EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.4.35 | phosphoprotein |
activation of isoform PDE5 by phosphorylation. PDE5 is dephosphorylated by the catalytic subunit of protein phosphatase 1 but not protein phosphatase 2A |
678974 |
| 3.1.4.35 | phosphoprotein |
phosphorylation presumably by protein kinase A or protein kinase G |
650813 |
| 3.1.4.35 | phosphoprotein |
protein kinase G-mediated phosphorylation up-regulates activity, PP1 phosphatase-mediated dephosphorylation down-regulates activity |
679401 |
| 3.1.4.35 | phosphoprotein |
suPDE5 activity is regulated by phosphorylation. In vitro dephosphorylation of suPDE5 decreases activity by 50% |
670209 |
| 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 |
693333 |
| 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 |
693333 |
