Ligand 3',5'-cyclic AMP

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Basic Ligand Information

Molecular Structure

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 pathways known for 3',5'-cyclic AMP

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Roles as Enzyme Ligand

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

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3',5'-cAMP + H2O = adenosine monophosphate

246817

7.6.2.2

ATP + H2O + cAMP/in = ADP + phosphate + cAMP/out

701356

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

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4.6.1.1

15 entries

7.6.2.2

ATP + H2O + cAMP/in = ADP + phosphate + cAMP/out

Substrate in Enzyme-catalyzed Reactions (35 results)

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cAMP + H2O = ?

cAMP + H2O = ?

3',5'-AMP + H2O = ?

cAMP + H2O = ?

cyclic 3',5'-AMP + H2O = ?

cAMP + H2O = ?

3',5'-cAMP + H2O = 5'-AMP

690833, 649785, 669288, 668987

3.1.4.42

3',5'-cyclic AMP + H2O = 5'-AMP

3',5'-cyclic AMP + H2O = ?

246716, 246717, 172176

3.5.4.4

cAMP + H2O = ?

209627

3.5.4.46

3',5'-cyclic AMP + H2O = 3',5'-cyclic IMP + NH3

739775

3.6.1.9

3',5'-cAMP + H2O = adenosine monophosphate

246817

7.6.2.2

ATP + H2O + cAMP/in = ADP + phosphate + cAMP/out

701356

Product in Enzyme-catalyzed Reactions (23 results)

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ATP + H2O + cAMP/in = ADP + phosphate + cAMP/out

Enzyme Cofactor/Cosubstrate (21 results)

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2.7.1.1

stimulates, 0.2-0.8 mM: 2fold

Activator in Enzyme-catalyzed Reactions (94 results)

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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

725279

2.7.1.107

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

slight stimulation

enzyme activity is induced by

645901

3.1.11.5

less effective than ATP

slight activation

1 mM, 30°C, pH 7.5, 115% relative activity with glycogen synthase D as substrate

655958

3.1.3.2

1 mM, activity: 106%, isoenzyme 1; 1 mM, activity: 126%, isoenzyme 2

691171

1z5u, 3D-view

3.1.3.99

130% activity at 2.5 mM

735628

3.1.4.16

2',3'-cyclic nucleotide phosphodiesterase activity

135201

3.1.4.4

at 1 mM, 273% of control activity

653204

3.1.4.53

binds to N-terminus and GAF domain, affinity of 0.0005 mM; binds to N-terminus and GAF domain, affinity of 0.001 mM

678039

2pw3, 3D-view

3.2.1.28

activation is dependent on presence of ATP and a divalent cation such as Mg2+, Mn2+ or Co2+

136162

3.3.1.1

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

729515

5.1.1.13

650894

Inhibitor in Enzyme-catalyzed Reactions (83 results)

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1.1.1.149

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

488252

2.4.1.16

2 mM, slight inhibition

488660

2.4.1.66

4.5 mM: 26% inhibition

636785

2.4.2.14

competitive inhibitor

736283

2.7.1.107

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

210223

3.6.1.9

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

671312