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Literature summary for 3.6.4.7 extracted from

  • Blok, N.B.; Tan, D.; Wang, R.Y.; Penczek, P.A.; Baker, D.; DiMaio, F.; Rapoport, T.A.; Walz, T.
    Unique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy (2015), Proc. Natl. Acad. Sci. USA, 112, E4017-E4025.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome peroxisomal Pex1/Pex6 ATPase complex Saccharomyces cerevisiae 5777
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required 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
-
?

Organism

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

Purification (Commentary)

Purification (Comment) Organism
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 Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O = ADP + phosphate ATP hydrolysis occurs in a unidirectional manner around the ring, with one subunit primarily affecting ATP hydrolysis of only one of the neighboring subunits. ATP binding is initiated on one side of the ring at the nucleotide-free sites where the subunits are most widely spaced Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Saccharomyces cerevisiae ADP + phosphate
-
?
ATP + H2O nucleotide hydrolysis by the ATPase domain of Pex1 Saccharomyces cerevisiae ADP + phosphate
-
?
ATP + H2O nucleotide hydrolysis by the ATPase domain of Pex6 Saccharomyces cerevisiae ADP + phosphate
-
?

Subunits

Subunits Comment Organism
heterohexamer the enzyme complex exhibts a unique double-ring structure, cryo-electron microscopy Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
peroxisomal Pex1/Pex6 ATPase complex
-
Saccharomyces cerevisiae
Pex1
-
Saccharomyces cerevisiae
Pex1/Pex6 complex
-
Saccharomyces cerevisiae
PEX6
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution Pex1 and Pex6 are members of the AAA family of ATPases Saccharomyces cerevisiae
malfunction mutations in the proteins frequently cause peroxisomal diseases Saccharomyces cerevisiae
additional information 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 Saccharomyces cerevisiae
physiological function ATP hydrolysis at both Pex1p/Pex6p complex sites is needed for cell viability Saccharomyces cerevisiae