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Literature summary 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

EC Number Protein Variants Comment Organism
3.4.24.B18 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

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.B18 mitochondrial inner membrane
-
 Saccharomyces cerevisiae 5743
-
3.4.24.B18 mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.B18 protein + H2O Saccharomyces cerevisiae degradation of proteins exposing loops or domain at either sides of the mitochondrial inner membrane peptides
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B18 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.B18 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B18 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 ?
-
 ?
3.4.24.B18 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 ?
-
 ?
3.4.24.B18 protein + H2O degradation of proteins exposing loops or domain at either sides of the mitochondrial inner membrane Saccharomyces cerevisiae peptides
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B18 M41.003 Merops-ID Saccharomyces cerevisiae
3.4.24.B18 mitochondrial AAA protease
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.B18 37
-
-
 Saccharomyces cerevisiae

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.24.B18 additional information
-
 no activity at 25°C, unfolding of Yme2p at 37°C triggers its proteolytic breakdown Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.24.B18 ATP dependent on Saccharomyces cerevisiae