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.
Word Map on EC 3.4.24.64
-
3.4.24.64
-
presequence
-
nuclear-encoded
-
preproteins
-
intermembrane
-
frataxin
-
metalloendopeptidase
-
friedreich
-
matrix-targeting
-
hxxeh
-
mas1
-
plumbaginifolia
-
nuclearly
-
matrix-localized
-
intermediate-sized
-
agriculture
- 3.4.24.64
- presequence
-
nuclear-encoded
- preproteins
-
intermembrane
- frataxin
- metalloendopeptidase
-
friedreich
-
matrix-targeting
-
hxxeh
- mas1
- plumbaginifolia
-
nuclearly
-
matrix-localized
-
intermediate-sized
- agriculture
Reaction
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2 =
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
3.4.24.64 mitochondrial processing peptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.64 - mitochondrial processing peptidase
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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
Abz-FRSGQPLQNKVQLQ-ED(Dnp) + H2O
Abz-FRSGQPLQ + NKVQLQ-ED(Dnp)
-
-
-
?
Abz-MTAALKTK(Dnp)-NH2 + H2O
Abz-MT + AALK + TK(Dnp)-NH2
cleavage sites: 2-aminobenzoyl-MT-/-AALK-/-TK-(N-(2,4-dinitrophenyl)-ethylenediamine)-NH2
-
-
?
Abz-TTKLKAAK(Dnp)-NH2 + H2O
Abz-TTKL + L-Lys + L-Ala + AK(Dnp)-NH2
cleavage sites: 2-aminobenzoyl-TTKL-/-K-/-A-/-AK-(N-(2,4-dinitrophenyl)-ethylenediamine)-NH2
-
-
?
Abz-VRNFRSGQPLQNKVQ-ED(Dnp) + H2O
Abz-VRNFRSGQPLQ + NKVQ-ED(Dnp)
-
-
-
?
ADP/ATP translocator precursor protein + H2O
?
-
from potato, poor substrate
-
-
?
Chimeric preproteins derived from precursor of cytochrome b2 fused to dehydrofolate reductase + H2O
Pb2(1-31) + ib2delta19(167)-DHFR processed protein
-
e.g. pb2delta19(167)-DHFR, cleavage site: Arg30-Xaa31-+-Xaa32, the term -+- depicts the point of cleavage
no further cleavage
?
composite precursor protein Atp25 + H2O
?
-
homologue protein of the bacterial ribosome-silencing factor (Rsf) is generated from the composite precursor protein Atp25 upon internal cleavage by the matrix processing peptidase MPP. In vitro incubation of Atp25 with purified MPP results in three fragments resembling the MTS, the Rsf, and the M domain
-
-
?
Cyclophilin precursor + H2O
Cyclophilin intermediate form
-
cleavage site: Ala36-Phe37
-
?
epidermal growth factor receptor preprotein + H2O
mature epidermal growth factor receptor + prepeptide of epidermal growth factor receptor
frataxin + H2O
mature frataxin 56-210 + prepeptide
-
removal of the N-terminal peptide, MPP cleavage site between residues 55 and 56
the N-terminus of MPP-processed frataxin shows a unique high-affinity iron site, and this iron center appears to mediate a self-cleavage reaction, overview
-
?
MAS1 precursor + H2O
MAS1
-
MAS1 takes part in its own precursor activation
-
?
Methylmalonyl-CoA mutase + H2O
Methylmalonyl-CoA mutase
-
from human
-
?
Mitochondrial alcohol dehydrogenase precursor + H2O
Mitochondrial alcohol dehydrogenase
-
-
-
?
mitochondrial glycerol-3-phosphate dehydrogenase + H2O
processed mitochondrial glycerol-3-phosphate dehydrogenase + prepeptide
mitochondrial malate dehydrogenase precursor + H2O
mitochondrial malate dehydrogenase + mitochondrial malate dehydrogenase transit peptide
mitochondrial matrix protein precursor + H2O
mitochondrial matrix protein + precursor
-
-
-
-
?
MPPI precursor + H2O
MPPI
-
MPPI presumably takes part in its own precursor activation
-
?
Ornithine carbamoyl transferase precursor + H2O
Ornithine carbamoyl transferase intermediate form
P-25 peptide + H2O
?
-
matrix-targeting peptide containing cleavage site of authentic precursor protein
-
-
?
P53 precursor + H2O
P53
-
i.e. subunit II of cytochrome c reductase complex, cleavage site: Tyr32-Ser33
-
?
