EC Number   |
Inhibitors |
Structure |
|---|
   3.6.4.7 | more |
Pex1 is completely inhibited when Pex6 is trapped in a permanently ATP-bound state, whereas Pex6 maintains some hydrolysis activity despite an ATP-bound state in Pex1; Pex1 is completely inhibited when Pex6 is trapped in a permanently ATP-bound state, whereas Pex6 maintains some hydrolysis activity despite an ATP-bound state in Pex1 |
 |
| 3.6.4.7 | more |
disassembly of the complex into its Pex1p and Pex6p subunits is observed upon ATP-depletion; disassembly of the complex into its Pex1p and Pex6p subunits is observed upon ATP-depletion |
|
| 3.6.4.7 | NEM |
in the presence of N-ethylmaleimide, ATPase activity of the peroxisomal AAA-complex is drastically decreased and the complex dissociates; in the presence of N-ethylmaleimide, ATPase activity of the peroxisomal AAA-complex is drastically decreased and the complex dissociates |
  |
| 3.6.4.7 | Pex15 |
the membrane anchor required for Pex1/Pex6 recruitment to peroxisomes inhibits the ATP-hydrolysis activity of Pex1/Pex6; the membrane anchor required for Pex1/Pex6 recruitment to peroxisomes inhibits the ATP-hydrolysis activity of Pex1/Pex6 |
|
| 3.6.4.7 | Pex15 |
Pex15 inhibits the ATPase activity of Pex1/Pex6 in a pore-loop-dependent manner because its cytosolic portion is recognized as a substrate |
|
