EC Number   |
Inhibitors |
Structure |
|---|
   3.6.5.6 | guanosine 5'-(gamma-thiotriphosphate) |
inhibits both tubulin polymerization and GTP hydrolysis |
   |
| 3.6.5.6 | more |
the phosphorylated protein shows hardly any activity |
|
| 3.6.5.6 | more |
a class of destabilizers consists of the microtubule-severing enzymes from the ATPases associated with various cellular activities (AAA+) family of ATP-enzymes. GTP-driven microtubule dynamics are coupled to ATP-driven destabilization by severing enzymes, examples and mechanism, detailed overview |
|
| 3.6.5.6 | N-ethylmaleimide |
inhibits GTP hydrolysis, but not the assembly reaction |
|
| 3.6.5.6 | N-terminal part of stathimin like-domains |
- |
|
| 3.6.5.6 | NO3- |
- |
|
| 3.6.5.6 | rotenone |
rotenone inhibits both the assembly and the GTP hydrolysis rate of microtubules in vitro |
|
| 3.6.5.6 | tubulin |
unassembled tubulin denatures relatively easily, and the denatured tubulin can inhibit the assembly itself |
|
| 3.6.5.6 | vinblastine |
- |
|
| 3.6.5.6 | vinblastine |
a small molecule inhibitor that binds to tubulin dimers rendering them unable to incorporate into filaments. It does not destabilize actively, but rather inhibit repolymerization after regular depolymerization |
|
