EC Number   |
General Information |
Reference  |
|---|
   3.6.4.7 | evolution |
Arabidopsis contains four Lon protease-like proteins (AtLon1-AtLon4), predicted to be localized in different cellular organelles, including mitochondria, peroxisomes and plastids. AtLon2 is clustered in group II together with several Lon orthologues, which lack putative organelle N-terminal pre-sequences but contain the peroxisomal C-terminal localization signal, suggesting that plant orthologues within this group are localized to the peroxisomes |
682349 |
| 3.6.4.7 | malfunction |
in fibroblasts from patients defective in Pex1, Pex6 and Pex26, (all of which are required for Pex5 export) Pex5 stability is decreased |
721087 |
| 3.6.4.7 | physiological function |
results identify AWP1 as a novel cofactor of Pex6 involved in the regulation of Pex5 export during peroxisome biogenesis |
721087 |
| 3.6.4.7 | evolution |
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases |
733235 |
| 3.6.4.7 | evolution |
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases. Peroxismal Lon protease from Hansenula polymorpha shows 39% sequence identity with the putative peroxisomal Lon protease of Mus musculus |
-, 733235 |
| 3.6.4.7 | malfunction |
the absence of enzyme HpPln affects the viability of cells blocked in pexophagy, but does not affect cell growth. The number of peroxisomes is enhanced in enzyme deletion mutant cells |
-, 733235 |
| 3.6.4.7 | more |
the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789). The ATPase domain in Lon proteases is required for ATP?dependent unfolding of the target protein, prior to degradation by the protease domain |
-, 733235 |
| 3.6.4.7 | physiological function |
most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality |
733235 |
| 3.6.4.7 | physiological function |
most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality, although the enzyme is not important for the viability |
-, 733235 |
| 3.6.4.7 | evolution |
the enzyme belongs to the a member of the Lon-family of proteases in the AAA+ ATPase superfamily, type I AAA+ ATPase |
733421 |
