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Literature summary for 3.4.24.B18 extracted from

  • Arnold, I.; Langer, T.
    Membrane protein degradation by AAA proteases in mitochondria (2002), Biochim. Biophys. Acta, 1592, 89-96.
    View publication on PubMed
Search for more literature for 3.4.24.B18

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane integral, active at the matrix side of the inner membrane Saccharomyces cerevisiae 5743
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mitochondrion
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 Saccharomyces cerevisiae 5739
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Metals/Ions

Metals/Ions Comment Organism Structure
additional information a consensus metal-binding site represents the proteolytic centre, metallopeptidase of the M41 family Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protein + H2O Saccharomyces cerevisiae quality control system to selectively remove non-assembled polypeptides and to prevent their possible deleterious accumulation in the membrane, enzyme is crucial for viability 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 mechanism, m-AAA protease shows overlapping substrate specificity with the i-AAA protease, intermolecular catalytic role of SRH domain at the C-terminus of the AAA domain, m-AAA protease shows overlapping substrate specificity with the i-AAA protease, enzyme degrades domains of substrate proteins exposed to the opposite membrane surface, active site contains the conserved motif HEXXH, a helical region is located at the extreme C-terminus of the subunit Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protein + H2O activity depends on oligomerisation Saccharomyces cerevisiae peptides
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 ?
protein + H2O quality control system to selectively remove non-assembled polypeptides and to prevent their possible deleterious accumulation in the membrane, enzyme is crucial for viability Saccharomyces cerevisiae peptides
-
 ?

Subunits

Subunits Comment Organism
More subunits span the membrane twice, activity depends on oligomerisation, the enzyme consists of a AAA domain, providing chaperone-like properties and binding to the unfolded, solvent-exposed domains of the substrate protein, a proteolytic domain, and a Walker-type P-loop ATPase domain Saccharomyces cerevisiae
oligomer x * 70000-80000, homooligomeric Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
M41.003 Merops-ID Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP dependent on, enzyme contains an ATPase domain with a Walker-type P-loop typical for the AAA protease family Saccharomyces cerevisiae