EC Number |
General Information |
Reference |
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3.6.4.7 | metabolism |
a complex of the PEX1 and PEX6 ATPases and the PEX26 tail-anchored membrane protein removes ubiquitinated PEX5 from the peroxisomal membrane |
758016 |
3.6.4.7 | malfunction |
a deletion of peroxisomal Lon results in a specific growth defect on media containing oleic acid as a sole carbon source, conditions which require peroxisomal enzymes of the beta-oxidation pathway, the growth defect is accompanied by the formation of protein aggregates in the peroxisomal matrix |
733421 |
3.6.4.7 | malfunction |
a Lon protease deletion strain does not display a growth defect but a decreased viability of the cells |
733421 |
3.6.4.7 | malfunction |
a mutation of the conserved Walker A lysine in the D1 domain of Pex1, but not Pex6, dramatically affects the recovery of fully assembled recombinant hexamer |
734485 |
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 | physiological function |
ATP hydrolysis at both Pex1p/Pex6p complex sites is needed for cell viability |
735192 |
3.6.4.7 | malfunction |
enzyme complex absence results in the selective degradation of the peroxisome. Loss of the enzyme complex does not prevent matrix protein import, but instead causes an upregulation of peroxisome degradation by macroautophagy, or pexophagy. The loss of enzyme complex function in cells results in the accumulation of ubiquitinated PEX5 on the peroxisomal membrane that signals pexophagy |
755919 |
3.6.4.7 | more |
enzyme Pex1p/Pex6p complex structure modeling using a computational approach that combines Monte Carlo placement of structurally homologous domains into density maps with energy minimization and refinement protocols. Pex1 and Pex6 assemble into hexameric double rings and perform vital functions, structure-function relationship, molecular models. Comparison of the structures of the Pex1/Pex6 complex determined in presence of ATPgammaS and ADP |
735192 |
3.6.4.7 | evolution |
enzymes Pex1 and Pex6 are type-2 AAA+ ATPases |
734485 |
3.6.4.7 | malfunction |
in cells of a PLN deletion strain, peroxisomes contain protein aggregates, a major component of which is catalase-peroxidase. Cells of the pln mutant strain contain enhanced levels of catalase-peroxidase protein but reduced catalase-peroxidase enzyme activities. And the absence of Pln results in the formation of protein aggregates in the peroxisomal matrix |
-, 734186 |