P55 precursor + H2O
P55
-
i.e. subunit I of cytochrome c reductase complex, cleavage site: Ser32-Ser33
-
?
Precytochrome b2-mouse dehydrofolate reductase fusion protein + H2O
31-aminoacid presequence + cytochrome b2-mouse dehydrofolate reductase protein
presequence-containing protein + H2O
presequence + protein
-
-
-
-
?
processing enhancing protein precursor + H2O
processing enhancing protein + ?
-
-
-
-
?
Rhodanese with added MPP recognition site + H2O
?
-
i.e. R-3 site: Xaa-Arg-Xaa-Tyr-+-Ser/Ala, added after residue 22 of rhodanese, processed to a lesser extent than native precursor proteins, the term-+- depicts the point of cleavage
-
-
?
RPG-Rhodanese with added MPP recognition site + H2O
?
-
i.e. R-3 site: Xaa-Arg-Xaa-Tyr-+-Ser/Ala, added after residue 22 of rhodanese, processed to a lesser extent than native precursor proteins, the term-+- depicts the point of cleavage
-
-
?
Serine-pyruvate aminotransferase precursor + H2O
Serine-pyruvate aminotransferase
-
-
-
?
Ubiquinol-cytochrome c reductase iron-sulfur subunit precursor + H2O
Ubiquinol-cytochrome c reductase iron-sulfur subunit intermediate form
-
Neurospora crassa enzyme
from Neurospora
?
COX IV precursor + H2O
processed COX IV + mitochondrial targeting sequence of COX IV
-
-
-
?
COX IV precursor + H2O
processed COX IV + mitochondrial targeting sequence of COX IV
recombinant C-terminally His-tagged substrate
-
-
?
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
-
tested as fusion protein b2-DFHR
-
?
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
-
-
-
?
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
-
-
-
?
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
-
-
-
?
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
-
-
-
?
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
-
-
-
?
Cytochrome c oxidase subunit IV precursor + H2O
Cytochrome c oxidase subunit IV
-
-
-
-
?
Cytochrome c oxidase subunit IV precursor + H2O
Cytochrome c oxidase subunit IV
-
-
-
?
Cytochrome c oxidase subunit IV precursor + H2O
Cytochrome c oxidase subunit IV
-
-
-
?
Cytochrome c oxidase subunit V precursor + H2O
Cytochrome c oxidase subunit V
-
-
-
?
Cytochrome c oxidase subunit V precursor + H2O
Cytochrome c oxidase subunit V
-
-
-
?
Cytochrome c1 precursor + H2O
Cytochrome c1 intermediate form
-
membrane-bound enzyme
-
-
?
Cytochrome c1 precursor + H2O
Cytochrome c1 intermediate form
-
membrane-bound enzyme
-
?
Cytochrome c1 precursor + H2O
Cytochrome c1 intermediate form
-
membrane-bound enzyme
-
?
epidermal growth factor receptor preprotein + H2O
mature epidermal growth factor receptor + prepeptide of epidermal growth factor receptor
-
-
-
-
?
epidermal growth factor receptor preprotein + H2O
mature epidermal growth factor receptor + prepeptide of epidermal growth factor receptor
-
analysis of the fluorescence resonance energy transfer between EGFP fused to a yeast aconitase presequence and regiospecific 7-dietylamino-3-(4'-maleimidyl phenyl)-4-methyl coumarin-labelled yeast MPPs, overview
-
-
?
F1-ATPase alpha-subunit precursor + H2O
F1-ATPase alpha-subunit
-
-
-
?
F1-ATPase alpha-subunit precursor + H2O
F1-ATPase alpha-subunit
-
-
-
?
F1-ATPase alpha-subunit precursor + H2O
F1-ATPase alpha-subunit
-
-
-
?
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
-
cleavage site: Phe40-Ala41
-
-
?
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
-
-
-
-
?
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
-
-
-
-
?
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
-
F0F1-ATP-synthase F1beta subunit precursor from Neurospora crassa
-
-
?
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
-
F0F1-ATP-synthase F1beta subunit precursor from Nicotiana plumbaginifolia
-
-
?
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
-
no cleavage with isolated enzyme subunits
-
-
?
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
-
F0F1-ATP-synthase F1beta subunit precursor from Neurospora crassa
-
-
?
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
-
F0F1-ATP-synthase F1beta subunit precursor from Nicotiana plumbaginifolia
-
-
?
mitochondrial carrier protein + H2O
?
