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3-Hydroxyacyl-CoA dehydrogenase precursor + H2O
?
-
EC 1.1.1.35
-
-
?
Abz-FQTKVAAK(Dnp)-NH2 + H2O
Abz-FQ + TKVAAK(Dnp)-NH2
-
-
-
?
Abz-FRSGQPLQNKVQLQ-ED(Dnp) + H2O
Abz-FRSGQPLQ + NKVQLQ-ED(Dnp)
-
-
-
?
Abz-FSSKTTVK(Dnp)-NH2 + H2O
Abz-FS + SKTTVK(Dnp)-NH2
-
-
-
?
Abz-IKQSSLLK(Dnp)-NH2 + H2O
Abz-IKQ + SSLLK(Dnp)-NH2
-
-
-
?
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-NLMKKSTK(Dnp)-NH2 + H2O
Abz-NLM + KKSTK(Dnp)-NH2
-
-
-
?
Abz-QPLANKVQ-ED(Dnp) + H2O
Abz-QPLA + NKVQ-ED(Dnp)
-
-
-
?
Abz-QPLQAKVQ-ED(Dnp) + H2O
Abz-QPLQ + AKVQ-ED(Dnp)
-
-
-
?
Abz-QPLQNKVQ-ED(Dnp) + H2O
Abz-QPLQ + NKVQ-ED(Dnp)
-
-
-
?
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-VAAQTKTK(Dnp)-NH2 + H2O
Abz-VAA + QTKTK(Dnp)-NH2
-
-
-
?
Abz-VISSRLEK(Dnp)-NH2 + H2O
Abz-VIS + SRLEK(Dnp)-NH2
-
-
-
?
Abz-VRNFRSGQPLQNKVQ-ED(Dnp) + H2O
Abz-VRNFRSGQPLQ + NKVQ-ED(Dnp)
-
-
-
?
Abz-WTTGGKAK(Dnp)-NH2 + H2O
Abz-WT + TGGKAK(Dnp)-NH2
-
-
-
?
Acetoacetyl-CoA thiolase precursor + H2O
?
-
EC 2.3.1.9
-
-
?
ADP/ATP translocator precursor protein + H2O
?
-
from potato, poor substrate
-
-
?
adrenodoxin precursor + H2O
?
-
processing
-
?
Adrenodoxin precursor + H2O
Adrenodoxin
Aldehyde dehydrogenase precursor + H2O
?
-
-
-
-
?
ALQPARDYAAQASPSPKA + H2O
?
-
-
-
?
ALQPARDYAAQASPSPKAGATTGRIVAV + H2O
?
-
-
-
?
amino benzoyl-LARPVGAALRRSFSTY(NO2)AQNN + H2O
?
ARAARAARAFAASA + H2O
?
-
-
-
?
ARAARAARAFASAA + H2O
?
-
-
-
?
ARAARAARAFATSA + H2O
?
-
-
-
?
ARAARAARAFSAAA + H2O
?
-
-
-
?
ARAARAARAFSASA + H2O
?
-
-
-
?
ARAARAARAFSCSA + H2O
?
-
-
-
?
ARAARAARAFSNSA + H2O
?
-
-
-
?
ARAARAARAFSSAA + H2O
?
-
-
-
?
ARAARAARAFSSSA + H2O
?
-
-
-
?
ARAARAARAFSTAA + H2O
?
-
-
-
?
ARAARAARAFSTSA + H2O
?
-
-
-
?
ARAARAARAFSVSA + H2O
?
-
-
-
?
ARAARAARAFTSSA + H2O
?
-
-
-
?
ARAARAARAYGSTA + H2O
?
-
-
-
?
ARAARAARAYGTTA + H2O
?
-
-
-
?
ARAARAARAYSSTA + H2O
?
-
-
-
?
ARAARAARAYSTTA + H2O
?
-
-
-
?
aspartate aminotransferase + H2O
?
-
processing
-
?
ASVRYSHTDIKVPDFSDYRRPEVLD + H2O
?
-
-
-
?
