EC Number   |
Natural Substrates |
|---|
   3.6.4.7 | ATP + H2O |
- |
| 3.6.4.7 | ATP + H2O |
the recombinant Pex1-FLAG/His-Pex6 complex is an active ATPase |
| 3.6.4.7 | more |
AWP1 interacts with Pex6 AAA ATPase, but not with Pex1-Pex6 complexes. The ATPase activity of Pex6 modulates its interaction with AWP1 |
| 3.6.4.7 | more |
in vitro binding assays with GST-fused Pex26p show that Pex1p and Pex6p bind to Pex26p in a manner dependent on ATP binding but not ATP hydrolysis |
| 3.6.4.7 | more |
identification of a peroxisome-specific isoform of Lon protease, an ATP-dependent protease with chaperone-like activity |
| 3.6.4.7 | more |
model of Pex5p export by threading through the central Pex1p-Pex6p pore, overview |
| 3.6.4.7 | more |
Pex1 and Pex6 interact in vivo in an ATP-dependent manner. In the absence of nucleotide, the association of Pex1 with Pex6-FLAG is substantially diminished |
| 3.6.4.7 | more |
Pln is a bifunctional protein with chaperone and protease activities, it acts as an ATP-fueled protease and chaperone. Oxidatively damaged, but not the native protein, is a substrate of the Pln protease |
| 3.6.4.7 | more |
the enzyme degrades soluble unfolded and non-assembled peroxisomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein |
| 3.6.4.7 | more |
The recombinant AAA-complex exhibits an ATPase activity |
