EC Number   |
Activating Compound |
Reference |
|---|
   3.1.4.35 | 8-bromo-cGMP |
- |
653180 |
| 3.1.4.35 | alpha-subunit of transducin |
activation of isoform PDE6 by binding to the inhibitory gamma-subunit |
680735 |
| 3.1.4.35 | alpha-subunit of transducin |
in presence of transducin alpha-subunit-GTP, the inhibitory gamma subunit of PDE6 remains attached to the rest of the PDE6 molecule, but after conversion to transducin alpha-subunit-GDP, the PDE6 gamma subunit may dissociate from PDE6 and exchange with a cytoplasmic pool |
681542 |
| 3.1.4.35 | cGMP |
activation by suggested binding to PDE5 GAF domain |
650813 |
| 3.1.4.35 | cGMP |
allosteric activation |
650180, 679401 |
| 3.1.4.35 | cGMP |
allosteric activation, cGMP binds to F205 in N-terminal GAF-domain of PDE5 |
651322 |
| 3.1.4.35 | cGMP |
cGMP binding to the GAF-A domain is necessary to achieve full activation of PDE5, 3fold activation of blood platelet PDE5 occurs at 0.02 mM cGMP |
713068 |
| 3.1.4.35 | cGMP |
maximal 2.4fold activation below 0.001 mM, half-maximal activation at 0.00016 mM, inhibition above 0.001 mM |
653180 |
| 3.1.4.35 | cGMP |
preincubation with cGMP increases catalytic activity for cGMP degradation, this increase may be caused by binding of cGMP to either the PDE5 allosteric sites, catalytic sites, or both. Full-length GAF-B subdomain conjoined with catalytic domain is sufficient for this conversion |
681583 |
| 3.1.4.35 | cyclic AMP-dependent protein-kinase |
phosphorylates alpha- and beta-subunit |
135360 |
