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Literature summary for 3.4.24.B18 extracted from

  • Langer, T.; Kaser, M.; Klanner, C.; Leonhard, K.
    AAA proteases of mitochondria: quality control of membrane proteins and regulatory functions during mitochondrial biogenesis (2001), Biochem. Soc. Trans., 29, 431-436.
    View publication on PubMed
Search for more literature for 3.4.24.B18

Protein Variants

Protein Variants Comment Organism
additional information inactivation of the enzyme impairs respiratory competence Saccharomyces cerevisiae
additional information mutant enzyme variants are sufficient to suppress growth defects of the respective null-mutant cells eukaryota

Inhibitors

Inhibitors Comment Organism Structure
prohibitin located at the periphery of mitochondria at protein import sites, has a regulatory role, deletion of prohibitin leads to accelerated degradation of non-assembled membrane proteins by the m-AAA protease, overexpression of prohibitin stabilizes non-native polypeptides against degradation Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane both subunit types span the membrane twice, integral, active at the matrix side of the inner membrane eukaryota 5743
-
mitochondrial inner membrane both subunit types span the membrane twice, integral, active at the matrix side of the inner membrane Saccharomyces cerevisiae 5743
-
mitochondrial inner membrane integral, active at the matrix side of the inner membrane Saccharomyces cerevisiae 5743
-
mitochondrion
-
 eukaryota 5739
-
mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information conserved metal-binding motif HEXGH at the proteolytic centre Saccharomyces cerevisiae
Zn2+ dependent on eukaryota
Zn2+ dependent on Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 the enzyme is part of a supercomplex in the inner mitochondrial membrane with a native MW of approximately 2000 kDa, assembling with the prohibitin complex Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protein + H2O eukaryota enzyme is essential for cell viability, the enzyme affects the splicing of transcripts of mitochondrial genes encoding essential respiratory complexes and the ATP synthase, degradation of membrane proteins, essentially required as a membrane-integrated quality control, inactivation of AAA proteases cause severe defects in various organisms, including neurodegeneration in humans peptides
-
 ?
protein + H2O Saccharomyces cerevisiae enzyme is essential for cell viability, the enzyme affects the splicing of transcripts of mitochondrial genes encoding essential respiratory complexes and the ATP synthase, degradation of membrane proteins, essentially required as a membrane-integrated quality control, inactivation of AAA proteases cause severe defects in various organisms, including neurodegeneration in humans peptides
-
 ?
protein + H2O Saccharomyces cerevisiae important role in the removal of non-assembled polypeptides from the inner membrane, inactivation of the enzyme is lethal, loss of activity causes respiration-deficiency, affects the splicing of transcripts of mitochondrial genes encoding essential respiratory chain subunits and controls the post-translational asembly of respiratory complexes and the ATP synthase, required as a membrane-integrated quality control to facilitate protein folding and to ensure the selective removal of non-native polypeptides peptides
-
 ?
protein Cob + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?
protein Cox1 + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?
protein Cox3 + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?
protein F0 subunit 6 + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?
protein F0 subunit 8 + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?
protein F0 subunit 9 + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?

Organism

Organism UniProt Comment Textmining
eukaryota
-
 enzyme belongs to the AAA protease family
-
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae
-
 enzyme belongs to the AAA protease family
-

Reaction

Reaction Comment Organism Reaction ID
proteolytic degradation of proteins degradation of hydrophobic membrane-spanning segments of misfolded mitochondrial membrane proteins Saccharomyces cerevisiae
a
proteolytic degradation of proteins 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
proteolytic degradation of proteins mechanism, model, degradation of hydrophobic membrane-spanning segments of misfolded mitochodrial membrane proteins eukaryota
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information shedding model for availability of water molecules: enzyme shed solvent exposed loops or domains from membrane-embedded polypeptides, pulling model: binding of unfolded substrate protein segments together with ATP-dependent conformational changes in the enzyme can provide a pulling force on membrane proteins, with the enzyme being embedded in the bilayer eukaryota ?
-
 ?
protein + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae peptides product peptides in the matrix space are actively transported across the inner membrane by an ABC transporter Mdl1 ?
protein + H2O enzyme probably forms a pore-like structure facilitating the transport of hydrophilic parts of the substrate protein during its extraction, limited substrate recognition Saccharomyces cerevisiae peptides product peptides in the matrix space are actively transported across the inner membrane by an ABC transporter Mdl1 ?
protein + H2O unfoldase activity might be a common property of ATP-dependent proteases eukaryota peptides
-
 ?
protein + H2O enzyme is essential for cell viability, the enzyme affects the splicing of transcripts of mitochondrial genes encoding essential respiratory complexes and the ATP synthase, degradation of membrane proteins, essentially required as a membrane-integrated quality control, inactivation of AAA proteases cause severe defects in various organisms, including neurodegeneration in humans eukaryota peptides
-
 ?
protein + H2O enzyme is essential for cell viability, the enzyme affects the splicing of transcripts of mitochondrial genes encoding essential respiratory complexes and the ATP synthase, degradation of membrane proteins, essentially required as a membrane-integrated quality control, inactivation of AAA proteases cause severe defects in various organisms, including neurodegeneration in humans Saccharomyces cerevisiae peptides
-
 ?
protein + H2O important role in the removal of non-assembled polypeptides from the inner membrane, inactivation of the enzyme is lethal, loss of activity causes respiration-deficiency, affects the splicing of transcripts of mitochondrial genes encoding essential respiratory chain subunits and controls the post-translational asembly of respiratory complexes and the ATP synthase, required as a membrane-integrated quality control to facilitate protein folding and to ensure the selective removal of non-native polypeptides Saccharomyces cerevisiae peptides
-
 ?
protein Cob + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
protein Cox1 + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
protein Cox3 + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
protein F0 subunit 6 + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
protein F0 subunit 8 + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
protein F0 subunit 9 + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?

Subunits

Subunits Comment Organism
? x * 70000-80000, subunits Yta10 and Yta12 in equimolar amounts Saccharomyces cerevisiae
More ATP binding is required for enzyme assembly eukaryota
More formation of a supercomplex between the enzyme and a large complex containing the prohibitin homologues Phb1p and Phb2p, ATP binding is required for enzyme assembly Saccharomyces cerevisiae
More the enzyme consists of an AAA domain, providing chaperone-like properties and binding to the unfolded, solvent-exposed domains of the substrate protein, a proteolytic doamin, and a Walker-type P-loop ATPase domain, both subunits span the membrane twice Saccharomyces cerevisiae
oligomer homooligomer, Class-I and Class-II subunits eukaryota
oligomer homooligomeric, subunits Yta10p and Yta12p, i.e. Afg3p and Rca1p Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
M41.003 Merops-ID eukaryota
M41.003 Merops-ID Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP ATP binding is required for enzyme assembly, enzyme contains conserved Walker-type ATPase domain of approximately 230 amino acids, dependent on eukaryota
ATP ATP binding is required for enzyme assembly, enzyme contains conserved Walker-type ATPase domain of approximately 230 amino acids, dependent on Saccharomyces cerevisiae
ATP dependent on, enzyme contains an ATPase domain with a Walker-type P-loop typical for the AAA protease family, hydrolysis induces conformational changes of the AAA domain driving substrate unfolding and dislocation from the membrane Saccharomyces cerevisiae