ATP synthase subunit 2 precursor + H2O
ATP synthase subunit 2
-
-
-
?
ATP synthase subunit 9 precursor + H2O
ATP synthase subunit 9
-
-
-
?
AVALHSAVSASDLELHPPSY + H2O
?
-
-
-
?
AVALHSAVSASDLELHPPSYPWSHRGLLSS + H2O
?
-
-
-
?
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
?
Citrate synthase precursor + H2O
Citrate synthase
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
-
-
?
COX IV 2-25 + H2O
?
-
-
-
?
COX IV precursor + H2O
processed COX IV + mitochondrial targeting sequence of COX IV
Cyclophilin precursor + H2O
Cyclophilin intermediate form
-
cleavage site: Ala36-Phe37
-
?
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
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 c1 precursor + H2O
Cytochrome c1 intermediate form
DAC-MDH5-25 + H2O
?
-
-
-
?
Enoyl-CoA hydratase precursor + H2O
?
-
EC 4.2.1.17
-
-
?
epidermal growth factor receptor preprotein + H2O
mature epidermal growth factor receptor + prepeptide of epidermal growth factor receptor
F1-ATPase alpha-subunit precursor + H2O
F1-ATPase alpha-subunit
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
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
-
?
malate dehydrogenase + H2O
?
-
processing
-
?
MAS1 precursor + H2O
MAS1
-
MAS1 takes part in its own precursor activation
-
?
MDH 1-21 (14A) peptide MLSALARPVGAALARS FSTSA + H2O
?
-
-
-
?
MDH1-21 + H2O
?
-
synthetic peptide substrate
-
?
Medium chain acyl-CoA dehydrogenase precursor + H2O
?
-
EC 1.3.99.3
-
-
?
Methylmalonyl-CoA mutase + H2O
Methylmalonyl-CoA mutase
-
from human
-
?
Mitochondrial alcohol dehydrogenase precursor + H2O
Mitochondrial alcohol dehydrogenase
-
-
-
?
mitochondrial carrier protein + H2O
?
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
-
-
-
-
?
mitochondrial matrix proteins + H2O
?
-
-
-
?
Mitochondrial proteins with artificial precursors + H2O
?
MLSALARPVGAALARSFSTSA + H2O
?
MPPI precursor + H2O
MPPI
-
MPPI presumably takes part in its own precursor activation
-
?
Nfs1 + H2O
processed Nfs1
nuclear-encoded polyprotein precursor + H2O
?
Ornithine carbamoyl transferase precursor + H2O
Ornithine carbamoyl transferase intermediate form
P-25 peptide + H2O
?
-
matrix-targeting peptide containing cleavage site of authentic precursor protein
-
-
?
P-27 protein precursor + H2O
P-27 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
-
?
pea glutathione reductase + H2O
?
phosphatase and tensin homologue-induced kinase 1 + H2O
?
-
-
-
-
?
plant mitochondrial carrier proteins + H2O
?
pre-F1FO-ATP synthase + H2O
mature F1FO-ATP synthase + prepeptide
Precytochrome b2-mouse dehydrofolate reductase fusion protein + H2O
31-aminoacid presequence + cytochrome b2-mouse dehydrofolate reductase protein
preprotein Din7 + H2O
presequence + protein Din7
preprotein Mrx8 + H2O
presequence + protein Mrx8
preprotein Yhb1 + H2O
presequence + protein Yhb1
presequence-containing protein + H2O
presequence + protein
-
-
-
-
?
Processing enhancing protein precursor + H2O
Processing enhancing protein
processing enhancing protein precursor + H2O
processing enhancing protein + ?
-
-
-
-
?
rat MDH precursor + H2O
?
-
-
-
?
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
-
-
?
Rieske FES protein precursor + H2O
Rieske FES protein intermediate form
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
-
-
?
RPLVASVSLNVPASVRYSHTDIKVPDF + H2O
?
-
-
-
?
Serine-pyruvate aminotransferase precursor + H2O
Serine-pyruvate aminotransferase
-
-
-
?
Soluble mitochondrial heat stress protein + H2O
?
-
i.e. HSP68
-
-
?
TbIscU preprotein + H2O
?
-
-
-
-
?
Ubiquinol-cytochrome c reductase iron-sulfur subunit precursor + H2O
Ubiquinol-cytochrome c reductase iron-sulfur subunit intermediate form
-
Neurospora crassa enzyme
from Neurospora
?
VPASVRYSHTDIK + H2O
?
-
-
-
?
additional information
?
-
Adrenodoxin precursor + H2O
Adrenodoxin
-
-
-
?
Adrenodoxin precursor + H2O
Adrenodoxin
-
-
-
?
amino benzoyl-LARPVGAALRRSFSTY(NO2)AQNN + H2O
?
-
-
-
?
amino benzoyl-LARPVGAALRRSFSTY(NO2)AQNN + H2O
?
-
-
-
?
Citrate synthase precursor + H2O
Citrate synthase
-
-
-
?
Citrate synthase precursor + H2O
Citrate synthase
-
-
-
?
Citrate synthase precursor + H2O
Citrate synthase
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
?
-
-
-
-
?
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
?
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
?
-
-
-
-
?
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
?
-
-
-
-
-
?
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
?
-
-
substrate recognition specificity
-
-
?
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
?
-
-
highly specific enzyme
-
-
?
additional information
?
-
-
highly specific enzyme
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
highly specific enzyme
-
-
?
additional information
?
-
-
No substrates are several non-mitochondrial proteins
-
-
?
additional information
?
-
-
highly specific enzyme
-
-
?
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
?
-
-
No substrates are denatured enzyme precursors
-
-
?
additional information
?
-
-
the large subunit alone has no cleavage activity
-
-
?
additional information
?
-
-
removes amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins during or after translocation across mitochondrial membranes
-
-
?
additional information
?
-
-
no stimulation by mitochondrial matrix fraction
-
-
?
additional information
?
-
-
plant enzyme is integral part of bifunctional cytochrome c reductase complex
-
-
?
additional information
?
-
-
plant enzyme is integral part of bifunctional cytochrome c reductase complex
-
-
?
additional information
?
-
-
neither the individual subunits nor their combinations are catalytically active in in vitro processing
-
-
?
additional information
?
-
-
plays an essential role in mitochondrial protein import
-
?
additional information
?
-
-
no stimulation by mitochondrial matrix fraction
-
-
?
additional information
?
-
-
substrate recognition specificity
-
-
?
additional information
?
-
-
does cleave 4 out of 4 hydrogenosomal presequences, 1 out of 3 mitosomal substrates and 2 out of 3 mitochondrial substrates
-
-
?
additional information
?
-
-
plays an essential role in mitochondrial protein import
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COX IV precursor + H2O
processed COX IV + mitochondrial targeting sequence of COX IV
-
-
-
?
epidermal growth factor receptor preprotein + H2O
mature epidermal growth factor receptor + prepeptide of epidermal growth factor receptor
-
-
-
-
?
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 matrix protein precursor + H2O
mitochondrial matrix protein + precursor
-
-
-
-
?
Nfs1 + H2O
processed Nfs1
-
MPP cleaves the precursor between Phe33 and Tyr34, Nfs1 processing, 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
-
-
?
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
-
-
?
phosphatase and tensin homologue-induced kinase 1 + H2O
?
-
-
-
-
?
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
-
-
?
presequence-containing protein + H2O
presequence + protein
-
-
-
-
?
processing enhancing protein precursor + H2O
processing enhancing protein + ?
-
-
-
-
?
additional information
?
-
additional information
?
-
-
mitosomal substrates of the enzyme are processed to mature proteins in Antonospora locustae with a simplified processing complex, overview
-
-
?
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
?
-
-
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 cleaves off presequences from mitochondrial precursor proteins
-
-
?
additional information
?
-
-
plays an essential role in mitochondrial protein import
-
?
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
?
-
-
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
?
-
-
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
-
-
?
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
?
-
-
plays an essential role in mitochondrial protein import
-
?
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Rawlings, N.D.; Barrett, A.J.
Homologues of insulinase, a new superfamily of metalloendopeptidases
Biochem. J.
275
389-391
1991
Saccharomyces cerevisiae, Neurospora crassa
brenda
Kalousek, F.; Neupert, W.; Omura, T.; Schatz, G.; Schmitz, U.K.
Uniform nomenclature for the mitochondrial peptidases cleaving precursors of mitochondrial proteins
Trends Biochem. Sci.
18
249
1993
Saccharomyces cerevisiae, Neurospora crassa, Rattus norvegicus, Solanum tuberosum
brenda
Bhni, P.C.; Daum, G.
Processing of mitochondrial polypeptide precursors in yeast
Methods Enzymol.
97
311-323
1983
Saccharomyces cerevisiae, Saccharomyces cerevisiae D-273-10B
brenda
McAda, P.C.; Douglas, M.G.
A yeast mitochondrial chelator-sensitive protease that processes cytoplasmically synthesized protein precursors: isolation from yeast and assay
Methods Enzymol.
97
337-344
1983
Saccharomyces cerevisiae
brenda
Bhni, P.C.; Daum, G.; Schatz, G.
Import of proteins into mitochondria. Partial purification of a matrix-located protease involved in cleavage of mitochondrial precursor polypeptides
J. Biol. Chem.
258
4937-4943
1983
Saccharomyces cerevisiae, Saccharomyces cerevisiae D-273-10B
brenda
Miura, S.; Amaya, Y.; Mori, M.
A metalloprotease involved in the processing of mitochondrial precursor proteins
Biochem. Biophys. Res. Commun.
134
1151-1159
1986
Rattus norvegicus
brenda
Kumamoto, T.; Omura, T.
Characterization of a mitochondrial matrix protease catalyzing the processing of adrenodoxin precursor
J. Biochem.
100
247-254
1986
Bos taurus, Rattus norvegicus
brenda
Hawlitschek, G.; Schneider, H.; Schmidt, B.; Tropschug, M.; Hartl, F.U.; Neupert, W.
Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein
Cell
53
795-806
1988
Neurospora crassa
brenda
Yang, M.; Jensen, R.E.; Yaffe, M.P.; Oppliger, W.; Schatz, G.
Import of proteins into yeast mitochondria: the purified matrix processing protease contains two subunits which are encoded by the nuclear MAS1 and MAS2 genes
EMBO J.
7
3857-3862
1988
Saccharomyces cerevisiae, Saccharomyces cerevisiae D-273-10B
brenda
Jensen, R.E.; Yaffe, M.P.
Import of proteins into yeast mitochondria: the nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MAS1-encoded subunit
EMBO J.
7
3863-3871
1988
Saccharomyces cerevisiae
brenda
Witte, C.; Jensen, R.E.; Yaffe, M.P.; Schatz, G.
MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease
EMBO J.
7
1439-1447
1988
Saccharomyces cerevisiae, More
brenda
Kleiber, J.; Kalousek, F.; Swaroop, M.; Rosenberg, L.E.
The general mitochondrial matrix processing protease from rat liver: structural characterization of the catalytic subunit
Proc. Natl. Acad. Sci. USA
87
7978-7982
1990
More, Rattus norvegicus
brenda
Geli, V.; Yang, M.; Suda, K.; Lustig, A.; Schatz, G.
The MAS-encoded processing protease of yeast mitochondria. Overproduction and characterization of its two nonidentical subunits
J. Biol. Chem.
265
19216-19222
1990
Saccharomyces cerevisiae
brenda
Schneider, H.; Arretz, M.; Wachter, E.; Neupert, W.
Matrix processing peptidase of mitochondria. Structure-function relationships
J. Biol. Chem.
265
9881-9887
1990
More, Neurospora crassa
brenda
Isaya, G.; Kalousek, F.; Fenton, W.A.; Rosenberg, L.E.
Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide
J. Cell Biol.
113
65-76
1991
Rattus norvegicus
brenda
Yang, M.; Geli, V.; Oppliger, W.; Suda, K.; James, P.; Schatz, G.
The MAS-encoded processing protease of yeast mitochondria. Interaction of the purified enzyme with signal peptides and a purified precursor protein
J. Biol. Chem.
266
6416-6423
1991
Saccharomyces cerevisiae
brenda
Eriksson, A.C.; Glaser, E.
Mitochondrial processing proteinase: a general processing proteinase of spinach leaf mitochondria is a membrane-bound enzyme
Biochim. Biophys. Acta
1140
208-214
1992
More, Solanum tuberosum, Spinacia oleracea
-
brenda
Emmermann, M.; Schmitz, U.K.
The cytochrome c reductase integrated processing peptidase from potato mitochondria belongs to a new class of metalloendoproteases
Plant Physiol.
103
615-620
1993
Solanum tuberosum
brenda
Emmermann, M.; Braun, H.P.; Arretz, M.; Schmitz, U.K.
Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria
J. Biol. Chem.
268
18936-18942
1993
More, Solanum tuberosum
brenda
Saavedra-Alanis, V.M.; Rysavy, P.; Rosenberg, L.E.; Kalousek, F.
Rat liver mitochondrial processing peptidase. Both alpha- and beta-subunits are required for activity
J. Biol. Chem.
269
9284-9288
1994
Rattus norvegicus
brenda
Arretz, M.; Schneider, H.; Guiard, B.; Brunner, M.; Neupert, W.
Characterization of the mitochondrial processing peptidase of Neurospora crassa
J. Biol. Chem.
269
4959-4967
1994
Neurospora crassa
brenda
Geli, V.
Functional reconstitution in Escherichia coli of the yeast mitochondrial matrix peptidase from its two inactive subunits
Proc. Natl. Acad. Sci. USA
90
6247-6251
1993
Saccharomyces cerevisiae
brenda
Sjling, S.; Eriksson, A.C.; Glaaser, E.
A helical element in the C-terminal domain of the N. plumbaginifolia F1 beta presequence is important for recognition by the mitochondrial processing peptidase
J. Biol. Chem.
269
32059-32062
1994
Spinacia oleracea
brenda
Bassham, D.C.; Creighton, A.M.; Arretz, M.; Brunner, M.; Robinson, C.
Efficient but aberrant cleavage of mitochondrial precursor proteins by the chloroplast stromal processing peptidase
Eur. J. Biochem.
221
523-528
1994
Neurospora crassa
brenda
Brunner, M.; Neupert, W.
Purification and characterization of mitochondrial processing peptidase of Neurospora crassa
Methods Enzymol.
248
717-728
1995
Neurospora crassa
brenda
Braun, H.P.; Schmitz, U.K.
The bifunctional cytochrome c reductase/processing peptidase complex from plant mitochondria
J. Bioenerg. Biomembr.
27
423-436
1995
Solanum tuberosum, Spinacia oleracea, Triticum aestivum
brenda
Waltner, M.; Weiner, H.
Conversion of a nonprocessed mitochondrial precursor protein into one that is processed by the mitochondrial processing peptidase
J. Biol. Chem.
270
26311-26317
1995
Rattus norvegicus
brenda
Gakh, O.; Obsil, T.; Adamec, J.; Spizek, J.; Amler, E.; Janata, J.; Kalousek, F.
Substrate binding changes conformation of the alpha-, but not the beta-subunit of mitochondrial processing peptidase
Arch. Biochem. Biophys.
385
392-396
2001
Saccharomyces cerevisiae
brenda
Kitada, S.; Kojima, K.; Ito, A.
Glu191 and Asp195 in rat mitochondrial processing peptidase beta subunit are involved in effective cleavage of precursor protein through interaction with the proximal arginine
Biochem. Biophys. Res. Commun.
287
594-599
2001
Rattus norvegicus
brenda
Braun, H.P.; Schmitz, U.K.
The mitochondrial processing peptidase
Int. J. Biochem. Cell Biol.
29
1043-1045
1997
Neurospora sp., Rattus norvegicus, Saccharomyces cerevisiae, Solanum tuberosum, Triticum aestivum
brenda
Song, M.C.; Ogishima, T.; Ito, A.
Importance of residues carboxyl terminal relative to the cleavage site in substrates of mitochondrial processing peptidase for their specific recognition and cleavage
J. Biochem.
124
1045-1049
1998
Bos taurus
brenda
Deng, K.; Zhang, L.; Kachurin, A.M.; Yu, L.; Xia, D.; Kim, H.; Deisenhofer, J.; Yu, C.A.
Activation of a matrix processing peptidase from the crystalline cytochrome bc1 complex of bovine heart mitochondria
J. Biol. Chem.
273
20752-20757
1998
Bos taurus
brenda
Shimokata, K.; Kitada, S.; Ogishima, T.; Ito, A.
Role of alpha-subunit of mitochondrial processing peptidase in substrate recognition
J. Biol. Chem.
273
25158-25163
1998
Saccharomyces cerevisiae
brenda
Kojima, K.; Kitada, S.; Shimokata, K.; Ogishima, T.; Ito, A.
Cooperative formation of a substrate binding pocket by alpha- and beta-subunits of mitochondrial processing peptidase
J. Biol. Chem.
273
32542-32546
1998
Saccharomyces cerevisiae
brenda
Kitada, S.; Kojima, K.; Shimokata, K.; Ogishima, T.; Ito, A.
Glutamate residues required for substrate binding and cleavage activity in mitochondrial processing peptidase
J. Biol. Chem.
273
32547-32553
1998
Saccharomyces cerevisiae, Rattus norvegicus
brenda
Kojima, K.; Kitada, S.; Ogishima, T.; Ito, A.
A proposed common structure of substrates bound to mitochondrial processing peptidase
J. Biol. Chem.
276
2115-2121
2001
Saccharomyces cerevisiae
brenda
Kitada, S.; Yamasaki, E.; Kojima, K.; Ito, A.
Determination of the cleavage site of the presequence by mitochondrial processing peptidase on the substrate binding scaffold and the multiple subsites inside a molecular cavity
J. Biol. Chem.
278
1879-1885
2003
Saccharomyces cerevisiae, Rattus norvegicus
brenda
Taylor, A.B.; Smith, B.S.; Kitada, S.; Kojima, K.; Miyaura, H.; Otwinowski, Z.; Ito, A.; Deisenhofer, J.
Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences
Structure
9
615-625
2001
Saccharomyces cerevisiae
brenda
Janata, J.; Hola, K.; Kubala, M.; Gakh, O.; Parkhomenko, N.; Matuskova, A.; Kutejova, E.; Amler, E.
Substrate evokes translocation of both domains in the mitochondrial processing peptidase alpha-subunit during which the C-terminus acts as a stabilizing element
Biochem. Biophys. Res. Commun.
316
211-217
2004
Saccharomyces cerevisiae
brenda
Oshima, T.; Yamasaki, E.; Ogishima, T.; Kadowaki, K.; Ito, A.; Kitada, S.
Recognition and processing of a nuclear-encoded polyprotein precursor by mitochondrial processing peptidase
Biochem. J.
385
755-761
2005
Saccharomyces cerevisiae
brenda
Nomura, H.; Athauda, S.B.; Wada, H.; Maruyama, Y.; Takahashi, K.; Inoue, H.
Identification and reverse genetic analysis of mitochondrial processing peptidase and the core protein of the cytochrome bc1 complex of Caenorhabditis elegans, a model parasitic nematode
J. Biochem.
139
967-979
2006
Brugia malayi, Caenorhabditis elegans
brenda
Rudhe, C.; Clifton, R.; Chew, O.; Zemam, K.; Richter, S.; Lamppa, G.; Whelan, J.; Glaser, E.
Processing of the dual targeted precursor protein of glutathione reductase in mitochondria and chloroplasts
J. Mol. Biol.
343
639-647
2004
Solanum tuberosum
brenda
Murcha, M.W.; Elhafez, D.; Millar, A.H.; Whelan, J.
The N-terminal extension of plant mitochondrial carrier proteins is removed by two-step processing: the first cleavage is by the mitochondrial processing peptidase
J. Mol. Biol.
344
443-454
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae MY111-2, Solanum tuberosum
brenda
Nishino, T.G.; Kitano, K.; Kojima, K.; Ogishima, T.; Ito, A.; Kitada, S.
Spatial orientation of mitochondrial processing peptidase and a preprotein revealed by fluorescence resonance energy transfer
J. Biochem.
141
889-895
2007
Saccharomyces cerevisiae
brenda
Mukhopadhyay, A.; Yang, C.S.; Wei, B.; Weiner, H.
Precursor protein is readily degraded in mitochondrial matrix space if the leader is not processed by mitochondrial processing peptidase
J. Biol. Chem.
282
37266-37275
2007
Homo sapiens, Saccharomyces cerevisiae
brenda
Yoon, T.; Dizin, E.; Cowan, J.A.
N-terminal iron-mediated self-cleavage of human frataxin: regulation of iron binding and complex formation with target proteins
J. Biol. Inorg. Chem.
12
535-542
2007
Homo sapiens
brenda
Osman, C.; Wilmes, C.; Tatsuta, T.; Langer, T.
Prohibitins interact genetically with Atp23, a novel processing peptidase and chaperone for the F1Fo-ATP synthase
Mol. Biol. Cell
18
627-635
2007
Saccharomyces cerevisiae
brenda
Burri, L.; Williams, B.A.; Bursac, D.; Lithgow, T.; Keeling, P.J.
Microsporidian mitosomes retain elements of the general mitochondrial targeting system
Proc. Natl. Acad. Sci. USA
103
15916-15920
2006
Antonospora locustae, no activity in Encephalitozoon cuniculi
brenda
Nagayama, K.; Itono, S.; Yoshida, T.; Ishiguro, S.; Ochiai, H.; Ohmachi, T.
Antisense RNA inhibition of the beta subunit of the Dictyostelium discoideum mitochondrial processing peptidase induces the expression of mitochondrial proteins
Biosci. Biotechnol. Biochem.
72
1836-1846
2008
Dictyostelium discoideum
brenda
Smid, O.; Matuskova, A.; Harris, S.R.; Kucera, T.; Novotny, M.; Horvathova, L.; Hrdy, I.; Kutejova, E.; Hirt, R.P.; Embley, T.M.; Janata, J.; Tachezy, J.
Reductive evolution of the mitochondrial processing peptidases of the unicellular parasites trichomonas vaginalis and giardia intestinalis
PLoS Pathog.
4
e1000243
2008
Giardia intestinalis, Trichomonas vaginalis
brenda
Voegtle, F.N.; Wortelkamp, S.; Zahedi, R.P.; Becker, D.; Leidhold, C.; Gevaert, K.; Kellermann, J.; Voos, W.; Sickmann, A.; Pfanner, N.; Meisinger, C.
Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability
Cell
139
428-439
2009
Saccharomyces cerevisiae
brenda
Naamati, A.; Regev-Rudzki, N.; Galperin, S.; Lill, R.; Pines, O.
Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55
J. BIOL. CHEM.
284
30200-30208
2009
Saccharomyces cerevisiae
brenda
Nagayama, K.; Ohmachi, T.
Mitochondrial processing peptidase activity is controlled by the processing of alpha-MPP during development in Dictyostelium discoideum
Microbiology
156
978-989
2010
Dictyostelium discoideum (Q86A84), Dictyostelium discoideum
brenda
Ohtsuka, J.; Ichihara, Y.; Ebihara, A.; Nagata, K.; Tanokura, M.
Crystal structure of TTHA1264, a putative M16-family zinc peptidase from Thermus thermophilus HB8 that is homologous to the β subunit of mitochondrial processing peptidase
Proteins
75
774-780
2009
Thermus thermophilus (Q5SIV0), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SIV0)
brenda
Mossmann, D.; Meisinger, C.; Voegtle, F.
Processing of mitochondrial presequences
Biochim. Biophys. Acta
1819
1098-1106
2012
Saccharomyces cerevisiae
brenda
Teixeira, P.; Glaser, E.
Processing peptidases in mitochondria and chloroplasts
Biochim. Biophys. Acta
1833
360-370
2013
Homo sapiens
brenda
Greene, A.; Grenier, K.; Aguileta, M.; Muise, S.; Farazifard, R.; Haque, M.; McBride, H.; Park, D.; Fon, E.
Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment
EMBO Rep.
13
378-385
2012
Homo sapiens
brenda
Endow, J.; Inoue, K.
Stable complex formation of thylakoidal processing peptidase and PGRL1
FEBS Lett.
587
2226-2231
2013
Arabidopsis thaliana
brenda
Mach, J.; Poliak, P.; Matuskova, A.; Zarsky V.; Janata, J.; Lukes, J.; Tachezy, J.
An advanced system of the mitochondrial processing peptidase and core protein family in Trypanosoma bruceiand multiple origins of the Core I subunit in eukaryotes
Genome Biol. Evol.
5
860-875
2013
Trypanosoma brucei
brenda
Desy, S.; Schneider, A.; Mani, J.
Trypanosoma brucei has a canonical mitochondrial processing peptidase
Mol. Biochem. Parasitol.
185
161-164
2012
Trypanosoma brucei
brenda
Kwasniak, M.; Pogorzelec, L.; Migdal, I.; Smakowska, E.; Janska, H.
Proteolytic system of plant mitochondria
Physiol. Plant.
145
187-195
2012
Arabidopsis thaliana
brenda
Jobling, R.K.; Assoum, M.; Gakh, O.; Blaser, S.; Raiman, J.A.; Mignot, C.; Roze, E.; Duerr, A.; Brice, A.; Levy, N.; Prasad, C.; Paton, T.; Paterson, A.D.; Roslin, N.M.; Marshall, C.R.; Desvignes, J.P.; Roeckel-Trevisiol, N.; Scherer, S.W.; Rouleau, G.A.; Megarbane, A.; Isaya, G.; Delague, V.; Yoon, G.
PMPCA mutations cause abnormal mitochondrial protein processing in patients with non-progressive cerebellar ataxia
Brain
138
1505-1517
2015
Homo sapiens (Q10713 AND O75439), Homo sapiens
brenda
Joshi, M.; Anselm, I.; Shi, J.; Bale, T.A.; Towne, M.; Schmitz-Abe, K.; Crowley, L.; Giani, F.C.; Kazerounian, S.; Markianos, K.; Lidov, H.G.; Folkerth, R.; Sankaran, V.G.; Agrawal, P.B.
Mutations in the substrate binding glycine-rich loop of the mitochondrial processing peptidase-alpha protein (PMPCA) cause a severe mitochondrial disease
Cold Spring Harb. Mol. Case Stud.
2
a000786
2016
Homo sapiens (Q10713), Homo sapiens
brenda
Marcondes, M.F.; Alves, F.M.; Assis, D.M.; Hirata, I.Y.; Juliano, L.; Oliveira, V.; Juliano, M.A.
Substrate specificity of mitochondrial intermediate peptidase analysed by a support-bound peptide library
FEBS open bio
5
429-436
2015
Homo sapiens (Q10713 AND O75439)
brenda
Burkhart, J.M.; Taskin, A.A.; Zahedi, R.P.; Voegtle, F.N.
Quantitative profiling for substrates of the mitochondrial presequence processing protease reveals a set of nonsubstrate proteins increased upon proteotoxic stress
J. Proteome Res.
14
4550-4563
2015
Saccharomyces cerevisiae (P10507 AND P11914), Saccharomyces cerevisiae ATCC 204508 (P10507 AND P11914)
brenda
Woellhaf, M.W.; Sommer, F.; Schroda, M.; Herrmann, J.M.
Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein
Mol. Biol. Cell
27
3031-3039
2016
Saccharomyces cerevisiae
brenda