-
the N-terminal extension of plant mitochondrial carrier proteins is removed by two-step processing. The first cleavage is by the mitochondrial processing peptidase
-
-
?
mitochondrial glycerol-3-phosphate dehydrogenase + H2O
processed mitochondrial glycerol-3-phosphate dehydrogenase + prepeptide
-
-
-
-
?
mitochondrial glycerol-3-phosphate dehydrogenase + H2O
processed mitochondrial glycerol-3-phosphate dehydrogenase + prepeptide
-
arginine residue at the -2 position from the MPP cleavage site, a possible processing site is indicated around residue 40, estimated from deletion experiments
-
-
?
mitochondrial malate dehydrogenase precursor + H2O
mitochondrial malate dehydrogenase + mitochondrial malate dehydrogenase transit peptide
-
-
-
?
mitochondrial malate dehydrogenase precursor + H2O
mitochondrial malate dehydrogenase + mitochondrial malate dehydrogenase transit peptide
-
from rat
-
?
mitochondrial malate dehydrogenase precursor + H2O
mitochondrial malate dehydrogenase + mitochondrial malate dehydrogenase transit peptide
-
from rat
from rat
?
mitochondrial malate dehydrogenase precursor + H2O
mitochondrial malate dehydrogenase + mitochondrial malate dehydrogenase transit peptide
-
the extreme C-terminus of the alpha-subunit of mitochondrial processing peptidase provides mechanical support to the C-terminal domain of the protein during its extensive conformational change accompanying the substrate recognition site
-
-
?
Mitochondrial proteins with artificial precursors + H2O
?
-
cleavage specificity
-
-
?
Mitochondrial proteins with artificial precursors + H2O
?
-
containing presequence of ATPase subunit 9 fused to dehydrofolate reductase, i.e. pre-Su9-DHFR
-
-
?
MLSALARPVGAALARSFSTSA + H2O
?
-
i.e. mouse malate dehydrogenase precursor MDH1-21
-
-
?
MLSALARPVGAALARSFSTSA + H2O
?
-
i.e. mouse malate dehydrogenase precursor MDH1-21
-
-
?
MPP precursor + H2O
MPP
-
i.e. alpha-MPP, processed by the combined mature forms of MPP and processing enhancing protein
i.e. alpha-MPP
?
Nfs1 + H2O
processed Nfs1
-
MPP cleaves the precursor between Phe33 and Tyr34, Nfs1 processing, overview
-
-
?
Nfs1 + H2O
processed Nfs1
-
recombinant His-tagged substrate. Nfs1 is a highly conserved mitochondrial cysteine desulfurase with dual localization in mitochondria and nuclei, mechanism of Nfs1 distribution, overview
-
-
?
nuclear-encoded polyprotein precursor + H2O
?
-
the nuclear-encoded protein RPS14 (ribosomal protein S14) of rice mitochondria is synthesized in the cytosol as a polyprotein consisting of a large N-terminal domain comprising preSDHB (succinate dehydrogenase B precursor) and the C-terminal RPS14. After the preSDHBRPS14 polyprotein is transported into the mitochondrial matrix, the protein is processed into three peptides: the N-terminal prepeptide, the SDHB domain and the C-terminal mature RPS14. MPP (mitochondrial processing peptidase) plays an essential role in processing of the polyprotein. Purified yeast MPP cleaves both the N-terminal presequence and the connector region between SDHB and RPS14. The connector region is processed more rapidly than the presequence. The cleavage site between SDHB and RPS14 is located in an MPPprocessing motif. MPP interacts with multiple sites in the region, possibly in a similar manner to the interaction with the N-terminal presequence. In addition, MPP preferentially recognizes the unfolded structure of preSDHBRPS14. In mitochondria, MPP may recognize the stretched poly-protein during passage of the precursor through the translocational apparatus in the inner membrane, and cleaves the connecting region between the SDHB and RPS14 domains even before processing of the presequence
-
-
?
nuclear-encoded polyprotein precursor + H2O
?
