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Literature summary for 3.6.4.7 extracted from

  • Saffian, D.; Grimm, I.; Girzalsky, W.; Erdmann, R.
    ATP-dependent assembly of the heteromeric Pex1p-Pex6p-complex of the peroxisomal matrix protein import machinery (2012), J. Struct. Biol., 179, 126-132.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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 Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
additional information disassembly of the complex into its Pex1p and Pex6p subunits is observed upon ATP-depletion; disassembly of the complex into its Pex1p and Pex6p subunits is observed upon ATP-depletion Saccharomyces cerevisiae
NEM 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 Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.17
-
ATP recombinant Pex1p/Pex6p complex, pH 7.4, 37°C Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome
-
Saccharomyces cerevisiae 5777
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
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 Saccharomyces cerevisiae
360000
-
Pex1p trimeric complex in the presence of ATP, without ATP Pex1p seems to form higher molecular weight structures, most likely aggregates Saccharomyces cerevisiae
700000
-
recombinant Pex1p/Pex6p complex, gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Saccharomyces cerevisiae
-
ADP + phosphate
-
?
additional information Saccharomyces cerevisiae The recombinant AAA-complex exhibits an ATPase activity ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P24004 PEX1
-
Saccharomyces cerevisiae P33760 PEX6
-

Purification (Commentary)

Purification (Comment) Organism
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 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Saccharomyces cerevisiae ADP + phosphate
-
?
additional information The recombinant AAA-complex exhibits an ATPase activity Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
heterohexamer Pex1p and Pex6p interact and form a heterohexameric complex in a one-to-one ratio of both AAA-proteins Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Pex1p
-
Saccharomyces cerevisiae
Pex1p-Pex6p-complex
-
Saccharomyces cerevisiae
Pex6p
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution Pex1p and Pex6p belong to the group of type-II AAA proteins characterized by the presence of two AAA-domains, termed D1 and D2, post-positioned to an N-terminal domain Saccharomyces cerevisiae
additional information Pex1p and Pex6p interact and form a heteromeric complex. Disassembly of the complex into its Pex1p and Pex6p subunits is observed upon ATP-depletion, indicating that formation of the Pex1p/Pex6p-complex requires the presence of ATP Saccharomyces cerevisiae
physiological function the peroxisomal matrix protein import is facilitated by soluble receptor molecules which cycle between cytosol and the peroxisomal membrane. At the end of the receptor cycle, the import receptors are exported back to the cytosol in an ATP-dependent manner catalyzed by a complex of Pex1p and Pex6p Saccharomyces cerevisiae