3.4.24.B19: i-AAA protease
This is an abbreviated version!
For detailed information about i-AAA protease, go to the full flat file.
Word Map on EC 3.4.24.B19
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3.4.24.B19
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intermembrane
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xiap
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survivin
-
proteostasis
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dynamin-like
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degradation
- 3.4.24.B19
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intermembrane
- xiap
- survivin
-
proteostasis
-
dynamin-like
- degradation
Reaction
proteolytic degradation of proteins =
Synonyms
AAA protease, casein lytic proteinase XP, ClpXP, FtsH4, i-AAA Protease, IAP, IAP-1, M41.004, OSD1 protein, TAT-binding homolog 11, YME1, YME1 AAA protease, Yme1L, Yme1p
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3.4.24.B19 i-AAA proteaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.24.B19 - i-AAA protease
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DnaX + H2O
?
-
the enzyme partially degrades DnaX to produce stable fragments upon encountering a glycine-rich region adjacent to a structured domain
-
-
?
hybrid protein of subunit 2 of cytochrome oxidase residues 1-74, mouse dihydrofolate reductase, and mitochondrial presequence, residues 1-66, of subunit 9 of the ATPase of Neurospora crassa + H2O
4 peptide fragments f1-f4
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in vitro import into the mitochondrion
product characterization
?
loosely folded Yta10(161)-dihydrofolate reductase + H2O
?
-
in vitro import into mitochondria, not intact wild-type dihydrofolate reductase
-
?
polynucleotide phosphorylase + H2O
?
-
Yme1 is required for PNPase assembly in the intermembrane space
-
-
?
protein Cox2 + H2O
?
-
degradation of membrane protein, essentially required as a membrane-integrated quality control
-
?
residues 1-74 of subunit 2 of cytochrome oxidase + H2O
?
-
two-step procedure, in vitro import into the mitochondrion
-
?
unassembled gamma subunit of mitochondrial ATP-synthase + H2O
?
-
i.e. Atp3p
-
?
unassembled subunit II of cytochrome oxidase + H2O
?
-
i.e. Cox2p
-
?
protein + H2O
peptides
-
quality control system to selectively remove non-assembled polypeptides and to prevent their possible deleterious accumulation in the membrane, enzyme is crucial for viability
-
?
protein + H2O
peptides
-
ATP hydrolysis causes conformational changes, regulates the accessibility of the proteolytic sites and trigger unfolding of substrate polypeptides, substrate recognition and binding to the enzymes ATPase domain is crucial for proteolytic function against unfolded membrane protein substrates
product peptides are released directly into the intermembrane space
?
protein + H2O
peptides
-
enzyme probably forms a pore-like structure facilitating the transport of hydrophilic parts of the substrate protein during its extraction, limited substrate recognition, 25 amino acids of the substrate exposed to the solvent are sufficient for the enzyme to bind via its AAA domain
product peptides are released directly into the intermembrane space
?
protein + H2O
peptides
-
important role in the removal of non-assembled polypeptides from the inner membrane, inactivation of the enzyme is lethal, enzyme deficiency causes pleiotropic defects, including impaired respiration at high temperature and an aberrant mitochondrial morphology, required as a membrane-integrated quality control to facilitate protein folding and to ensure the selective removal of non-native polypeptides
-
?
protein + H2O
peptides
-
proteolytic activity of the i-AAA protease is required for the maintenance of mitochondrial function at high temperature, pointing to an important role in mitochondrial biogenesis
-
?
protein + H2O
peptides
-
the substrate binding region is mapped to the N-terminus of the AAA domain and is probably close to the membrane surface, degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
Tim17-2 + H2O
?
substrate is an essential component of the mitochondrial TIM17:23 translocase
-
-
?
Tim17-2 + H2O
?
substrate is an essential component of the mitochondrial TIM17:23 translocase
-
-
?
membrane protein + H2O
?
additional information
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proteolytic activity depends on the presence of hydrophobic amino acid residues at position 354 within the pore loop of Yme1
-
-
?
additional information
?
-
-
does not cleave subunit 2 of cytochrome c oxidase
-
-
?
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 plling force on membrane proteins, with the enzyme being embedded in the bilayer
-
?
additional information
?
-
-
polynucleotide phosphorylase-dihydrofolate reductase is not a proteolytic substrate for Yme1
-
-
?
additional information
?
-
Yme1 probably chaperones the folding and/or assembly of Oxa1-exported Cox2 (cytochrome c oxidase subunit) in the absence of Mrg1 or Mgr3
-
-
?
additional information
?
-
-
Yme1 probably chaperones the folding and/or assembly of Oxa1-exported Cox2 (cytochrome c oxidase subunit) in the absence of Mrg1 or Mgr3
-
-
?
additional information
?
-
-
YME1L degradation involves the activity of the ATP-independent mitochondrial protease OMA1
-
-
?
additional information
?
-
-
primary function of Tim9 is to protect Tim10 from degradation by Yme1 via assembly into the Tim9-Tim10 complex
-
-
?
additional information
?
-
-
Yme1p degrades Tim10 more rapidly than Tim9, and loss of Tim10 is accelerated by disruption of conserved disulfide bonds within the substrate. An unstructured N-terminal region of Tim10 is necessary and sufficient to target the substrate to the protease through recognition of a short phenylalanine rich motif
-
-
?
additional information
?
-
-
primary function of Tim9 is to protect Tim10 from degradation by Yme1 via assembly into the Tim9-Tim10 complex
-
-
?