-
the nuclear-encoded protein RPS14 (ribosomal protein S14) of rice mitochondria is synthesized in the cytosol as a polyprotein consisting of a large N-terminal domain comprising preSDHB (succinate dehydrogenase B precursor) and the C-terminal RPS14. After the preSDHBRPS14 polyprotein is transported into the mitochondrial matrix, the protein is processed into three peptides: the N-terminal prepeptide, the SDHB domain and the C-terminal mature RPS14. MPP (mitochondrial processing peptidase) plays an essential role in processing of the polyprotein. Purified yeast MPP cleaves both the N-terminal presequence and the connector region between SDHB and RPS14. The connector region is processed more rapidly than the presequence. The cleavage site between SDHB and RPS14 is located in an MPP processing motif. MPP interacts with multiple sites in the region, possibly in a similar manner to the interaction with the N-terminal presequence. In addition, MPP preferentially recognizes the unfolded structure of preSDHBRPS14. In mitochondria, MPP may recognize the stretched poly-protein during passage of the precursor through the translocational apparatus in the inner membrane, and cleaves the connecting region between the SDHB and RPS14 domains even before processing of the presequence
-
-
?
Ornithine carbamoyl transferase precursor + H2O
Ornithine carbamoyl transferase intermediate form
-
-
-
-
?
Ornithine carbamoyl transferase precursor + H2O
Ornithine carbamoyl transferase intermediate form
-
EC 2.1.3.3, from rat
-
-
?
Ornithine carbamoyl transferase precursor + H2O
Ornithine carbamoyl transferase intermediate form
-
EC 2.1.3.3, from human
-
-
?
pea glutathione reductase + H2O
?
-
signal peptide is cleaved off by the mitochondrial processing peptidase. Removal of 30 N-terminal amino acid residues of the signal peptide (GRD130) greatly stimulates processing activity. Constructs with a deletion of an additional ten amino acid residues (GRD140) and deletion of 22 amino acid residues in the middle of the GR signal sequence (GRD3052) are not celeaved by MPP. Mutations within two amino acid residues on either side of the processing site have inhibitory effect on processing by MPP with a nearly complete inhibition for mutations at position K1. Mutation of positively charged residues in the C-terminal half of the GR targeting peptide inhibit processing by MPP
-
-
?
plant mitochondrial carrier proteins + H2O
?
-
yeast mitochondria process the plant mitochondrial carrier protein to the same intermediate size as purified plant MPP. This intermediary processing does not occur in a temperature sensitive yeast mutant for MPP at the restrictive temperature
-
-
?
plant mitochondrial carrier proteins + H2O
?
-
yeast mitochondria process the plant mitochondrial carrier protein to the same intermediate size as purified plant MPP. This intermediary processing does not occur in a temperature sensitive yeast mutant for MPP at the restrictive temperature
-
-
?
pre-F1FO-ATP synthase + H2O
mature F1FO-ATP synthase + prepeptide
-
on one hand, Atp23 serves as a processing peptidase and mediates the maturation of the mitochondrially-encoded FO-subunit Atp6 after its insertion into the inner membrane, on the other hand, independent of its proteolytic activity, Atp23 promotes the association of mature Atp6 with Atp9 oligomers with chaperone activity, overview, the assembly step is thus under the control of two substrate-specific chaperones, Atp10 and Atp23, which act on opposite sides of the inner membrane, modelling of assembly, overview
-
-
?
pre-F1FO-ATP synthase + H2O
mature F1FO-ATP synthase + prepeptide
-
putative catalytically active Glu168
-
-
?
Precytochrome b2-mouse dehydrofolate reductase fusion protein + H2O
31-aminoacid presequence + cytochrome b2-mouse dehydrofolate reductase protein
-
i.e. artificial fusion protein containing 22 amino acid presequence of cytochrome oxidase subunit IV fused to mouse dehydrofolate reductase, substitution of Arg2 or Tyr1 of matrix targeting sequence of cytochrome b2 prevents processing
-
?
Precytochrome b2-mouse dehydrofolate reductase fusion protein + H2O
31-aminoacid presequence + cytochrome b2-mouse dehydrofolate reductase protein
-
-
-
-
?
preprotein Din7 + H2O
presequence + protein Din7
-
-
-
?
preprotein Din7 + H2O
presequence + protein Din7
-
-
-
?
preprotein Mrx8 + H2O
presequence + protein Mrx8
-
-
-
?
preprotein Mrx8 + H2O
presequence + protein Mrx8
-
-
-
?
preprotein Yhb1 + H2O
presequence + protein Yhb1
-
-
-
?
preprotein Yhb1 + H2O
presequence + protein Yhb1
-
-
-
?
Processing enhancing protein precursor + H2O
Processing enhancing protein
-
processed by the combined mature forms of MPP and processing enhancing protein
i.e. PEP
?
Processing enhancing protein precursor + H2O
Processing enhancing protein
-
processed by the combined mature forms of MPP and processing enhancing protein
i.e. PEP
?
