3.6.4.7: peroxisome-assembly ATPase
This is an abbreviated version!
For detailed information about peroxisome-assembly ATPase, go to the full flat file.
Word Map on EC 3.6.4.7
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3.6.4.7
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proteasome
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dementia
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frontotemporal
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myopathy
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paget
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atpases
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sclerosis
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ibmpfd
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amyotrophic
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er-associated
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misfolded
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inclusions
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ubiquitin-proteasome
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pex5
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reticulum-associated
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polyubiquitinated
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hexameric
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zellweger
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ubiquitin-dependent
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proteinopathy
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lobar
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aaa-atpase
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progranulin
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proteostasis
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glycosomal
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pex14p
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retrotranslocation
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ubiquitin-positive
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spastin
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cdc48p
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segregase
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medicine
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aggresome
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inclusion-body
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adrenoleukodystrophy
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refsum
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c9orf72
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pmp70
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pexophagy
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peroxisome-targeting
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peroxisome-deficient
- 3.6.4.7
- proteasome
- dementia
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frontotemporal
- myopathy
-
paget
- atpases
- sclerosis
-
ibmpfd
-
amyotrophic
-
er-associated
-
misfolded
- inclusions
-
ubiquitin-proteasome
- pex5
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reticulum-associated
-
polyubiquitinated
-
hexameric
- zellweger
-
ubiquitin-dependent
- proteinopathy
-
lobar
- aaa-atpase
- progranulin
-
proteostasis
- glycosomal
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pex14p
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retrotranslocation
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ubiquitin-positive
- spastin
- cdc48p
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segregase
- medicine
-
aggresome
-
inclusion-body
- adrenoleukodystrophy
- refsum
-
c9orf72
- pmp70
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pexophagy
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peroxisome-targeting
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peroxisome-deficient
Reaction
Synonyms
AAA protein, AAA+-ATPase, AAA+-type II ATPase, AAA-ATPase, AAA-complex, AFG1, APEM10, AtLon2, ATP-dependent lon protease, ATPase associated with diverse cellular activities, ATPase associated with various cellular activities, Cdc48, Cdc48p, HpPln, lon, lon protease, LON protease 2, lon2, LONP2, Mm-p, Nc-p, NSF, NSF-like ATPase, p97/VCP, PAF-2, PAS1, PAS1p, PAS8, peroxin, peroxin ATPase complex, peroxisomal AAA ATPase complex, peroxisomal AAA complex, peroxisomal Lon protease, peroxisomal Lon-protease, peroxisomal Pex1/Pex6 ATPase complex, peroxisomal protease LON2, peroxisomal receptor export complex, peroxisome assembly factor-2, peroxisome-assembly ATPase, peroxisome-associated ATPase, Pex1, PEX1/6, Pex1/6 AAA+ complex, Pex1/6 type II AAA+ complex, Pex1/6p-complex, Pex1/Pex6, Pex1/Pex6 complex, Pex1p, Pex1p-Pex6p complex, Pex1p-Pex6p-complex, Pex1p/Pex6p, PEX6, Pex6 AAA ATPase, Pex6p, Pln, REM, SEC18p, TBP1, valosin-containing protein, VCP, Yl-p, Zm-p
ECTree
3.6.4.7 peroxisome-assembly ATPaseAdvanced search results
results (
results (Natural Substrates Products
Natural Substrates Products on EC 3.6.4.7 - peroxisome-assembly ATPase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
the recombinant Pex1-FLAG/His-Pex6 complex is an active ATPase
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?
additional information
?
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AWP1 interacts with Pex6 AAA ATPase, but not with Pex1-Pex6 complexes. The ATPase activity of Pex6 modulates its interaction with AWP1
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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identification of a peroxisome-specific isoform of Lon protease, an ATP-dependent protease with chaperone-like activity
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?
additional information
?
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model of Pex5p export by threading through the central Pex1p-Pex6p pore, overview
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?
additional information
?
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model of Pex5p export by threading through the central Pex1p-Pex6p pore, overview
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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The recombinant AAA-complex exhibits an ATPase activity
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?
additional information
?
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The recombinant AAA-complex exhibits an ATPase activity
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?
additional information
?
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The recombinant AAA-complex exhibits an ATPase activity
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?
additional information
?
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a set of proteins, PEX1, PEX6 and a poorly conserved tail-anchored membrane protein, is required to extract monoubiquitinated PEX5 from the docking/translocation module. The PEX15 fragment is acting as a substrate for PEX1/PEX6
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additional information
?
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the natural substrate for the Pex1p-Pex6p-dependent release is monoubiquitinated Pex5p
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additional information
?
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the Pex1/Pex6 complex acts on ubiquitinated Pex5
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additional information
?
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the Pex1p/Pex6p enzyme complex is able to bind efficiently to Pex15p in vivo. Pex6p mediates binding to the cytosolic part of Pex15p via a direct interaction
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