Information on EC 3.6.4.7 - peroxisome-assembly ATPase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.6.4.7
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RECOMMENDED NAME
GeneOntology No.
peroxisome-assembly ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (peroxisome-assembling)
An extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle. Their molecular masses range from 25 to 600 kDa.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
chinese hamster
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
Lon protease homolog 2, peroxisomal; gene NCU08303
UniProt
Manually annotated by BRENDA team
PLN, Lon protease homolog 2, peroxisomal; i.e. Pichia angusta
UniProt
Manually annotated by BRENDA team
strain E122
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-
Manually annotated by BRENDA team
Lon protease homolog 2, peroxisomal
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-casein + H2O
?
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
beta-casein + H2O
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NEM
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in the presence of N-ethylmaleimide, ATPase activity of the peroxisomal AAA-complex is drastically decreased and the complex dissociates; in the presence of N-ethylmaleimide, ATPase activity of the peroxisomal AAA-complex is drastically decreased and the complex dissociates
Pex15
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the membrane anchor required for Pex1/Pex6 recruitment to peroxisomes inhibits the ATP-hydrolysis activity of Pex1/Pex6; the membrane anchor required for Pex1/Pex6 recruitment to peroxisomes inhibits the ATP-hydrolysis activity of Pex1/Pex6
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17 - 0.7
ATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at; assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at; assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
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PAF-1
98000
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about, sequence calculation
104000
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104900
about, sequence calculation
143000
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147000
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7 * 147000, small-angle X-ray scattering, SAXS, analysis
360000
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Pex1p trimeric complex in the presence of ATP, without ATP Pex1p seems to form higher molecular weight structures, most likely aggregates; Pex1p trimeric complex in the presence of ATP, without ATP Pex1p seems to form higher molecular weight structures, most likely aggregates
700000
1100000
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small-angle X-ray scattering, SAXS, analysis
additional information
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for Pex6p, the effect of ATP is not as striking but it is obvious that the yield for monomeric Pex6p is decreased and higher molecular weight species increased, which again might indicate aggregation; for Pex6p, the effect of ATP is not as striking but it is obvious that the yield for monomeric Pex6p is decreased and higher molecular weight species increased, which again might indicate aggregation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heptamer
heterohexamer
homohexamer
oligomer
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homo-oligomer in the cytosol, hetero-oligomer on peroxisome membranes
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
analysis of the crystal structures of the extreme N-terminal part of murine Pex1p exposed a double-psi-beta-barrel fold with similarities to adaptor binding domains of p97 and NSF; analysis of the crystal structures of the extreme N-terminal part of murine Pex1p exposed a double-psi-beta-barrel fold with similarities to adaptor binding domains of p97 and NSF
N-terminal domain, supradomain architecture is a common feature of organellar membrane-associating AAA-ATPases
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme Pln enzyme is sensitive to oxidative damage
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734186
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-purification of recombinant Strep-tagged Pex1 and His6-tagged Pex6 from yeast cells by sequential affinity chromatography on Ni-NTA and streptavidin agarose resins, followed by gel filtration; co-purification of recombinant Strep-tagged Pex1 and His6-tagged Pex6 from yeast cells by sequential affinity chromatography on Ni-NTA and streptavidin agarose resins, followed by gel filtration
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copurification of recombinant FLAG-tagged Pex1 and His-tagged Pex6 from Escherichia coli by tandem-affinity chromatography using Ni-NTA agarose and alpha-FLAG affinity resin, followed by gel filtration; copurification of recombinant FLAG-tagged Pex1 and His-tagged Pex6 from Escherichia coli by tandem-affinity chromatography using Ni-NTA agarose and alpha-FLAG affinity resin, followed by gel filtration