Processing enhancing protein precursor + H2O
Processing enhancing protein
-
i.e. PEP precursor, takes part in its own precursor activation
i.e. PEP
?
Rieske FES protein precursor + H2O
Rieske FES protein intermediate form
-
-
from Neurospora
?
Rieske FES protein precursor + H2O
Rieske FES protein intermediate form
-
from Neurospora
from Neurospora
?
Rieske FES protein precursor + H2O
Rieske FES protein intermediate form
-
from Neurospora
-
-
?
Rieske FES protein precursor + H2O
Rieske FES protein intermediate form
-
from Neurospora
-
-
?
additional information
?
-
-
mitosomal substrates of the enzyme are processed to mature proteins in Antonospora locustae with a simplified processing complex, overview
-
-
?
additional information
?
-
-
no activity with the mitochondrial glycerol-3-phosphate dehydrogenase from Encephalitozoon cuniculi
-
-
?
additional information
?
-
-
isoform Plsp1 forms a stable complex with PGRL1 in Arabidopsis thylakoids
-
-
?
additional information
?
-
-
mitochondrial processing peptidase is essential for viability of Caenorhabditis elegans
-
-
?
additional information
?
-
-
does cleave 4 out of 4 mitosomal substrates, does not cleave 0 out of 4 hydrogenosomal presequences and 0 out of 3 mitochondrial presequences
-
-
?
additional information
?
-
-
the mitochondrial processing peptidase removes leader peptides of preproteins after import into the mitochondrial matrix space to increase protein stability, enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space, overview
-
-
?
additional information
?
-
-
binding of the iron-promoted binding of the iron-sulfur cluster assembly scaffold partner protein, ISU, overview
-
-
?
additional information
?
-
-
the enzyme specifically cleaves off presequences from mitochondrial precursor proteins
-
-
?
additional information
?
-
the enzyme shows a preference for uncharged polar residues at positions P1 and P1 and nonpolar residues at the substrate P3, P2, P2' and P3' positions
-
-
?
additional information
?
-
-
several chloroplast precursor proteins from wheat or Silene pratense
-
-
?
additional information
?
-
-
processing activity is optimal at a 1:1 molar ratio of alpha- and beta-MPP
-
-
?
additional information
?
-
-
MPP alone has a low processing activity, processing enhancing protein alone has none, upon recombining both, full processing activity is restored, both proteins cooperate in binding precursor substrates and proteolytic activity, the latter is associated with the MPP protein (MW 57000)
-
-
?
additional information
?
-
-
The mitochondrial processing peptidase from Neurospora crassa consists of two components: MPP and processing enhancing protein
-
-
?
additional information
?
-
-
comparison of MPP and pea stromal processing peptidase specificity
-
-
?
additional information
?
-
-
plays an essential role in mitochondrial protein import
-
?
additional information
?
-
-
thiolase with added R-3 MPP recognition site, rhodanese with RPG-linker (i.e. 3 amino acid linker of aldehyde dehydrogenase precursor), linker deleted aldehyde dehydrogenase
-
-
?
additional information
?
-
-
No substrates are mitochondrial matrix proteins lacking cleavable signal sequences, e.g. 3-oxoacyl-CoA thiolase, rhodanese
-
-
?
additional information
?
-
-
precursor substrates must be synthesized by translation in a mRNA-dependent in vitro translation system, e.g. nuclease-treated rabbit reticulocyte lysate
-
-
?
additional information
?
-
-
No substrates are cytochrome P-450 catalyzing side chain cleavage of cholesterol and of cytochrome P450 catalyzing 11beta-hydroxylation of steroids
-
-
?
additional information
?
-
-
No substrates are denatured enzyme precursors
-
-
?
additional information
?
-
-
No substrates are precursors of carbamoyl phosphate synthetase I, in vitro synthesized 3-ketoacyl-CoA thiolase (EC 2.3.1.16), carnitine palmitoyl transferase (EC 2.3.1.23), carnitine acyltransferase (EC 2.3.1.7)
-
-
?
additional information
?
-
-
removes amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins during or after translocation across mitochondrial membranes
-
-
?
additional information
?
-
-
removes amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins during or after translocation across mitochondrial membranes
-
-
?
additional information
?
-
-
polypeptides destined to be imported from cytosol into mitochondrial matrix or inner mitochondrial membrane, critical step in the import of nuclear encoded precursor proteins into mitochondria
-
-
?
additional information
?
