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Literature summary extracted from

  • Reingruber, J.; Holcman, D.
    Estimating the rate constant of cyclic GMP hydrolysis by activated phosphodiesterase in photoreceptors (2008), J. Chem. Phys., 129, 145102.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.4.35 additional information phosphorylation acts in concert with allosteric cGMP binding to stimulate the PDE5 catalytic site, which should promote negative feedback regulation of the cGMP pathway in intact cells Homo sapiens
3.1.4.35 additional information phosphorylation acts in concert with allosteric cGMP binding to stimulate the PDE5 catalytic site, which should promote negative feedback regulation of the cGMP pathway in intact cells Bos taurus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.35
-
 Homo sapiens
3.1.4.35
-
 Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.4.35 tadalafil cGMP modestly but significantly increases the affinity of PDE5 for tadalafil by 1.7fold Bos taurus
3.1.4.35 tadalafil cGMP modestly but significantly increases the affinity of PDE5 for tadalafil by 1.7fold Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.4.35 0.0247
-
 2'-O-anthraniloyl-cGMP phosphorylated PDE5, at 30°C with 50 mM Tris-HCl, pH 7.5 Homo sapiens
3.1.4.35 0.0651
-
 2'-O-anthraniloyl-cGMP unphosphorylated PDE5, at 30°C with 50 mM Tris-HCl, pH 7.5 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.35 Bos taurus
-
-
-
3.1.4.35 Homo sapiens
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.4.35 side-chain modification PDE5 is phosphorylated at Ser102 by cyclic nucleotide-dependent protein kinases, phosphorylation activates PDE5 catalytic site independently of cGMP binding to the allosteric sites Homo sapiens
3.1.4.35 side-chain modification PDE5 is phosphorylated at Ser92 by cyclic nucleotide-dependent protein kinases, phosphorylation activates PDE5 catalytic site independently of cGMP binding to the allosteric sites Bos taurus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.4.35 Ni-NTA agarose column chromatography Homo sapiens
3.1.4.35 Ni-NTA agarose column chromatography Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.35 2'-O-anthraniloyl-cGMP + H2O phosphorylation increases affinity for hydrolysis of 2'-O-anthraniloyl-cGMP by about 3fold Homo sapiens ?
-
 ?
3.1.4.35 2'-O-anthraniloyl-cGMP + H2O phosphorylation increases affinity for hydrolysis of 2'-O-anthraniloyl-cGMP by about 3fold Bos taurus ?
-
 ?
3.1.4.35 3',5'-cGMP + H2O
-
 Homo sapiens 5'-GMP
-
 ?
3.1.4.35 3',5'-cGMP + H2O
-
 Bos taurus 5'-GMP
-
 ?
3.1.4.35 additional information tadalafil is not degraded by PDE5 Homo sapiens ?
-
 ?
3.1.4.35 additional information tadalafil is not degraded by PDE5 Bos taurus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.4.35 PDE5
-
 Homo sapiens
3.1.4.35 PDE5
-
 Bos taurus
3.1.4.35 phosphodiesterase-5
-
 Homo sapiens
3.1.4.35 phosphodiesterase-5
-
 Bos taurus