EC Number   |
Activating Compound |
Reference |
|---|
   1.14.13.39 | Acetylsalicylic acid |
maximal activation at 0.004 mM |
684277 |
| 1.14.13.39 | Ca2+/calmodulin |
activate the electron transfer |
673804 |
| 1.14.13.39 | Ca2+/calmodulin |
calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electron transfer between NADPH and heme |
674558 |
| 1.14.13.39 | Ca2+/calmodulin |
calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme |
674558 |
| 1.14.13.39 | Calmodulin |
- |
659646, 660022, 764203, 765745 |
| 1.14.13.39 | Calmodulin |
activates O2 consumption of eNOS |
687615 |
| 1.14.13.39 | Calmodulin |
activates the neuronal NOS by binding and inhibiting the suppression through the C-terminal tail of the enzyme, overview |
685120 |
| 1.14.13.39 | Calmodulin |
Ca2+-calmodulin binds between the reductase and oxygenase domains to activate nitric-oxide synthesis. The enzyme adopts an ensemble of open and closed conformational states and that Ca2+-calmodulin binding induces a dramatic rearrangement of the reductase domain. Calmodulin-specific activation triggers release and rotation of the FMN subdomain to expose the flavin for electron transfer to the heme |
745299 |
| 1.14.13.39 | Calmodulin |
in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation. Binding of NADPH and calmodulin influence interdomain distance relationships as well as reaction chemistry. An important effect of calmodulin binding is to suppress adventitious electron transfer from nNOS to molecular oxygen and thereby preventing accumulation of reactive oxygen species |
745293 |
| 1.14.13.39 | Calmodulin |
required |
658405, 658767, 763831 |