-
-
plays an essential role in mitochondrial protein import
-
?
additional information
?
-
-
the large subunit alone has no cleavage activity
-
-
?
additional information
?
-
-
alpha-MPP (formerly MAS2) alone has no catalytic activity
-
-
?
additional information
?
-
-
No substrates are several non-mitochondrial proteins
-
-
?
additional information
?
-
-
No substrates are several non-mitochondrial proteins
-
-
?
additional information
?
-
-
e.g. bovine serum albumin, mouse immunoglobulin G, yeast hexokinase or yeast tryptophan synthase, neither in native nor in heat or pH-denatured form
-
-
?
additional information
?
-
-
No substrates are mature mitochondrial proteins
-
-
?
additional information
?
-
-
precursor substrates must be synthesized by translation in a mRNA-dependent in vitro translation system, e.g. nuclease-treated rabbit reticulocyte lysate
-
-
?
additional information
?
-
-
No substrates are denatured enzyme precursors
-
-
?
additional information
?
-
-
MAS2 activity alone is very low, MAS1 restores activity
-
-
?
additional information
?
-
-
substrate binds to MAS2, not MAS1 enzyme component (photocrosslinking experiment)
-
-
?
additional information
?
-
-
substrate binding changes conformation of the alpha-subunit
-
?
additional information
?
-
-
removes amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins during or after translocation across mitochondrial membranes
-
-
?
additional information
?
-
-
removes amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins during or after translocation across mitochondrial membranes
-
-
?
additional information
?
-
-
removes amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins during or after translocation across mitochondrial membranes
-
-
?
additional information
?
-
-
plays an essential role in mitochondrial protein import
-
?
additional information
?
-
-
the enzyme genetically interacts with prohibitins in the inner mitochondrial membrane and links the function of prohibitins to the F1FO-ATP synthase complex
-
-
?
additional information
?
-
-
the enzyme specifically recognizes mitochondrial preproteins and removes their basic N-terminal signal prepeptides
-
-
?
additional information
?
-
-
the mitochondrial processing peptidase removes leader peptides of preproteins after import into the mitochondrial matrix space to increase protein stability, enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space, overview
-
-
?
additional information
?
-
-
the enzyme specifically recognizes mitochondrial preproteins and removes their basic N-terminal signal prepeptides, overview
-
-
?
additional information
?
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cleavage site specificity of the major mitochondrial processing peptidase for removal of N-terminal presequences from mitochondrial proteins during maturation, global analysis of the N-proteome of yeast mitochondria, method, overview. For a number of proteins such as Gif1 and Pdb1, more than one N-terminus exist, therefore two truncated versions of the proteins are synthesized and compared to the in organello processing product, product identification by LC-MS/MS analysis
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construction of a mutant MPP recognition sequence in substrate Nfs1 by replacing the two arginine codons at positions -2 and -3 prevents cleavage by MPP
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quantitative ChaFRADIC (charge-based fractional diagonal chromatography) analysis identifies 66 novel substrate proteins, which allow refinement of the MPP cleavage site establishing R2 as a major determinant of mitochondrial processing protease recognition and processing. Proteins that do not posses a presequence are not substrates
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quantitative ChaFRADIC (charge-based fractional diagonal chromatography) analysis identifies 66 novel substrate proteins, which allow refinement of the MPP cleavage site establishing R2 as a major determinant of mitochondrial processing protease recognition and processing. Proteins that do not posses a presequence are not substrates
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No substrates are several non-mitochondrial proteins
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No substrates are several non-mitochondrial proteins
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e.g. bovine serum albumin, mouse immunoglobulin G, yeast hexokinase or yeast tryptophan synthase, neither in native nor in heat or pH-denatured form
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No substrates are mature mitochondrial proteins
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No substrates are denatured enzyme precursors
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the large subunit alone has no cleavage activity
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removes amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins during or after translocation across mitochondrial membranes
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no stimulation by mitochondrial matrix fraction
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plant enzyme is integral part of bifunctional cytochrome c reductase complex
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plant enzyme is integral part of bifunctional cytochrome c reductase complex
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neither the individual subunits nor their combinations are catalytically active in in vitro processing
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plays an essential role in mitochondrial protein import
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no stimulation by mitochondrial matrix fraction
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does cleave 4 out of 4 hydrogenosomal presequences, 1 out of 3 mitosomal substrates and 2 out of 3 mitochondrial substrates
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plays an essential role in mitochondrial protein import
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