EC Number   |
Inhibitors |
Structure |
|---|
   3.6.5.1 | betagamma subunit of the hetreotrimeric G protein |
the beta and gamma subunit of G protein form tightly associated complexes, large number of possible combinations of unique beta and gamma subunits, inhibition of steady-state GTP hydrolysis catalyzed by Gsalpha, Goalpha and myristoylated rGialpha2 |
 |
| 3.6.5.1 | betagamma subunit of the hetreotrimeric G protein |
inhibits by selectively binding to and stabilization of the GDP-bound state |
|
| 3.6.5.1 | GDP |
competitive inhibition |
  |
| 3.6.5.1 | Gpp(NH)p |
competitive inhibition |
|
| 3.6.5.1 | Leu-Gly-Asn repeat-enriched protein |
LGN protein, GDP dissociation inhibitor, GDI, binds to the alpha subunit of transducin in the GDP-bound state |
|
| 3.6.5.1 | more |
GTPase rate is unaffected when transducin alpha-subunit binds to the inhibitory gamma-subunit of cGMP phosphodiesterase, altough this binding is fast and of high affinity |
|
| 3.6.5.1 | more |
GTPase activity of transducin is blocked by ADP-ribosylation |
|
| 3.6.5.1 | more |
tubulin binds to Gs alpha, Gi alpha1 and Gq alpha, destabilize microtubules |
|
| 3.6.5.1 | Pasteurella multocida toxin |
deamidates glutamine-205 of G alphaI2 to glutamic acid, inhibits intrinsic GTPase activity, causes persistent activation of the G protein |
|
| 3.6.5.1 | pertussis toxin |
pertussis toxin-catalysed ADP-ribosylation prevents functional contacts between G-protein-coupled receptors and the Gi-like G-proteins |
|
