EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.1.4.17 | cGMP | binding of cGMP to GAF domains within PDE2 results in the activation of all PDE2 variants | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.4.17 | cGMP | the hydrolysis of cGMP by PDE3 inhibits the hydrolysis of cAMP | Homo sapiens | |
3.1.4.17 | EHNA | a selective PDE2 inhibitor | Homo sapiens | |
3.1.4.53 | rolipram | a selective inhibitor of PDE4 | Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.1.4.17 | membrane | PDE2A2 and PDE2A3, and PDE3A and PDE3B | Homo sapiens | 16020 | - |
3.1.4.17 | soluble | PDE2A1 | Homo sapiens | - |
- |
3.1.4.53 | cytosol | with the exception of one isoform PDE4A, PDE4 enzymes are primarily cytosolic enzymes | Homo sapiens | 5829 | - |
3.1.4.53 | membrane | isozyme PDE4A | Homo sapiens | 16020 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.4.53 | additional information | Homo sapiens | recruitment of PDE4 to the beta2 adrenergic receptor | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.4.17 | Homo sapiens | - |
- |
- |
3.1.4.53 | Homo sapiens | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.1.4.17 | phosphoprotein | in adipocytes, insulin induces formation of macromolecular complexes containing signaling molecules such as IRS-1, PI3K and PKB, proteins involved in PDE3B activation/phosphorylation | Homo sapiens |
3.1.4.53 | phosphoprotein | PDE4 activation is regulated via phosphorylation by PKA in the UCR or phosphorylation by ERK in the C-terminus, depending on the individual isoform | Homo sapiens |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.4.17 | adipocyte | - |
Homo sapiens | - |
3.1.4.17 | cardiac myocyte | - |
Homo sapiens | - |
3.1.4.17 | erythrocyte | - |
Homo sapiens | - |
3.1.4.53 | cardiac myocyte | - |
Homo sapiens | - |
3.1.4.53 | erythrocyte | - |
Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.4.17 | adenosine 3',5'-cyclic phosphate + H2O | - |
Homo sapiens | adenosine 5'-phosphate | - |
? | |
3.1.4.17 | guanosine 3',5'-cyclic phosphate + H2O | - |
Homo sapiens | guanosine 5'-phosphate | - |
? | |
3.1.4.17 | additional information | PDE2 can hydrolyze both cAMP and cGMP with similar maximal rates. PDE1A prefers cGMP, PDE1B cAMP, and PDE1C hydrolyzes both substrates equally. The PDE3 family can hydrolyze both cAMP and cGMP | Homo sapiens | ? | - |
? | |
3.1.4.53 | adenosine 3',5'-cyclic phosphate + H2O | - |
Homo sapiens | adenosine 5'-phosphate | - |
? | |
3.1.4.53 | additional information | recruitment of PDE4 to the beta2 adrenergic receptor | Homo sapiens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.4.17 | cGMP-inhibited PDE | - |
Homo sapiens |
3.1.4.17 | PDE1 | - |
Homo sapiens |
3.1.4.17 | PDE1A | - |
Homo sapiens |
3.1.4.17 | PDE1B | - |
Homo sapiens |
3.1.4.17 | PDE1C | - |
Homo sapiens |
3.1.4.17 | PDE2 | - |
Homo sapiens |
3.1.4.17 | PDE2A1 | - |
Homo sapiens |
3.1.4.17 | PDE2A2 | - |
Homo sapiens |
3.1.4.17 | PDE2A3 | - |
Homo sapiens |
3.1.4.17 | PDE3A | - |
Homo sapiens |
3.1.4.17 | PDE3B | - |
Homo sapiens |
3.1.4.53 | PDE4 | - |
Homo sapiens |
EC Number | Organism | Comment | Expression |
---|---|---|---|
3.1.4.17 | Homo sapiens | epinephrine infusion stimulates skeletal muscle PDE2A expression | up |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.4.17 | metabolism | in adipocytes, insulin induces formation of macromolecular complexes containing signaling molecules such as IRS-1, PI3K and PKB, proteins involved in PDE3B activation/phosphorylation | Homo sapiens |
3.1.4.17 | physiological function | in erythrocytes, PDE3 selectively regulates cAMP synthesis stimulates by activation of the IP receptor. The isoform of PDE1 present in these erythrocytes is primarily involved in hydrolysis of cGMP. The regulated release of ATP from erythrocytes occurs via a defined signaling pathway and requires increases in cAMP. It is well recognized that cAMP is a critical second messenger in diverse signaling pathways. In all cells increases in cAMP are localized and regulated by the activity of phosphodiesterases, PDEs. The subcellular localization of PDEs is recognized to be a key mechanism for compartmentalization of cyclic nucleotide signaling. PDEs within these cells regulate the compartmentalization of cAMP signaling allowing for specific cell responses. The subcellular location of PDEs is critical for coupling these enzymes to specific signal transduction pathways, which permit specific PDEs to regulate local increases in cAMP produced by activation of ligand specific receptor | Homo sapiens |
3.1.4.53 | additional information | PDE4 is a cAMP-specific PDE which has four subfamilies, A thru D, that include over 50 isoforms | Homo sapiens |
3.1.4.53 | physiological function | in cardiac myocytes coupling of PDE4 members to the beta2 adrenergic receptor regulates several aspects of beta2 adrenergic signaling. Inhibition of PDE4 increases cAMP in response to activation of beta2 adrenergic receptors, but has no effect on beta1 adrenergic signaling, demonstrating the selectivity of PDE association. Recruitment of PDE4 to the beta2 adrenergic receptor allows PDE4 to act locally and hydrolyze cAMP produced in response to activation of this receptor, modulating its downstream effects. PDE4 activation is regulated via phosphorylation by PKA in the UCR or phosphorylation by ERK in the C-terminus, depending on the individual isoform. The regulated release of ATP from erythrocytes occurs via a defined signaling pathway and requires increases in cAMP. It is well recognized that cAMP is a critical second messenger in diverse signaling pathways. In all cells increases in cAMP are localized and regulated by the activity of phosphodiesterases, PDEs. The subcellular localization of PDEs is recognized to be a key mechanism for compartmentalization of cyclic nucleotide signaling. PDEs within these cells regulate the compartmentalization of cAMP signaling allowing for specific cell responses. The subcellular location of PDEs is critical for coupling these enzymes to specific signal transduction pathways, which permit specific PDEs to regulate local increases in cAMP produced by activation of ligand specific receptor | Homo sapiens |