyclic AMP

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Basic Ligand Information

Molecular Structure
Picture of 3',5'-cyclic AMP (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C10H12N5O6P
3',5'-cyclic AMP
IVOMOUWHDPKRLL-KQYNXXCUSA-N
Synonyms:
3',5'-AMP, 3',5'-cAMP, 3',5'-cyclic-AMP, 3'-5'-AMP, 3'5'-cyclic AMP, 3':5'-AMP, 3':5'cAMP, Acrasin, adenosine-3',5'-cyclic monophosphate, adenosine 3',5'-cyclic phosphate, adenosine 3',5'-monophosphate, adenosine 3',5' cyclic monophosphate, adenosine 3':5'-cyclic monophosphate, adenosine cyclic 3'-5'monophosphate, c-3',5'-AMP, c3',5'-AMP, cAMP, cyclic-3',5'-AMP, cyclic 3',5'-AMP, cyclic AMP

Show all pahtways known for Show all pathways known for 3',5'-cyclic AMP

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
3',5'-cAMP + H2O = adenosine monophosphate
show the reaction diagram
-
ATP + H2O + cAMP/in = ADP + phosphate + cAMP/out
show the reaction diagram
-

In Vivo Product in Enzyme-catalyzed Reactions (16 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + cAMP/in = ADP + phosphate + cAMP/out
show the reaction diagram
-
-

Substrate in Enzyme-catalyzed Reactions (35 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
cAMP + H2O = ?
show the reaction diagram
-
cAMP + H2O = ?
show the reaction diagram
-
3',5'-AMP + H2O = ?
show the reaction diagram
cAMP + H2O = ?
show the reaction diagram
-
cyclic 3',5'-AMP + H2O = ?
show the reaction diagram
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cAMP + H2O = ?
show the reaction diagram
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3',5'-cAMP + H2O = 5'-AMP
show the reaction diagram
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3',5'-cyclic AMP + H2O = 5'-AMP
show the reaction diagram
-
3',5'-cyclic AMP + H2O = ?
show the reaction diagram
-
cAMP + H2O = ?
show the reaction diagram
-
3',5'-cyclic AMP + H2O = 3',5'-cyclic IMP + NH3
show the reaction diagram
-
3',5'-cAMP + H2O = adenosine monophosphate
show the reaction diagram
-
ATP + H2O + cAMP/in = ADP + phosphate + cAMP/out
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (23 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + cAMP/in = ADP + phosphate + cAMP/out
show the reaction diagram
-
-

Enzyme Cofactor/Cosubstrate (21 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
stimulates, 0.2-0.8 mM: 2fold
-

Activator in Enzyme-catalyzed Reactions (94 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
stimulation
-
1 mM
-
non-hydrolysable cAMP analog stimulates DBH promoter activity
-
ascites tumour cells
-
induction of isozyme type III from brain astrocytes
-
the activity with CMP and UMP requires activation by cAMP
-
stimulates nuclear diacylglycerol kinase catalytic activity
-
PI 3-kinase is activated in response to cAMP or IGF-I, the PI 3-kinase activity bound to its p85 regulatory subunit increases by 1.7fold. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1
-
PI 3-kinase is activated in response to cAMP or IGF-I, the PI 3-kinase activity bound to its p85 regulatory subunit increases by 1.7fold. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1
-
slight stimulation
-
enzyme activity is induced by
-
less effective than ATP
-
slight activation
-
1 mM, 30°C, pH 7.5, 115% relative activity with glycogen synthase D as substrate
-
1 mM, activity: 106%, isoenzyme 1; 1 mM, activity: 126%, isoenzyme 2
130% activity at 2.5 mM
-
2',3'-cyclic nucleotide phosphodiesterase activity
-
at 1 mM, 273% of control activity
-
binds to N-terminus and GAF domain, affinity of 0.0005 mM; binds to N-terminus and GAF domain, affinity of 0.001 mM
activation is dependent on presence of ATP and a divalent cation such as Mg2+, Mn2+ or Co2+
-
cAMP at 0.010 mM enhances the hydrolytic activity of native AdoHcy-hydrolase by 35%, whereas the activity of the enzyme in its NAD+ form is not stimulated by cAMP. The cAMP-binding site at the AdoHcy-hydrolase is independent of the NAD+/NADH ratio of the enzyme and is identical with the high affinity-binding site of adenosine. cAMP does not interact with the catalytic site of AdoHcyhydrolase and does not act as an allosteric effector
-
weak activation
-
enzyme induction at 5-10 mM
-
maximum activation at concentrations of 1-10 mM
-

Inhibitor in Enzyme-catalyzed Reactions (83 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
coenzyme-competitive inhibitor
-
competitive
-
10% inhibition at 5 mM
-
weak inhibition
-
10 mM, 76% inhibition in the reaction with 0.04 mM 2,6-dichlorophenolindophenol and 0.032 mM NADH
-
no inhibition
-
5 mM, weak inhibition
-
2 mM, slight inhibition
-
4.5 mM: 26% inhibition
-
competitive inhibitor
-
0.5 mM, 20% inhibition of DGK I and 15% inhibition of DGK IV
-
3.5 mM, 20% inhibition
-
strong competitive inhibitor
-
weak
-
less effective than phosphate
-
weak
-
1 mM, 30°C, pH 7.5, 83% remaining activity with histone as substrate and 83% with phosphorylase a
-
3 mM, 86% residual activity
-
IC50: above 0.5 mM
-
19% inhibition at 0.86 mM
-
58% inhibition at 0.1 mM
-
20% inhibition at 3 mM
-
4% inhibition at 2 mM
-
cyclic AMP inhibits the activity and promotes the acetylation of acetyl-CoA synthetase through competitive binding to the highly conserved ATP/AMP binding pocket and restrains SeAcs in an open conformation. cAMP directly binds to the enzyme and inhibits its activity in a substrate-competitive manner. cAMP binding increases SeAcs acetylation by simultaneously promoting Pat-dependent acetylation and inhibiting CobB-dependent deacetylation, resulting in enhanced SeAcs inhibition
inhibits adenylation reaction
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3D Structure of Enzyme-Ligand-Complex (PDB) (27 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (23 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
0.017
-
-
46
-
pH 7.5, 30°C

KM Value (112 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.7
-
-
0.1
-
-
0.5
-
-
0.17
-
pH 7.5, 30°C
14
-
-

Ki Value (13 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.56
-
pH 7.4
0.9
-
-
0.6
-
pH and temperature not specified in the publication
0.4
-
-
0.3
-
-

IC50 Value (4 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.5
-
IC50: above 0.5 mM
0.0012
-
IC50: 1200 nM, PDE11A4

References & Links

Links to other databases for 3',5'-cyclic AMP

ChEBI
PubChem
ChEBI
PubChem