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Literature summary for 3.4.24.B18 extracted from

  • Gerdes, F.; Tatsuta, T.; Langer, T.
    Mitochondrial AAA proteases - Towards a molecular understanding of membrane-bound proteolytic machines (2012), Biochim. Biophys. Acta, 1823, 49-55.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane
-
Saccharomyces cerevisiae 5743
-
mitochondrion
-
Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae m-AAA protease ensures maturation of cytochrome c peroxidase 1 (Ccp1). The precursor of Ccp1 is dislocated from the inner mitochondrial membrane to allow cleavage by the rhomboid protease Pcp1. Dislocation depends on the ATPase but not the proteolytic activity of the m-AAA protease ?
-
?
MrpL32 + H2O Saccharomyces cerevisiae MrpL32 receives processing by the m-AAA protease after import into the matrix ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information m-AAA protease ensures maturation of cytochrome c peroxidase 1 (Ccp1). The precursor of Ccp1 is dislocated from the inner mitochondrial membrane to allow cleavage by the rhomboid protease Pcp1. Dislocation depends on the ATPase but not the proteolytic activity of the m-AAA protease Saccharomyces cerevisiae ?
-
?
MrpL32 + H2O MrpL32 receives processing by the m-AAA protease after import into the matrix Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
hexamer
-
Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
mitochondrial AAA protease
-
Saccharomyces cerevisiae
Yta10 subunit Saccharomyces cerevisiae
Yta12 subunit Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP intersubunit coordination of the ATP hydrolysis leads to an ordered ATP hydrolysis within the AAA ring, which ensures efficient substrate dislocation from the membrane and translocation to the proteolytic chamber Saccharomyces cerevisiae