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Literature summary for 3.4.24.B18 extracted from

  • Leonhard, K.; Guiard, B.; Pellecchia, G.; Tzagoloff, A.; Neupert, W.; Langer, T.
    Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface (2000), Mol. Cell, 5, 629-638.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information construction of chimeric protein substrates: 1. the matrix domain of Yme2p is replaced by mouse dihydrofolate reductase, 2. a chimeric protein consisting of a loosely folded mutant variant of dihydrofolate reductase and the C-terminal end of Yme2p Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane
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Saccharomyces cerevisiae 5743
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mitochondrion
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Saccharomyces cerevisiae 5739
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protein + H2O Saccharomyces cerevisiae degradation of proteins exposing loops or domain at either sides of the mitochondrial inner membrane peptides
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?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
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Reaction

Reaction Comment Organism Reaction ID
proteolytic degradation of proteins overlapping substrate specificity with i-AAA protease EC 3.4.24.B19, mechanism, reaction involves an active extraction of transmembrane segments and transport of solvent-exposed domains across the membrane, inner membrane proteins, active site at the opposite membrane surface Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
mitochondrial integral inner membrane protein Yme2p + H2O wild-type and chimeric mutant containing the dihydrofolate reductase loosely folded mutant, not the one containing the wild-type dihydrofolate reductase, overview, unfolding of the substrate at one side of the membrane might be sufficient for proteolysis, in vitro synthesized protein substrate, imported into the mitochondria, spans the membrane once and exposes large domains at both membrane surfaces Saccharomyces cerevisiae ?
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?
additional information construction of several deletion mutants of Yme2p and investigation of their behaviour as substrates, overview, the folded intermembrane space domain of Yme2p prevents proteolysis but not protease binding at the opposite membrane side Saccharomyces cerevisiae ?
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?
protein + H2O degradation of proteins exposing loops or domain at either sides of the mitochondrial inner membrane Saccharomyces cerevisiae peptides
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?

Synonyms

Synonyms Comment Organism
M41.003 Merops-ID Saccharomyces cerevisiae
mitochondrial AAA protease
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Saccharomyces cerevisiae

Temperature Optimum [°C]

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

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
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no activity at 25°C, unfolding of Yme2p at 37°C triggers its proteolytic breakdown Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Saccharomyces cerevisiae