3.4.24.64: mitochondrial processing peptidase
This is an abbreviated version!
For detailed information about mitochondrial processing peptidase, go to the full flat file.
Reaction
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
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Synonyms
Alpha-MPP, Atp23, Beta-MPP, EC 3.4.99.41, General mitochondrial processing peptidase, GPP, HA1523, HPP, Imp1, Imp2, inner membrane peptidase processing enzyme, Mas1, Mas2, Matrix peptidase, Matrix processing peptidase, Matrix processing proteinase, Mitochondrial chelator-sensitive protease, mitochondrial processing peptidase, mitochondrial processing peptidase-alpha protein, mitochondrial processing protease, Mitochondrial protein precursor-processing proteinase, MMP-beta, More, MPP, MPP-alpha, P-52, P-55, PEP, Plsp1, Plsp2, PMPCA, Processing enhancing peptidase, processing enhancing protein, processing peptidase, Proteinase, mitochondrial protein precursor-processing, thylakoidal processing peptidase, TPP, TTHA1264
ECTree
General Information
General Information on EC 3.4.24.64 - mitochondrial processing peptidase
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malfunction
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ablation of the enzyme not only affects processing of mitochondrial matrix proteins but also inhibits the import process itself
malfunction
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reducing enzyme activity induces phosphatase and tensin homologue-induced kinase 1 accumulation at the mitochondrial surface, leading to Parkin recruitment and mitophagy
malfunction
analysis of the mas1 mutant (temperature-sensitive mas1 mutant strain in which mitochondrial processing protease (MPP) is inactive when the cells are shifted to growth at nonpermissive temperature (37 °C)) reveales an increase in protein levels of nonprocessed mitochondrial proteins as well as an elevated membrane potential and increased oxygen consumption in mas1 mitochondria upon growth at nonpermissive temperature is observed. These findings might point toward a response in mas1 cells triggered to counterbalance the proteotoxic stress induced by MPP dysfunction
malfunction
mutations in the substrate binding glycine-rich loop of the mitochondrial processing peptidase-alpha protein (PMPCA) cause a severe mitochondrial disease
malfunction
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analysis of the mas1 mutant (temperature-sensitive mas1 mutant strain in which mitochondrial processing protease (MPP) is inactive when the cells are shifted to growth at nonpermissive temperature (37 °C)) reveales an increase in protein levels of nonprocessed mitochondrial proteins as well as an elevated membrane potential and increased oxygen consumption in mas1 mitochondria upon growth at nonpermissive temperature is observed. These findings might point toward a response in mas1 cells triggered to counterbalance the proteotoxic stress induced by MPP dysfunction
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metabolism
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yeast Nfs1 undergoes two steps of proteolytic processing: first it is cleaved by the mitochondrial processing peptidase, MPP, which removes its mitochondrial targeting sequence, and then it is cleaved by a peptidase, designated Icp55, which removes three amino acids from its N-terminus
metabolism
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the enzyme plays a role in phosphatase and tensin homologue-induced kinase 1 (PINK1) import and mitochondrial quality control via the PINK1-Parkin pathway
metabolism
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the thylakoid-transfer signal is required for energy-dependent translocation of preproteins into the thylakoid lumen and is removed by the thylakoidal processing peptidase
physiological function
MPP is involved in the transport of nuclear-encoded proteins from the cytosol into mitochondria
physiological function
MPP plays an essential role in mitochondrial biogenesis and cell proliferation
physiological function
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the mitochondrial processing protease is required in maturation of mitochondrial proproteins for removal of the N-terminal presequences
physiological function
most important processing enzyme that acts on proteins directed to the inner membrane intermembrane space or mitochondrial matrix. Most of the proteins targeted to the mitochondrial matrix or inner membrane present a single cleavage by mitochondrial processing peptidase
physiological function
primary enzyme responsible for the maturation of the vast majority of nuclear-encoded mitochondrial proteins, which is necessary for life at the cellular level. Analysis of lymphoblastoid cells and fibroblasts from patients homozygous for the PMPCA p.Ala377Thr, a mutation in the alpha subunit of mitochondrial processing peptidase and carriers demonstrate that the mutation impacts both the level of the alpha subunit encoded by PMPCA and the function of mitochondrial processing peptidase. This mutation impacts the maturation process of frataxin, the protein which is depleted in Friedreich ataxia
physiological function
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MPP is involved in the transport of nuclear-encoded proteins from the cytosol into mitochondria
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additional information
expression of mppA is developmentally regulated
additional information
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expression of mppA is developmentally regulated