EC Number   |
Inhibitors |
Structure |
|---|
   7.2.2.13 | oubain |
K+ completely abolishes oubain binding to alpha1-beta1 isoenzymes. Residual oubain binding is still observed at high K+ concentrations for alpha2-beta1 and alpha3-beta1 complexes |
   |
| 7.2.2.13 | oubain |
two apparently different oubain binding sites |
|
| 7.2.2.13 | oubain |
K+ protects against inhibition, probably due to phosphorylating effect |
|
| 7.2.2.13 | oubain |
quantitative aspects of the interaction between oubain and the enzyme in vitro |
|
| 7.2.2.13 | oubain |
half-maximal inhibition at 0.1 mM |
|
| 7.2.2.13 | p-chloro-diphenyl diselenide |
i.e. (p-ClC6H4Se)2, activity is restored by DTT |
|
| 7.2.2.13 | p-methoxyl-diphenyl diselenide |
i.e. (p-CH3OC6H4Se)2, activity is restored by DTT |
|
| 7.2.2.13 | palytoxin |
- |
|
| 7.2.2.13 | palytoxin |
mild, non-toxic, exposures to the Na+/K+-ATPase inhibitor palytoxin synergistically sensitizes the vulnerability of neurons to normally non-toxic concentrations of domoic acid, leaving NMDA receptor-mediated excitotoxic response unaltered. Palytoxin causes a voltage-sensitive Na+ channel-independent increase in intracellular Na+. Enhancement of the excitotoxic response to domoic acid by palytoxin is time-dependent and is not affected by gene expression inhibitors |
|
| 7.2.2.13 | panaxatriol |
- |
|
