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
-
frontotemporal
- myopathy
-
paget
- atpases
- sclerosis
-
ibmpfd
-
amyotrophic
-
er-associated
-
misfolded
- inclusions
-
ubiquitin-proteasome
- pex5
-
reticulum-associated
-
polyubiquitinated
-
hexameric
- zellweger
-
ubiquitin-dependent
- proteinopathy
-
lobar
- aaa-atpase
- progranulin
-
proteostasis
- glycosomal
-
pex14p
-
retrotranslocation
-
ubiquitin-positive
- spastin
- cdc48p
-
segregase
- medicine
-
aggresome
-
inclusion-body
- adrenoleukodystrophy
- refsum
-
c9orf72
- pmp70
-
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 (Engineering
Engineering on EC 3.6.4.7 - peroxisome-assembly ATPase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Q144stop
naturally occuring mutation, gene At5g47040 expression is sufficient to rescue the apem10 phenotype, overview
D662N
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Walker-motif mutant: mutant shows a lower level of targeting to EGFP-Pex26p as compared to wild-type
D803N
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Walker-motif mutant: mutant is transported to peroxisomes by EGFP-Pex26p to the same level as wild-type
D940N
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Walker-motif mutant: mutant shows a normal or slightly increased level of targeting to EGFP-Pex26p as compared to wild-type
G843D
K476E
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Walker-motif mutant: mutant shows a lower level of targeting to EGFP-Pex26p as compared to wild-type
K605E
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Walker-motif mutant: mutant are significantly reduced in translocation to EGFP-Pex26p as compared to wild-type
K750E
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Walker-motif mutant: mutant shows a lower level of targeting to EGFP-Pex26p as compared to wild-type
K887E
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Walker-motif mutant: mutant are significantly reduced in translocation to EGFP-Pex26p as compared to wild-type
L664P
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mutation identified in patients with Zellweger syndrome, stable protein, but verly low interaction with Pex6 protein
K174A
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mutant, binds with approximately the same affinity and specificity as the wild-type protein
R135A
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mutant, the conserved arginine surrounded by hydrophobic residues is essential for lipid binding
S815A
T246A
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the mutation of the Pex6 peptide decreases the apparent affinity of Pex1/Pex6 for Pex15 from 0.0006 to 0.002 mM
V245A
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the mutation of the Pex6 peptide decreases the apparent affinity of Pex1/Pex6 for Pex15 from 0.0006 to 0.002 mM
additional information
G843D
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most frequently identified mutation in patients with infantile Refsum disease, protein is rapidly degraded in vivo at 37°C, interaction with Pex6 protein at 50% of wild-type level
G843D
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the mutation of the PEX1 component causes a mild form of peroxisome biogenesis disorder
S815A
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site-directed mutagensis, a single amino acid substitution in the conserved catalytic dyad leads to a proteolytically inactive variant Plnin
S815A
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site-directed mutagensis, a single amino acid substitution in the conserved catalytic dyad leads to a proteolytically inactive variant Plnin
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additional information
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use of the mutants pex6-1 and pex6-1(35S-PEX5) which has decreased resp. elevated PEX5 levels
additional information
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deletion mutant of residues 634-690, identified in patients with Zellweger syndrome, stable protein, but verly low interaction with Pex6 protein
additional information
construction of the various disruption strains of the Hansenula polymorpha PLN gene, the pln deletion cells grow normally like wild-type cells on methanol at 37°C. Growth is also unaffected at elevated growth temperatures (45°C) or upon heat shock
additional information
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construction of the various disruption strains of the Hansenula polymorpha PLN gene, the pln deletion cells grow normally like wild-type cells on methanol at 37°C. Growth is also unaffected at elevated growth temperatures (45°C) or upon heat shock
additional information
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construction of the various disruption strains of the Hansenula polymorpha PLN gene, the pln deletion cells grow normally like wild-type cells on methanol at 37°C. Growth is also unaffected at elevated growth temperatures (45°C) or upon heat shock
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additional information
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. Compared to the ATPase rate of wild-type Pex1/Pex6, this Pex1 D1 Walker A mutant hexamer retains 70% activity. The Pex1 and Pex6 D2 Walker B double mutant shows no ATP-hydrolysis activity. The ATPase rate of the Pex1-WB/Pex6 mutant is very similar to the rate observed for wild-type Pex1/Pex6 at saturating concentrations of tPex15, but unlike for wild-type Pex1/Pex6, no inhibition of Pex1-WB/Pex6 by tPex15 is observed
additional information
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. Compared to the ATPase rate of wild-type Pex1/Pex6, this Pex1 D1 Walker A mutant hexamer retains 70% activity. The Pex1 and Pex6 D2 Walker B double mutant shows no ATP-hydrolysis activity. The ATPase rate of the Pex1-WB/Pex6 mutant is very similar to the rate observed for wild-type Pex1/Pex6 at saturating concentrations of tPex15, but unlike for wild-type Pex1/Pex6, no inhibition of Pex1-WB/Pex6 by tPex15 is observed
additional information
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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. Compared to the ATPase rate of wild-type Pex1/Pex6, this Pex1 D1 Walker A mutant hexamer retains 70% activity. The Pex1 and Pex6 D2 Walker B double mutant shows no ATP-hydrolysis activity. The ATPase rate of the Pex1-WB/Pex6 mutant is very similar to the rate observed for wild-type Pex1/Pex6 at saturating concentrations of tPex15, but unlike for wild-type Pex1/Pex6, no inhibition of Pex1-WB/Pex6 by tPex15 is observed
