Literature summary for 3.4.24.B19 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.

Search for more literature for 3.4.24.B19

Protein Variants

Protein Variants	Comment	Organism
additional information	inactivation of the enzyme causes pleiotropic defects, including impaired respiration and aberrant mitochondrial morphology	Saccharomyces cerevisiae

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	no inhibition by prohibitin	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrial inner membrane	integral, catalytic site facing the intermembrane space	Saccharomyces cerevisiae	5743	-
mitochondrial inner membrane	integral, catalytic site facing the intermembrane space	Neurospora crassa	5743	-
mitochondrial inner membrane	only subunit type Yme1p spans the membrane once, integral, catalytic site facing the inter membrane space	Saccharomyces cerevisiae	5743	-
mitochondrion	-	Saccharomyces cerevisiae	5739	-
mitochondrion	-	Neurospora crassa	5739	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	a consensus metal-binding site represents the proteolytic centre, metallopeptidase of the M41 family	Neurospora crassa
additional information	conserved metal-binding motif HEXGH at the proteolytic centre	Saccharomyces cerevisiae
Zn2+	dependent on	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
protein + H2O	Saccharomyces cerevisiae	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	peptides	-	?
protein + H2O	Neurospora crassa	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	-	?
protein + H2O	Saccharomyces cerevisiae	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	peptides	-	?
protein Cox2 + H2O	Saccharomyces cerevisiae	degradation of membrane protein, essentially required as a membrane-integrated quality control	?	-	?

Organism

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

Reaction

Reaction	Comment	Organism	Reaction ID
proteolytic degradation of proteins	i-AAA protease shows overlapping substrate specificity with the m-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, 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	Neurospora crassa	a
proteolytic degradation of proteins	mechanism, model, degradation of hydrophobic membrane-spanning segments of misfolded mitochodrial membrane proteins	Saccharomyces cerevisiae	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 plling force on membrane proteins, with the enzyme being embedded in the bilayer	Saccharomyces cerevisiae	?	-	?
protein + H2O	activity depends on oligomerisation	Neurospora crassa	peptides	-	?
protein + H2O	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	Saccharomyces cerevisiae	peptides	product peptides are released directly into the intermembrane space	?
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, 25 amino acids of the substrate exposed to the solvent are sufficient for the enzyme to bind via its AAA domain	Saccharomyces cerevisiae	peptides	product peptides are released directly into the intermembrane space	?
protein + H2O	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	Saccharomyces cerevisiae	peptides	-	?
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	Neurospora crassa	peptides	-	?
protein + H2O	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	Saccharomyces cerevisiae	peptides	-	?
protein Cox2 + H2O	degradation of membrane protein, essentially required as a membrane-integrated quality control	Saccharomyces cerevisiae	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 70000-80000, subunit Yme1p	Saccharomyces cerevisiae
More	activity depends on oligomerisation, 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, subunits span the membrane once	Neurospora crassa
More	ATP binding is not necessary for enzyme assembly	Saccharomyces cerevisiae
More	the enzyme consists of a AAA domain, providing chaperone-like properties and binding at its N-terminus to the unfolded, solvent-exposed domains of the substrate protein, a proteolytic doamin, and a Walker-type P-loop ATPase domain, single subunit type Yme1p contains 1 transmembrane segment	Saccharomyces cerevisiae
oligomer	homooligomeric, 1 subunit type Yme1p	Saccharomyces cerevisiae
oligomer	x * 70000-80000, homooligomeric	Neurospora crassa

Synonyms

Synonyms	Comment	Organism
M41.004	Merops-ID	Saccharomyces cerevisiae
M41.004	Merops-ID	Neurospora crassa
Yme1p	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
ATP	ATP binding is not necessary for enzyme assembly, enzyme contains conserved Walker-type ATPase domain of approximately 230 amino acids, dependent on, hydrolysis induces conformational changes	Saccharomyces cerevisiae
ATP	dependent on, enzyme contains an ATPase domain with a Walker-type P-loop typical for the AAA protease family	Neurospora crassa
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

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Release 2023.1 (January 2023)