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partially, peroxisomes isolated from rat liver by usual cell fractionation are further purified by immunoisolation using a specific antibody raised against a peroxisomal membrane protein, PMP70
recombinant MBP-fusion enzyme from Escherichia coli strain Rosetta 2 to homogeneity
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recombinant N-terminally His6-tagged and C-terminally GST-tagged Pex1p/His-Pex6p-complex from Escherichia coli strain Tuner(DE3) by nickel affinity chromatography and gel filtration; recombinant N-terminally His6-tagged and C-terminally GST-tagged Pex1p/His-Pex6p-complex from Escherichia coli strain Tuner(DE3) by nickel affinity chromatography and gel filtration
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using glutathione Sepharose
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a GST fusion protein containing the PEX1 gene encoding residues 3-180, the N-terminal domain, in pGEX-4T3-PRESAT is constructed
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AFG1 gene sequenced
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AtLon2 expression profile
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gene At5g47040, DNA and amino acid sequence determination and analysis, isozyme LON2 is encoded by gene aberrant peroxisome morphology 10, apem10
gene Lon1, phylogenetic tree
gene Lonp2, DNA and amino acid sequence determination and analysis, genetic structure
gene Lonp2, phylogenetic tree
gene NCU08303, phylogenetic tree
gene PEX1, functional expression of FLAG-tagged Pex1 in Saccharomyces cerevisiae, FLAG-tagged Pex1 and His-tagged Pex6 coexpression in Escherichia coli; gene PEX6, functional expression of FLAG-tagged Pex6 in Saccharomyces cerevisiae, FLAG-tagged Pex1 and His-tagged Pex6 coexpression in Escherichia coli
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gene PLN, phylogenetic tree, recombinant expression of HpPln, a GFP-PLN hybrid gene under control of the PLN promoter, constructed for the subcellular localization study, coexpression of te peroxisomal marker GFP-SKL in Hansenula polymorpha
gene pln, recombinant expression of GFP-tagged enzyme in GFP-SKL protoplasts, recombinant expression of Pln protein fused to maltose-binding protein (MBP) at the N-terminus and a His6-tag at the C-terminus, with a tobacco etch virus (TEV) cleavage site between MBP and Pln, in Escherichia coli strain Rosetta 2
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gene YALI0F23595g, phylogenetic tree
genes PEX1 and PEX6 cloned by functional complementation of corresponding peroxisome-deficient pex mutants
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organization and cloning of a recombinant Pex1p/Pex6p-complex, recombinant expression of the N-terminally His6-tagged and C-terminally GST-tagged Pex1p/His-Pex6p-complex in Escherichia coli strain Tuner(DE3), ATP-dependence of the Pex1p/Pex6p complex formation; organization and cloning of a recombinant Pex1p/Pex6p-complex, recombinant expression of the N-terminally His6-tagged and C-terminally GST-tagged Pex1p/His-Pex6p-complex in Escherichia coli strain Tuner(DE3), ATP-dependence of the Pex1p/Pex6p complex formation
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overexpression of the pex1p/pex6p complex in Escherichia coli or yeast, the complex assembles in the presence of a nucleotide; overexpression of the pex1p/pex6p complex in Escherichia coli or yeast, the complex assembles in the presence of a nucleotide
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PCR amplification, full-length human PAF-2 cDNA cloned
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PCR-based cDNA cloning of human PAF-2 to identify mutations in the PAF-2 gene of patients using a mammalian expression vector is under way
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peroxisome assembly factor-2 cloned from rat cDNA
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PEX1 and PEX6 genes cloned
PEX1 and PEX6 genes cloned and sequenced
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recombinant coexpression of Pex1 and Pex6 in yeast cells with an N-terminal SBP tag on Pex1 and an N-terminal His14 tag on Pex6; recombinant coexpression of Pex1 and Pex6 in yeast cells with an N-terminal SBP tag on Pex1 and an N-terminal His14 tag on Pex6
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
binding of Pex15p to the Pex1p-Pex6p complex downregulates the ATPase activity of the AAA+-complex, possibly by influencing the D2 AAA+-domain of Pex1p; binding of Pex15p to the Pex1p-Pex6p complex downregulates the ATPase activity of the AAA+-complex, possibly by influencing the D2 AAA+-domain of Pex1p
the expression of PLN is not significantly enhanced in glucose-grown cells upon heat shock as reported for the mitochondrial Lon protease, PIM1, of Saccharomyces cerevisiae
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
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 specifity as the wild-type protein
R135A
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mutant, the conserved arginine surrounded by hydrophobic residues is essential for lipid binding
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine