Information on EC 3.4.24.64 - mitochondrial processing peptidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.4.24.64
-
RECOMMENDED NAME
GeneOntology No.
mitochondrial processing peptidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
show the reaction diagram
release of N-terminal targeting peptides from precursor proteins imported into mitochondria typically with Arg in position P2
-
-
-
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
show the reaction diagram
limited proteolysis: cleaves precursors of mitochondrial proteins to their mature form, not further
-
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
show the reaction diagram
cleaves amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins
-
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
show the reaction diagram
structure-function relationship
-
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
show the reaction diagram
mechanism
-
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
show the reaction diagram
mechanism; structure-function relationship
-
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
show the reaction diagram
the amino acid residues on the C-terminal side of the cleavage site in the preprotein are orientated tail out from the large cavity of MPP and interact with the glycine-rich loop of the alpha-MPP subunit. Thus, MPP orientates preproteins at the specific cleft between the catalytic domain and the flexible glycine-rich loop, which seems to pinch the extended polypeptide, catalytic mechanism, overview
-
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
show the reaction diagram
cleaves amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins; limited proteolysis: cleaves precursors of mitochondrial proteins to their mature form, not further
Saccharomyces cerevisiae D-273-10B
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Alpha-MPP
-
-
-
-
Beta-MPP
-
-
-
-
General mitochondrial processing peptidase
-
-
-
-
HA1523
-
-
-
-
inner membrane peptidase processing enzyme
-
-
Matrix peptidase
-
-
-
-
Matrix processing peptidase
-
-
-
-
Matrix processing proteinase
-
-
-
-
Mitochondrial chelator-sensitive protease
-
-
-
-
mitochondrial processing peptidase
-
-
mitochondrial processing peptidase
-
-
MPP
-
-
-
-
MPP
-
-
MPP
Neurospora sp.
-
-
P-52
-
-
-
-
P-55
-
-
-
-
PEP
Neurospora sp.
-
-
Processing enhancing peptidase
-
-
-
-
processing enhancing protein
Neurospora sp.
-
-
processing peptidase
-
-
Proteinase, mitochondrial protein precursor-processing
-
-
-
-
TTHA1264
Q5SIV0
-
Mitochondrial protein precursor-processing proteinase
-
-
-
-
additional information
Q5SIV0
the enzyme belongs to the M16 zinc peptidase family
CAS REGISTRY NUMBER
COMMENTARY
86280-61-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
a fungal intracellular microsporidian parasite
-
-
Manually annotated by BRENDA team
bovine
-
-
Manually annotated by BRENDA team
bovine, beef
-
-
Manually annotated by BRENDA team
gene mppA encoding alpha-MPP
UniProt
Manually annotated by BRENDA team
wild-type strain 74A
-
-
Manually annotated by BRENDA team
Neurospora sp.
-
-
-
Manually annotated by BRENDA team
no activity in Encephalitozoon cuniculi
-
-
-
Manually annotated by BRENDA team
male Sprague-Dawley
-
-
Manually annotated by BRENDA team
mutant strains GL-1 (heme-deficient) or D273-10B-1 (rho-); strain D-273-10B
-
-
Manually annotated by BRENDA team
overproducing strain VGA
-
-
Manually annotated by BRENDA team
overproducing strains G10 (MAS1); overproducing strain VGA
-
-
Manually annotated by BRENDA team
overproducing strains G10 (MAS1); overproducing strains G12 (MAS2), derived from JK9-3D
-
-
Manually annotated by BRENDA team
recombinantly expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
several strains, overview
-
-
Manually annotated by BRENDA team
strain D-273-10B
-
-
Manually annotated by BRENDA team
strain MY111-2
-
-
Manually annotated by BRENDA team
wild-type and mas1-mutants
-
-
Manually annotated by BRENDA team
wild-type strain AH216 and mas2-mutants
-
-
Manually annotated by BRENDA team
wild-type strain S288c and derivatives
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae D-273-10B
strain D-273-10B
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae MY111-2
strain MY111-2
-
-
Manually annotated by BRENDA team
potato, var. Bintje
-
-
Manually annotated by BRENDA team
var. Marfona
-
-
Manually annotated by BRENDA team
strain HB8
UniProt
Manually annotated by BRENDA team
additional information
homology between rat, yeast and Neurospora enzymes
-
-
Manually annotated by BRENDA team
additional information
MAS1 protein of Saccharomyces cerevisiae is immunologically related to Neurospora crassa MPP
-
-
Manually annotated by BRENDA team
additional information
the enzymes from Spinacia oleracea or Solanum tuberosum are immunologically not related to MPP but to processing enhancing protein (i.e. PEP) from fungi and mammals
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
the mitochondrial processing protease is required in maturation of mitochondrial proproteins for removal of the N-terminal presequences
physiological function
-, Q86A84
MPP plays an essential role in mitochondrial biogenesis and cell proliferation
physiological function
Q5SIV0
MPP is involved in the transport of nuclear-encoded proteins from the cytosol into mitochondria
metabolism
-
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
additional information
-, Q86A84
expression of mppA is developmentally regulated
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-Hydroxyacyl-CoA dehydrogenase precursor + H2O
?
show the reaction diagram
-
EC 1.1.1.35
-
-
-
Acetoacetyl-CoA thiolase precursor + H2O
?
show the reaction diagram
-
EC 2.3.1.9
-
-
-
ADP/ATP translocator precursor protein + H2O
?
show the reaction diagram
-
from potato, poor substrate
-
-
-
Adrenodoxin precursor + H2O
Adrenodoxin
show the reaction diagram
-
-
-
-
adrenodoxin precursor + H2O
?
show the reaction diagram
-
processing
-
?
Aldehyde dehydrogenase precursor + H2O
?
show the reaction diagram
-
-
-
-
-
ALQPARDYAAQASPSPKA + H2O
?
show the reaction diagram
-
-
-
?
ALQPARDYAAQASPSPKAGATTGRIVAV + H2O
?
show the reaction diagram
-
-
-
?
amino benzoyl-LARPVGAALRRSFSTY(NO2)AQNN + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFAASA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFASAA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFATSA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFSAAA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFSASA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFSCSA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFSNSA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFSSAA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFSSSA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFSTAA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFSTSA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFSVSA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAFTSSA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAYGSTA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAYGTTA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAYSSTA + H2O
?
show the reaction diagram
-
-
-
?
ARAARAARAYSTTA + H2O
?
show the reaction diagram
-
-
-
?
aspartate aminotransferase + H2O
?
show the reaction diagram
-
processing
-
?
ASVRYSHTDIKVPDFSDYRRPEVLD + H2O
?
show the reaction diagram
-
-
-
?
ATP synthase subunit 2 precursor + H2O
ATP synthase subunit 2
show the reaction diagram
-
-
-
-
ATP synthase subunit 9 precursor + H2O
ATP synthase subunit 9
show the reaction diagram
-
-
-
-
AVALHSAVSASDLELHPPSY + H2O
?
show the reaction diagram
-
-
-
?
AVALHSAVSASDLELHPPSYPWSHRGLLSS + H2O
?
show the reaction diagram
-
-
-
?
C-DACMDH + H2O
?
show the reaction diagram
-
-
-
?
Chimeric preproteins derived from precursor of cytochrome b2 fused to dehydrofolate reductase + H2O
Pb2(1-31) + ib2delta19(167)-DHFR processed protein
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
Citrate synthase precursor + H2O
Citrate synthase
show the reaction diagram
-
-
-
-
Citrate synthase precursor + H2O
Citrate synthase
show the reaction diagram
-
-
-
-
-
COX IV 2-25 + H2O
?
show the reaction diagram
-
-
-
?
COX IV precursor + H2O
processed COX IV + mitochondrial targeting sequence of COX IV
show the reaction diagram
-, Q86A84
-
-
-
?
COX IV precursor + H2O
processed COX IV + mitochondrial targeting sequence of COX IV
show the reaction diagram
-, Q86A84
recombinant C-terminally His-tagged substrate
-
-
?
Cyclophilin precursor + H2O
Cyclophilin intermediate form
show the reaction diagram
-
cleavage site: Ala36-Phe37
-
-
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
show the reaction diagram
-
-
-
-
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
show the reaction diagram
-
-
-
-
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
show the reaction diagram
-
-
-
-
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
show the reaction diagram
-
tested as fusion protein b2-DFHR
-
-
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
show the reaction diagram
Saccharomyces cerevisiae D-273-10B
-
-
-
-
Cytochrome b2 precursor + H2O
Cytochrome b2 intermediate form
show the reaction diagram
Saccharomyces cerevisiae D-273-10B
-
-
-
-
Cytochrome c oxidase subunit IV precursor + H2O
Cytochrome c oxidase subunit IV
show the reaction diagram
-
-
-
-
-
Cytochrome c oxidase subunit IV precursor + H2O
Cytochrome c oxidase subunit IV
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae D-273-10B
-
-
-
-
Cytochrome c oxidase subunit V precursor + H2O
Cytochrome c oxidase subunit V
show the reaction diagram
-
-
-
-
Cytochrome c oxidase subunit V precursor + H2O
Cytochrome c oxidase subunit V
show the reaction diagram
-
-
-
-
Cytochrome c1 precursor + H2O
Cytochrome c1 intermediate form
show the reaction diagram
-
membrane-bound enzyme
-
-
-
Cytochrome c1 precursor + H2O
Cytochrome c1 intermediate form
show the reaction diagram
-
membrane-bound enzyme
-
-
Cytochrome c1 precursor + H2O
Cytochrome c1 intermediate form
show the reaction diagram
-
membrane-bound enzyme
-
-
DAC-MDH5-25 + H2O
?
show the reaction diagram
-
-
-
?
Enoyl-CoA hydratase precursor + H2O
?
show the reaction diagram
-
EC 4.2.1.17
-
-
-
epidermal growth factor receptor preprotein + H2O
mature epidermal growth factor receptor + prepeptide of epidermal growth factor receptor
show the reaction diagram
-
-, 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
show the reaction diagram
-
-
-
-
F1-ATPase alpha-subunit precursor + H2O
F1-ATPase alpha-subunit
show the reaction diagram
-
-
-
-
F1-ATPase alpha-subunit precursor + H2O
F1-ATPase alpha-subunit
show the reaction diagram
Saccharomyces cerevisiae D-273-10B
-
-
-
-
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
show the reaction diagram
-
-
-
-
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
show the reaction diagram
-
-
-
-
-
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
show the reaction diagram
-
-
-
-
-
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
show the reaction diagram
-
F0F1-ATP-synthase F1beta subunit precursor from Neurospora crassa
-
-
-
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
show the reaction diagram
-
F0F1-ATP-synthase F1beta subunit precursor from Nicotiana plumbaginifolia
-
-
-
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
show the reaction diagram
-
F0F1-ATP-synthase F1beta subunit precursor from Nicotiana plumbaginifolia
-
-
-
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
show the reaction diagram
-
cleavage site: Phe40-Ala41
-
-
-
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
show the reaction diagram
-
no cleavage with isolated enzyme subunits
-
-
-
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
show the reaction diagram
Saccharomyces cerevisiae D-273-10B
-
-
-
-
-
frataxin + H2O
mature frataxin 56-210 + prepeptide
show the reaction diagram
-
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
?
show the reaction diagram
-
processing
-
?
Malate dehydrogenase precursor + H2O
Malate dehydrogenase
show the reaction diagram
-
-
-
-
Malate dehydrogenase precursor + H2O
Malate dehydrogenase
show the reaction diagram
-
from rat
-
-
Malate dehydrogenase precursor + H2O
Malate dehydrogenase
show the reaction diagram
-
from rat
from rat
-
malate dehydrogenase precursor + H2O
?
show the reaction diagram
-
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
-
-
?
MAS1 precursor + H2O
MAS1
show the reaction diagram
-
MAS1 takes part in its own precursor activation
-
-
MDH 1-21 (14A) peptide MLSALARPVGAALARS FSTSA + H2O
?
show the reaction diagram
-
-
-
?
MDH 2-17 + H2O
?
show the reaction diagram
-
-
-
?
MDH1-21 + H2O
?
show the reaction diagram
-
synthetic peptide substrate
-
?
Medium chain acyl-CoA dehydrogenase precursor + H2O
?
show the reaction diagram
-
EC 1.3.99.3
-
-
-
Methylmalonyl-CoA mutase + H2O
Methylmalonyl-CoA mutase
show the reaction diagram
-
from human
-
-
Mitochondrial alcohol dehydrogenase precursor + H2O
Mitochondrial alcohol dehydrogenase
show the reaction diagram
-
-
-
-
mitochondrial carrier protein + H2O
?
show the reaction diagram
-
-, 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
show the reaction diagram
-
-, 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 proteins with artificial precursors + H2O
?
show the reaction diagram
-
cleavage specificity
-
-
-
Mitochondrial proteins with artificial precursors + H2O
?
show the reaction diagram
-
containing presequence of ATPase subunit 9 fused to dehydrofolate reductase, i.e. pre-Su9-DHFR
-
-
-
MPP precursor + H2O
MPP
show the reaction diagram
-
-
i.e. alpha-MPP
-
MPP precursor + H2O
MPP
show the reaction diagram
-
i.e. alpha-MPP, processed by the combined mature forms of MPP and processing enhancing protein
i.e. alpha-MPP
-
MPPI precursor + H2O
MPPI
show the reaction diagram
-
MPPI presumably takes part in its own precursor activation
-
-
N-DACMDH + H2O
?
show the reaction diagram
-
-
-
?
Nfs1 + H2O
processed Nfs1
show the reaction diagram
-
MPP cleaves the precursor between Phe33 and Tyr34, Nfs1 processing, overview, 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
?
show the reaction diagram
-
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, 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
show the reaction diagram
-
-
-
-
-
Ornithine carbamoyl transferase precursor + H2O
Ornithine carbamoyl transferase intermediate form
show the reaction diagram
-
EC 2.1.3.3, from rat
-
-
-
Ornithine carbamoyl transferase precursor + H2O
Ornithine carbamoyl transferase intermediate form
show the reaction diagram
-
EC 2.1.3.3, from human
-
-
-
P-25 peptide + H2O
?
show the reaction diagram
-
matrix-targeting peptide containing cleavage site of authentic precursor protein
-
-
-
P-27 protein precursor + H2O
P-27 protein
show the reaction diagram
-
-
-
-
P53 precursor + H2O
P53
show the reaction diagram
-
i.e. subunit II of cytochrome c reductase complex, cleavage site: Tyr32-Ser33
-
-
P55 precursor + H2O
P55
show the reaction diagram
-
i.e. subunit I of cytochrome c reductase complex, cleavage site: Ser32-Ser33
-
-
pea glutathione reductase + H2O
?
show the reaction diagram
-
-, 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
?
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae MY111-2
-
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
show the reaction diagram
-
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, putative catalytically active Glu168
-
-
?
Precytochrome b2-mouse dehydrofolate reductase fusion protein + H2O
31 Aminoacid presequence + cytochrome b2-mouse dehydrofolate reductase protein
show the reaction diagram
-
-
-
-
-
Precytochrome b2-mouse dehydrofolate reductase fusion protein + H2O
31 Aminoacid presequence + cytochrome b2-mouse dehydrofolate reductase protein
show the reaction diagram
-
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
-
-
Processing enhancing protein precursor + H2O
Processing enhancing protein
show the reaction diagram
-
processed by the combined mature forms of MPP and processing enhancing protein
i.e. PEP
-
Processing enhancing protein precursor + H2O
Processing enhancing protein
show the reaction diagram
-
processed by the combined mature forms of MPP and processing enhancing protein
i.e. PEP
-
Processing enhancing protein precursor + H2O
Processing enhancing protein
show the reaction diagram
-
i.e. PEP precursor, takes part in its own precursor activation
i.e. PEP
-
rat MDH precursor + H2O
?
show the reaction diagram
-
-
-
?
Rhodanese with added MPP recognition site + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
from Neurospora
-
Rieske FES protein precursor + H2O
Rieske FES protein intermediate form
show the reaction diagram
-
from Neurospora
-
-
-
Rieske FES protein precursor + H2O
Rieske FES protein intermediate form
show the reaction diagram
-
from Neurospora
-
-
-
Rieske FES protein precursor + H2O
Rieske FES protein intermediate form
show the reaction diagram
-
from Neurospora
from Neurospora
-
RPG-Rhodanese with added MPP recognition site + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
?
Serine-pyruvate aminotransferase precursor + H2O
Serine-pyruvate aminotransferase
show the reaction diagram
-
-
-
-
Soluble mitochondrial heat stress protein + H2O
?
show the reaction diagram
-
i.e. HSP68
-
-
-
Ubiquinol-cytochrome c reductase iron-sulfur subunit precursor + H2O
Ubiquinol-cytochrome c reductase iron-sulfur subunit intermediate form
show the reaction diagram
-
Neurospora crassa enzyme
from Neurospora
-
VPASVRYSHTDIK + H2O
?
show the reaction diagram
-
-
-
?
MLSALARPVGAALARSFSTSA + H2O
?
show the reaction diagram
-
i.e. mouse malate dehydrogenase precursor MDH1-21
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
the large subunit alone has no cleavage activity
-
-
-
additional information
?
-
-
highly specific enzyme
-
-
-
additional information
?
-
-
alpha-MPP (formerly MAS2) alone has no catalytic activity
-
-
-
additional information
?
-
-
several chloroplast precursor proteins from wheat or Silene pratense
-
-
-
additional information
?
-
-
No substrates are several non-mitochondrial proteins
-
-
-
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
?
-
-
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 mitochondrial matrix proteins lacking cleavable signal sequences, e.g. 3-oxoacyl-CoA thiolase, rhodanese
-
-
-
additional information
?
-
-
processing activity is optimal at a 1:1 molar ratio of alpha- and beta-MPP
-
-
-
additional information
?
-
-
no stimulation by mitochondrial matrix fraction
-
-
-
additional information
?
-
-
plant enzyme is integral part of bifunctional cytochrome c reductase complex
-
-
-
additional information
?
-
-
No substrates are mature mitochondrial proteins
-
-
-
additional information
?
-
-
substrate recognition specificity
-
-
-
additional information
?
-
-
substrate recognition specificity
-
-
-
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
?
-
-
precursor substrates must be synthesized by translation in a mRNA-dependent in vitro translation system, e.g. nuclease-treated rabbit reticulocyte lysate
-
-
-
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
?
-
-
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
?
-
-
No substrates are cytochrome P-450 catalyzing side chain cleavage of cholesterol and of cytochrome P450 catalyzing 11beta-hydroxylation of steroids
-
-
-
additional information
?
-
-
neither the individual subunits nor their combinations are catalytically active in in vitro processing
-
-
-
additional information
?
-
-
No substrates are denatured enzyme precursors
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
mitochondrial processing peptidase is essential for viability of Caenorhabditis elegans
-
-
-
additional information
?
-
-
mitosomal substrates of the enzyme are processed to mature proteins in Antonospora locustae with a simplified processing complex, overview
-
-
-
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
?
-
-
binding of the iron-promoted binding of the iron-sulfur cluster assembly scaffold partner protein, ISU, overview
-
-
-
additional information
?
-
-
no activity with the mitochondrial glycerol-3-phosphate dehydrogenase from Encephalitozoon cuniculi
-
-
-
additional information
?
-
-
the enzyme specifically recognizes mitochondrial preproteins and removes their basic N-terminal signal prepeptides, overview
-
-
-
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
?
-
-
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
?
-
-
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
?
-
Saccharomyces cerevisiae D-273-10B
-
highly specific enzyme, No substrates are several non-mitochondrial proteins
-
-
-
additional information
?
-
Saccharomyces cerevisiae D-273-10B
-
highly specific enzyme, No substrates are several non-mitochondrial proteins, e.g. bovine serum albumin, mouse immunoglobulin G, yeast hexokinase or yeast tryptophan synthase, neither in native nor in heat or pH-denatured form, No substrates are mature mitochondrial proteins, No substrates are denatured enzyme precursors
-
-
-
additional information
?
-
Saccharomyces cerevisiae D-273-10B
-
the large subunit alone has no cleavage activity, removes amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins during or after translocation across mitochondrial membranes
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
COX IV precursor + H2O
processed COX IV + mitochondrial targeting sequence of COX IV
show the reaction diagram
-, Q86A84
-
-
-
?
epidermal growth factor receptor preprotein + H2O
mature epidermal growth factor receptor + prepeptide of epidermal growth factor receptor
show the reaction diagram
-
-
-
-
?
mitochondrial carrier protein + H2O
?
show the reaction diagram
-
the N-terminal extension of plant mitochondrial carrier proteins is removed by two-step processing. The first cleavage is by the mitochondrial processing peptidase
-
-
?
Nfs1 + H2O
processed Nfs1
show the reaction diagram
-
MPP cleaves the precursor between Phe33 and Tyr34, Nfs1 processing, overview
-
-
?
nuclear-encoded polyprotein precursor + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
-
-
?
pre-F1FO-ATP synthase + H2O
mature F1FO-ATP synthase + prepeptide
show the reaction diagram
-
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
-
-
?
mitochondrial glycerol-3-phosphate dehydrogenase + H2O
processed mitochondrial glycerol-3-phosphate dehydrogenase + prepeptide
show the reaction diagram
-
-
-
-
?
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
?
-
-
mitochondrial processing peptidase is essential for viability of Caenorhabditis elegans
-
-
-
additional information
?
-
-
mitosomal substrates of the enzyme are processed to mature proteins in Antonospora locustae with a simplified processing complex, overview
-
-
-
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
?
-
Saccharomyces cerevisiae D-273-10B
-
removes amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins during or after translocation across mitochondrial membranes
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
activation of chelator-inactivated enzyme; metalloprotease
Co2+
-
metalloprotease; requirement
Co2+
-
metalloprotease; requirement (in vitro, in vivo not identified yet)
Co2+
-
activation; metalloprotease
Co2+
-
divalent cation required for enzyme activity
Fe2+
-
divalent cation required for enzyme activity
Fe2+
-
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, the N-terminus blocks previously defined iron-binding sites located on the carboxylate-rich surface defined by the helix alpha1 and the beta-sheet beta1, most likely through electrostatic contact with the carboxylate-rich surface on the core protein, as well as inhibiting iron-promoted binding of the iron-sulfur cluster assembly scaffold partner protein, ISU, overview
Mg2+
-
divalent cation required for enzyme activity
Mn2+
-
metalloprotease; requirement
Mn2+
-
requirement
Mn2+
-
requirement
Mn2+
-
metalloprotease; requirement; requirement (in vitro, in vivo not identified yet)
Zn2+
-
activation of chelator-inactivated enzyme
Zn2+
-
divalent cation required for enzyme activity
Zn2+
-
zinc binding motif in beta-MPP
Zn2+
-
localized in the active site cavity
Zn2+
-
MPP is a zinc-metalloendopeptidase
Zn2+
Q5SIV0
a zinc-metallopeptidase, the betaMPP subunit contains the zinc-binding motif, HxxEHx74E, essential for peptidase activity
Mn2+
-
divalent cation required for enzyme activity
additional information
-
metalloendopeptidase that does not contain His-Glu-X-X-His zinc-binding motif, cf. human insulinase or E. coli protease III
additional information
-
no activation by Ca2+, Mg2+, Cu2+, Ni2+ or Fe2+
additional information
-
atomic absorption spectroscopy: purified MAS1/MAS2-holoenzyme lacks significant amounts of zinc, manganese or cobalt, probably lost during purification
additional information
-
no externally added metal ions required
additional information
-
consensus metal-binding motif HEliH, formed by amino acid residues 167-171 of Atp23
additional information
-
GPP is a metallopeptidase
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
excess Zn2+ or Co2+ partially restores; soluble matrix enzyme
1,10-phenanthroline
-
excess Zn2+ or Co2+ partially restores
1,10-phenanthroline
-
excess Zn2+ or Co2+ partially restores; in vitro and in vivo
1,10-phenanthroline
-
not Zn2+, Ca2+, Mg2+, Cu2+, Ni2+, Fe2+
1,10-phenanthroline
-
excess Mn2+ (bovine, rat) restores
1,10-phenanthroline
-
excess Co2+ (rat) restores; excess Mn2+ (bovine, rat) restores
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
3-Oxoacyl-CoA thiolase signal peptide
-
weak, cytochrome c oxidase subunit IV as substrate
-
Aldehyde dehydrogenase precursor peptide
-
cytochrome c oxidase subunit IV as substrate
-
antisense RNA
-
transformants expressing the anti-sense RNA of the beta subunit of MPP: beta subunit of MPP protein increases about 1.8-fold relative to the wild type, and its mRNA increases 4.5-fold, expression of alpha subunit also increases. Results indicate that expression is induced by the antisense RNA of the MPP's beta subunit gene
-
ARAAARAAARAFAAAA
-
45% residual activity
dithiothreitol
-
partial, 81% inhibition
EDTA
-
excess Zn2+, Co2+ partially restores; soluble matrix enzyme
EDTA
-
excess Co2+ restores; excess Mn2+ restores; excess Zn2+, Co2+ partially restores
EDTA
-
excess Zn2+, Co2+ partially restores
EDTA
-
excess Mn2+ restores; not Zn2+, Ca2+, Mg2+, Cu2+, Ni2+, Fe2+
EDTA
-
excess Mn2+ restores
EDTA
-
GPP is a metallopeptidase
ferricyanide
-
partial, 28% inhibition
GTP
-
soluble matrix enzyme; Zn2+ or Co2+ in excess partially restores
GTP
-
Zn2+ or Co2+ in excess partially restores
IAA
-
affects specifically MPP, less effective than NEM or PCMB, dithioerythritol protects
iodoacetic acid
-
affects specifically MPP, less effective than NEM or PCMB, dithioerythritol protects
Myxothiazol
-
partial, 58% inhibition
N-ethylmaleimide
-
affects specifically MPP, dithioerythritol protects
N-ethylmaleimide
-
not
o-phenanthroline
-
-
o-phenanthroline
-
enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space
PCMB
-
affects specifically MPP, dithioerythritol protects
Peptide pb2(15-34)
-
derived from prepeptide of cytochrome b2 peptide pb2(1-31)
Peptide pF1beta(1-18)
-
derived from prepeptide of beta-subunit of F1-ATP-synthase, much less effective than pF1beta(38-54), N-terminal presequence
Peptide pF1beta(38-54)
-
derived from prepeptide of beta-subunit of F1-ATP-synthase, C-terminal presequence
Prepeptide p25
-
derived from amino terminal of cytochrome oxidase subunit IV precursor, kinetics
Prepeptide p34
-
derived from amino terminal of cytochrome oxidase subunit IV precursor, kinetics
Prepeptide pb2(1-31)
-
derived from cytochrome b2 presequence; kinetics
Prepeptide pb2(1-31)
-
derived from cytochrome b2 presequence
Prepeptide pc1(1-36)
-
derived from cytochrome c1 presequence
-
Prepeptide pF1beta(1-32)
-
derived from beta-subunit of F1-ATPase presequence
Prepeptide pSynC or pSynA2
-
less effective than p25 or p34
-
Rhodanese
-
cytochrome c oxidase subunit IV as substrate
-
Rhodanese signal peptide
-
-
-
Zn2+
-
bovine
Linker-deleted aldehyde dehydrogenase signal peptide
-
weak, cytochrome c oxidase subunit IV as substrate
-
additional information
-
isolated from dog; no inhibition by chymotryptic inhibitors; no inhibition by leupeptin or pepstatin; no inhibition by serine protease inhibitors, e.g. antipain, chymostatin; no inhibition by tryptic inhibitors; pancreas, chicken egg white or soybean
-
additional information
-
4-aminobenzamidine; tosyl-Lys chloromethyl ketone, tosyl-Phe chloromethyl ketone
-
additional information
-
4-aminobenzamidine; diisopropyl fluoride; isolated from bovine; no inhibition by leupeptin or pepstatin; no inhibition by serine protease inhibitors, e.g. antipain, chymostatin; no inhibition by tryptic inhibitors; pancreas, chicken egg white or soybean; PMSF
-
additional information
-
PMSF
-
additional information
-
chicken cystatin; epoxysuccinyl-leucyl agmatine from Aspergillus japonicum (i.e. E-64)
-
additional information
-
prepeptides pSynB2, p15
-
additional information
-
bestatin; no inhibition by leupeptin or pepstatin; PMSF
-
additional information
-
epoxysuccinyl-leucyl agmatine from Aspergillus japonicum (i.e. E-64); no inhibition by antimycin A, myxothiazol; no inhibition by leupeptin or pepstatin; PMSF
-
additional information
-
pb2(1-20)
-
additional information
-
arginine, synthetic helical 22 amino acid peptide derived from heparin-binding domain of antithrombin III (ATIII); pF1beta(51-54), pF1beta(49-54) or pF1beta(44-54)
-
additional information
-
glucagon, bovine serum albumin, rabbit reticulocyte lysate
-
additional information
-
antimycin, phenylmethylsulfonyl fluoride, hemin, pepstatin, and N-ethylmaleimide are no inhibitors
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Processing enhancing protein
-
activation, stimulates MPP protein to full processing activity
-
Triton X-100
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0425
-
ARAARAARAFAASA
-
pH 7.4, 30C
0.0215
-
ARAARAARAFASAA
-
pH 7.4, 30C
0.0074
-
ARAARAARAFATSA
-
pH 7.4, 30C
0.0296
-
ARAARAARAFSAAA
-
pH 7.4, 30C
0.0294
-
ARAARAARAFSASA
-
pH 7.4, 30C
0.0173
-
ARAARAARAFSCSA
-
pH 7.4, 30C
0.0095
-
ARAARAARAFSSAA
-
pH 7.4, 30C
0.0086
-
ARAARAARAFSSSA
-
pH 7.4, 30C
0.0038
-
ARAARAARAFSTAA
-
pH 7.4, 30C
0.0031
-
ARAARAARAFSTSA
-
pH 7.4, 30C
0.0165
-
ARAARAARAFSVSA
-
pH 7.4, 30C
0.0103
-
ARAARAARAFTSSA
-
pH 7.4, 30C
0.015
-
ARAARAARAFTSSA
-
pH 7.4, 30C
0.0098
-
ARAARAARAYGSTA
-
pH 7.4, 30C
0.0101
-
ARAARAARAYGSTA
-
pH 7.4, 30C
0.0108
-
ARAARAARAYSSTA
-
pH 7.4, 30C
0.0079
-
ARAARAARAYSTTA
-
pH 7.4, 30C
0.000063
-
MDH1-21
-
pH 7.5, 25C, mutant E47D
-
0.000074
-
MDH1-21
-
pH 7.5, 25C, wild type
-
0.000085
-
MDH1-21
-
pH 7.5, 25C, mutant E129A
-
0.00011
-
MDH1-21
-
pH 7.5, 25C, mutant E139Aand E75D
-
0.00013
-
MDH1-21
-
pH 7.5, 25C, mutant E129D
-
0.00021
-
MDH1-21
-
pH 7.5, 25C, mutant E77D
-
0.00023
-
MDH1-21
-
pH 7.5, 25C, mutant E75A
-
0.00024
-
MDH1-21
-
pH 7.5, 25C, mutant E77A
-
0.00029
-
MDH1-21
-
pH 7.5, 25C, mutant E47A
-
0.00045
-
MDH1-21
-
pH 7.5, 25C, mutant E79D
-
0.00091
-
MDH1-21
-
pH 7.5, 25C, mutant E79A
-
additional information
-
additional information
-
half-maximal processing of in vitro synthesized precursors to their respective mature forms: F1-ATPase beta-subunit at 1.5 min, cytochrome b2 at 22 min and cytochrome c oxidase at 4 min
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0016
-
MDH1-21
-
pH 7.5, 25C, mutant E79A
-
0.016
-
MDH1-21
-
pH 7.5, 25C, mutant E79D
-
0.06
-
MDH1-21
-
pH 7.5, 25C, mutant E129A
-
0.163
-
MDH1-21
-
pH 7.5, 25C, mutant E129D
-
0.3
-
MDH1-21
-
pH 7.5, 25C, mutant E47A
-
0.533
-
MDH1-21
-
pH 7.5, 25C, mutant E77D
-
0.7
-
MDH1-21
-
pH 7.5, 25C, mutant E47D
-
0.833
-
MDH1-21
-
pH 7.5, 25C, mutant E75D
-
0.916
-
MDH1-21
-
pH 7.5, 25C, mutant E77A
-
1.33
-
MDH1-21
-
pH 7.5, 25C, mutant E139A
-
1.4
-
MDH1-21
-
pH 7.5, 25C, wild type
-
6.08
-
MDH1-21
-
pH 7.5, 25C, mutant E139A; pH 7.5, 25C, mutant E75A; pH 7.5, 25C, mutant E75D; pH 7.5, 25C, mutant E77A; pH 7.5, 25C, mutant E77D
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.000001
-
-
artificial fusion protein
0.000003
-
-
P25-peptide
0.0000298
-
-
ATP synthase subunits 2 and 9
0.0023
-
-
approx., non-specified fluorescent peptide substrate based on the Trichomonas vaginalis adenylate kinase presequence, processing activity measured for the alpha subunit of HPP when associated with beta subunit of HPP
1.785
-
-
strain JKR 102(YEp13-MAS1), overexpressing MAS1
2.35
-
-
strain JKR 102
4.688
-
-
strain JKR 102(pCF35-MAS2), overexpressing MAS2
23.44
-
-
strain JKR 102(YEp13-MAS1 plus pCF35-MAS2), overexpressing MAS1 and MAS2
26.78
-
-
strain VGA
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
activity of the monomeric beta subunit of HPP is at the limit of detection for this assay (almost zero)
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8.5
-
-
7.3
-
-
assay at
8.5
9
-
rat
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.3
8.5
-
about half-maximal activity at pH 6.3 and about 90% of maximal activity at pH 8.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
F1beta-ATPase precursor protein
23
-
-
Rieske FeS precursor protein
37
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
40
-
in vitro processing is markedly impaired below 12C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-, Q86A84
expression analysis of the alpha-subunit of MPP during development, highest levels in vegetatively growing cells and during early development, marked downregulation after 10 h, alpha-MPPL and MPP activities completely disappear around the slug stage, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
beta-MPP, identical with core I protein of ubiquinol cytochrome c reductase complex
Manually annotated by BRENDA team
-
beta and alpha subunit of MPP, Western blot of the mitochondrial subfractions
Manually annotated by BRENDA team
-
beta subunit of MPP, not alpha subunit of MPP, Western blot of the mitochondrial subfractions
Manually annotated by BRENDA team
-
2 components, proteolytic activity bearing, matrix-soluble MPP protein and activating processing enhancing protein which is partly associated with the inner surface of the inner membrane; matrix
Manually annotated by BRENDA team
-
beta-MPP: membrane-associated
Manually annotated by BRENDA team
-
integral part of bc1-complex of respiratory chain
Manually annotated by BRENDA team
-
alpha-MPP: soluble; beta-MPP: membrane-associated
Manually annotated by BRENDA team
Neurospora sp., Rattus norvegicus
-
matrix
Manually annotated by BRENDA team
-
protein complex of the inner mitochondrial membrane
Manually annotated by BRENDA team
-
mitochondrial matrix space
Manually annotated by BRENDA team
-
mitochondrial matrix space
Manually annotated by BRENDA team
-, Q86A84
subcellular localization study, overview
Manually annotated by BRENDA team
Saccharomyces cerevisiae D-273-10B
-
matrix; matrix; matrix
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae MY111-2
-
-
-
Manually annotated by BRENDA team
-
inner membrane, a tiny double-membrane-bounded reduced mitochondrion, the mitosome has no genome and must import all its proteins from the cytosol, scheme of Imp1 and Imp2 in the microsporidian mitosome, overview
Manually annotated by BRENDA team
-
MPP protein
-
Manually annotated by BRENDA team
-
MAS1 becomes insoluble in the absence of MAS2, presumably by aggregation; MAS1 protein
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae D-273-10B
-
-
-
-
Manually annotated by BRENDA team
additional information
-
reduced complexity of targeting pathways in microsporidian mitosomes, overview
-
Manually annotated by BRENDA team
additional information
-
Nfs1 needs to be processed by MPP to be functional in the mitochondrion and the nucleus, the latter case requires a mechanism that involves reverse translocation of processed Nfs1, i.e. the retrograde movement of Nfs1
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
44500
-
-
calculated
47000
-
Q5SIV0
gel filtration, recombinant enzyme
48000
-
-
Saccharomyces cerevisiae, native MAS1 protein, SDS-PAGE
50000
-
-
gel filtration
50000
-
-
gel filtration; Saccharomyces cerevisiae, MAS1
51000
-
-
Saccharomyces cerevisiae, MAS2, SDS-PAGE, MAS1, predicted from DNA sequence
52000
-
-
Neurospora crassa, processing enhancing protein (i.e. PEP), gel filtration at 50 and 300 mM NaCl
52000
-
-
Saccharomyces cerevisiae, analytical sedimentation velocity ultracentrifugation at 20000 rpm, at lower speed aggregates of MW 90000 and MW 240000 occur
53000
-
-
Saccharomyces cerevisiae, MAS2, predicted from DNA-sequence
57000
-
-
Neurospora crassa, MPP, gel filtration at 50 and 300 mM NaCl
59060
-
-
Neurospora crassa, calculated from amino acid sequence
60000
70000
-
rat, bovine, gel filtration
100000
-
-
Saccharomyces cerevisiae, sucrose density gradient centrifugation
100000
-
-
sedimentation velocity analysis
108000
-
-
rat
108000
-
-
gel filtration; rat
additional information
-
-
amino acid sequence comparison on the basis of statistical analysis, FASTP program
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
1 * 48000 (MAS1) + 1 * 51000 (MAS2), Saccharomyces cerevisiae, SDS-PAGE
dimer
-
1 * 52000 + 1 * 55000, rat, SDS-PAGE
dimer
-
1 * 48800 (MAS1) + 1 * 51800 (MAS2), Saccharomyces cerevisiae, calculated from amino acid sequence
dimer
-
1 * 50000 (beta-MPP) + 1 * 53000 (alpha-MPP), rat, recombinant enzyme, SDS-PAGE
dimer
-
MPP is a heterodimeric enzyme consisting of regulatory alpha-MPP and catalytic beta-MPP subunits, 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, plausible model of preEGFP associated with MPP constructed in silico, structure modeling, overview
dimer
Saccharomyces cerevisiae D-273-10B
-
1 * 48000 (MAS1) + 1 * 51000 (MAS2), Saccharomyces cerevisiae, SDS-PAGE
-
heterodimer
-
-
heterodimer
-
consists of a alpha-mitochondrial processing peptidase and beta-MPP
heterodimer
-
alphaMPP and betaMPP
heterodimer
-
alpha and beta subunit of HPP, both subunits required to function most efficiently. Yeast alpha subunit of MPP does not interact with the Trichomonas beta subunit of HPP. Trichomonas alpha subunit of HPP is able to form a heterodimer with yeast beta subunit of MPP
monomer
-
1 * 57000, Neurospora crassa, MPP protein, SDS-PAGE
monomer
-
beta subunit, functions efficiently as a single subunit monomer, data indicate that the monomeric enzyme evolved from an ancestral heterodimeric MPP comprising both an alpha and a beta subunit
monomer
Q5SIV0
1 * 45578, alphabeta, sequence calculation
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); The mitochondrial processing peptidase from Neurospora crassa consists of two components: MPP and processing enhancing protein
additional information
-
Saccharomyces cerevisiae has two loosely associated non-identical subunits that dissociate upon gel filtration; the large subunit alone has no cleavage activity
additional information
-
homology between MAS1 and MAS2 amino acid sequences
additional information
-
MAS2 activity alone is very low, MAS1 restores activity
additional information
-
sequence homologies between P55, P53 from potato and processing enhancing protein from yeast or Neurospora crassa and between P51 from potato and MPP from yeast or Neurospora crassa; the mitochondrial processing peptidase components of cytochrome c reductase-processing peptidase complex are the three largest subunits: P55, P53 and P51, with MW 55000, 53000 and 51000, respectively, SDS-PAGE
additional information
-
processing activity is optimal at a 1:1 molar ratio of alpha- and beta-MPP; subunits do not form a stable complex
additional information
-
alpha-MPP (formerly MAS2) alone has no catalytic activity
additional information
Q5SIV0
TTHA1264 possesses two repetitive domains with a canonical fold for peptidase family M16. The betaMPP subunit contains the zinc-binding motif essential for peptidase activity, while subunit alphaMPP instead possesses a glycine-rich loop, which is proposed to be important for substrate recognition or restriction. Structure analysis, modelling, overview
additional information
Saccharomyces cerevisiae D-273-10B
-
Saccharomyces cerevisiae has two loosely associated non-identical subunits that dissociate upon gel filtration; the large subunit alone has no cleavage activity
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-, Q86A84
the larger form of the alpha-subunit alpha-MPPH is cleaved, removing its N-terminal region, to produce the functional alpha-MPPL form
additional information
-
probably a lipoprotein
additional information
Saccharomyces cerevisiae D-273-10B
-
probably a lipoprotein
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystalline cytochrome bc1 complex
-
crystal structure of the beta-MPP-substrate complex
-
mutant MPP complexed with 2 different synthtic peptide substrates, crystallized by hanging-drop vapor diffusion method, unit cell constants a = 133 A, b = 178 A, c = 201 A, space group P2(1)2(1)2(1)
-
purified recombinant SeMet-labeled enzyme, sitting-drop vapor-diffusion method, 0.001 ml of protein solution containing 22.5 mg/ml protein in 20 mM Tris-HCl (pH 8.0), 150 mM NaCl, and 1 mM DTT, are mixed with 0.001 ml of reservoir solution containing 0.15 M DL-malic acid, pH 7.0, 22% PEG 3350, X-ray diffraction structure determination and analysis at 2.29 A resolution
Q5SIV0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42
-
-
drastic decrease in activity, activated enzyme is unstable and becomes partially denatured
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Stable to 0.3-0.7 M urea
-
Detergents inactivate
-
Separation of the loosely associated subunits of MW 48000 and 51000 causes complete loss of activity
-
Sonication inactivates
-
Highly salt resistant, optimum at 0.9 M, still active at 1.5 M NaCl
-
Separation of subunit III from cytochrome reductase-processing peptidase complex leads to aggregation of the remaining subcomplex and irreversible loss of processing activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, in HEPES buffer, pH 7.4, in the presence of DTT, at least 6 months
-
-70C, after quick-freezing in liquid nitrogen, at least 1 month
-
-70C, partially purified soluble matrix enzyme, several days
-
Stored in liquid nitrogen, up to 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cytochrome bc1 complex
-
recombinant alpha-MPP and native beta-MPP
-
-
Neurospora sp.
-
2 components, a catalytically active MW 55000 and a MW 52000 subunit in a 1:1 ratio
-
alpha- and beta-subunit, isolated as recombinant fusion proteins with maltose-binding protein from Escherichia coli, treated with factor Xa, then separatly purified to homogeneity, active MPP recovered from mixed subunits after denaturation/renaturation procedure
-
histidine-tagged MPP subunits
-
2 components: MAS1 and MAS2; from isolated mitochondria
-
2 components: MAS1 and MAS2; if MAS1 is overproduced in the absence of MAS2 it is insoluble and not suitable for purification, it is therefore purified from the purified holoenzyme; improved procedure
-
from isolated mitochondria; partial
-
from isolated mitochondria; partial; soluble matrix enzyme
-
from soluble matrix fraction of isolated mitochondria
-
hexahistidine-tagged alpha-MPP and E73Q alpha/beta complex
-
hexahistidine-tagged MPP
-
histidine-tagged alpha-MPP subunit
-
native enzyme partially by purification of mitochondria via sucrose gradient centrifugation
-
recombinant alpha- and beta-subunit separatly and as holoenzyme from Escherichia coli lysate
-
recombinant enzyme
-
wild-type and mutant enzyme
-
from isolated mitochondria
-
recombinant MPP from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography, hydroxyapatite chromatography, and gel filtration
Q5SIV0
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Saccharomyces cerevisiae strain JK9-3da/a
-
expression of beta subunit of MPP mRNA is down-regulated during early development, the level of the beta subunit of MPP protein is constant throughout the life cycle
-
gene mppA, encoding subunit alpha-MPP, located on chromosome 2, DNA and amino acid sequence determination and analysis, sequence comparisons, expression of alphaMPP237-GFP, a fusion protein in which the N-terminal 237 amino acids of alpha-MPP are fused to GFP. Expression of mppA is developmentally regulated. Overexpression in Dictyostelium, Development of an alpha-mpp antisense strain is delayed, disruption of the mppA gene is lethal in Dictyostelium
-, Q86A84
expressed in Escherichia coli; Neurospora crassa (alpha-MPP)
-
Neurospora crassa (alpha-MPP); Neurospora crassa (MPP)
-
Neurospora crassa and processing enhancing protein subunit
-
beta-MPP combined with yeast alpha-MPP expressed in soluble monomeric form, each subunit gene cloned into an expression vector pTrc99A and transformed into Escherichia coli BL21(DE3)
-
expressed in Escherichia coli; rat, alpha- and beta-subunit, expressed in Escherichia coli as fusion proteins with maltose-binding protein
-
rat (MPP1 polypeptide)
-
alpha-MPP expressed in soluble monomeric form combined with rat beta-MPP, each subunit gene cloned into an expression vector pTrc99A and transformed into Escherichia coli BL21(DE3)
-
cDNA of the precursor form of alpha and beta-MPP expressed in Escherichia coli BL21
-
coexpression of both subunits results in functionally active enzyme; expressed in Escherichia coli; Saccharomyces cerevisiae
-
E73Q alpha/beta complex expressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli BL21 (DE3)
-
expression of wild-type enzyme and enzyme mutants in DELTA atp23cells
-
Saccharomyces cerevisiae (MAS2)
-
Saccharomyces cerevisiae (wild-type MAS1)
-
wild-type and mutant enzyme overexpressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli; Solanum tuberosum, subunits I-III
-
sequence comparisons, overview, expression in Escherichia coli strain BL21(DE3)
Q5SIV0
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D188A
-
site-directed mutagenesis
D195A
-
site-directed mutagenesis
D195E
-
site-directed mutagenesis
D195N
-
site-directed mutagenesis
D324A
-
site-directed mutagenesis
D413A
-
site-directed mutagenesis
E129A
-
site-directed mutagenesis
E136A
-
site-directed mutagenesis
E136D
-
site-directed mutagenesis
E139A
-
site-directed mutagenesis
E191A
-
site-directed mutagenesis
E191A/D195A
-
site-directed mutagenesis
E191D
-
site-directed mutagenesis
E191Q
-
site-directed mutagenesis
E390Q/D391N
-
site-directed mutagenesis
E420A/D421A
-
site-directed mutagenesis
E47A
-
site-directed mutagenesis
E47D
-
site-directed mutagenesis
E59Q
-
site-directed mutagenesis
E75A
-
site-directed mutagenesis
E75D
-
site-directed mutagenesis
E77A
-
site-directed mutagenesis
E77D
-
site-directed mutagenesis
E79A
-
site-directed mutagenesis
E79D
-
site-directed mutagenesis
H56R
-
site-directed mutagenesis
H60R
-
site-directed mutagenesis
Q190A
-
site-directed mutagenesis
D378N
-
constructed mutant
D405N/D406N
-
constructed mutant
delW481-F482
-
mutation has no effect on protein solubility, slightly unstable during long-term storage
E168Q
-
site-directed mutation in the consensus metal-binding site, the active site residue mutant is proteolytically inactive, but shows processing of the Atp6 subunit of pre-F1FO-ATP synthase
E177G
-
mutation does not affect enzymatic activity
E197Q/E201Q
-
constructed mutant
E217G
-
mutation does not affect enzymatic activity
E351Q
-
constructed mutant
E351Q/D352N/E353Q
-
constructed mutant
E353Q
-
constructed mutant
E377Q
-
constructed mutant
E377Q/D378N
-
constructed mutant
E395D
-
constructed mutant
E73Q
-
alpha/beta complex
E73Q
-
cleavage-deficient mutant
E73Q
-
site-directed mutagenesis, active site mutant, forms dimers like the wild-type enzyme
H167A
-
site-directed mutation in the consensus metal-binding site, the mutant does not show processing of the Atp6 subunit of pre-F1FO-ATP synthase
H171A
-
site-directed mutation in the consensus metal-binding site, the mutant does not show processing of the Atp6 subunit of pre-F1FO-ATP synthase
Q350R
-
mutation does not affect enzymatic activity
R8A
-
constructed mutant
S20A
-
mutation does not affect enzymatic activity
S84P
-
mutation does not affect enzymatic activity
W223F
-
mutation leads to a nearly entirely insoluble protein
W223M
-
mutation leads to an entirely insoluble protein
W481F
-
mutation has no effect on protein solubility
W481H
-
mutation has no effect on protein solubility
W481Y
-
mutation has no effect on protein solubility
additional information
-, Q86A84
construction of alphaMPP237-GFP, a fusion protein in which the N-terminal 237 amino acids of alpha-MPP are fused to GFP for subcellular localization study
additional information
-
yeast malate dehydrogenase and human, yeast, or rat liver aldehyde dehydrogenases are mutated so that they would not be processed by the enzyme after import into the mitochondrial matrix space, the mutant nonprocessed enzymes are functional but instable, the nonprocessed precursors are degraded in the matrix space, expression in HeLa cells, overview
H18A
-
constructed mutant
additional information
-
construction of a EGFP fused to a yeast aconitase presequence and 7-dietylamino-3-(4'-maleimidyl phenyl)-4-methyl coumarin-labelled yeast MPPs for fluorescence resonance energy transfer analysis
additional information
-
yeast aldehyde dehydrogenase and malate dehydrogenase are mutated so that they would not be processed by the enzyme after import into the mitochondrial matrix space, the mutant nonprocessed enzymes are functional but instable, the nonprocessed precursors are degraded in the matrix space, expression in HWTHL10 cells, overview
additional information
-
deletion of ATP23 completely inhibits the assembly of the mitochondrial-encoded FO-subunits into the F1FO-ATP synthase, which is observed in wild-type mitochondria
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
Neurospora sp., Rattus norvegicus
-
MPP which are specific for the soluble form only present in fungi and animals may work as fungicides or insecticides