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 hide
3.4.24.64
-
RECOMMENDED NAME
GeneOntology No.
mitochondrial processing peptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
86280-61-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a fungal intracellular microsporidian parasite
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Encephalitozoon cuniculi
-
-
-
Manually annotated by BRENDA team
strain D-273-10B
-
-
Manually annotated by BRENDA team
strain MY111-2
-
-
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
strain HB8
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Trypansoma brucei
-
-
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
?
show the reaction diagram
-
processing
-
?
Adrenodoxin precursor + H2O
Adrenodoxin
show the reaction diagram
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
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
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 c oxidase subunit IV precursor + H2O
Cytochrome c oxidase subunit IV
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
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
F1-ATPase alpha-subunit precursor + H2O
F1-ATPase alpha-subunit
show the reaction diagram
F1-ATPase beta-subunit precursor + H2O
F1-ATPase beta-subunit
show the reaction diagram
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
-
?
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
mitochondrial glycerol-3-phosphate dehydrogenase + H2O
processed mitochondrial glycerol-3-phosphate dehydrogenase + prepeptide
show the reaction diagram
mitochondrial malate dehydrogenase precursor + H2O
mitochondrial malate dehydrogenase + mitochondiral malate dehydrogenase transit peptide
show the reaction diagram
mitochondrial malate dehydrogenase precursor + H2O
mitochondrial malate dehydrogenase + mitochondrial malate dehydrogenase transit peptide
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
-
-
?
mitochondrial matrix protein precursor + H2O
mitochondrial matrix protein + precursor
show the reaction diagram
Trypansoma brucei
-
-
-
-
?
Mitochondrial proteins with artificial precursors + H2O
?
show the reaction diagram
MLSALARPVGAALARSFSTSA + H2O
?
show the reaction diagram
MPP precursor + H2O
MPP
show the reaction diagram
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
nuclear-encoded polyprotein precursor + H2O
?
show the reaction diagram
Ornithine carbamoyl transferase precursor + H2O
Ornithine carbamoyl transferase intermediate form
show the reaction diagram
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
phosphatase and tensin homologue-induced kinase 1 + H2O
?
show the reaction diagram
-
-
-
-
?
plant mitochondrial carrier proteins + H2O
?
show the reaction diagram
pre-F1FO-ATP synthase + H2O
mature F1FO-ATP synthase + prepeptide
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
presequence-containing protein + H2O
presequence + protein
show the reaction diagram
-
-
-
-
?
Processing enhancing protein precursor + H2O
Processing enhancing protein
show the reaction diagram
processing enhancing protein precursor + H2O
processing enhancing protein + ?
show the reaction diagram
-
-
-
-
?
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
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
-
-
-
TbIscU preprotein + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
-
-
?
mitochondrial glycerol-3-phosphate dehydrogenase + H2O
processed mitochondrial glycerol-3-phosphate dehydrogenase + prepeptide
show the reaction diagram
-
-
-
-
?
mitochondrial matrix protein precursor + H2O
mitochondrial matrix protein + precursor
show the reaction diagram
Trypansoma brucei
-
-
-
-
?
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 preSDHB–RPS14 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 preSDHB–RPS14. 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 (GRD1–30) greatly stimulates processing activity. Constructs with a deletion of an additional ten amino acid residues (GRD1–40) and deletion of 22 amino acid residues in the middle of the GR signal sequence (GRD30–52) 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
?
show the reaction diagram
-
-
-
-
?
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
-
-
?
presequence-containing protein + H2O
presequence + protein
show the reaction diagram
-
-
-
-
?
processing enhancing protein precursor + H2O
processing enhancing protein + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
divalent cation required for enzyme activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
ferricyanide
-
partial, 28% inhibition
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
Linker-deleted aldehyde dehydrogenase signal peptide
-
weak, cytochrome c oxidase subunit IV as substrate
-
Myxothiazol
-
partial, 58% inhibition
N-ethylmaleimide
o-phenanthroline
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)
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
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Processing enhancing protein
-
activation, stimulates MPP protein to full processing activity
-
Triton X-100
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0425
ARAARAARAFAASA
-
pH 7.4, 30°C
0.0215
ARAARAARAFASAA
-
pH 7.4, 30°C
0.0074
ARAARAARAFATSA
-
pH 7.4, 30°C
0.0296
ARAARAARAFSAAA
-
pH 7.4, 30°C
0.0294
ARAARAARAFSASA
-
pH 7.4, 30°C
0.0173
ARAARAARAFSCSA
-
pH 7.4, 30°C
0.0095
ARAARAARAFSSAA
-
pH 7.4, 30°C
0.0086
ARAARAARAFSSSA
-
pH 7.4, 30°C
0.0038
ARAARAARAFSTAA
-
pH 7.4, 30°C
0.0031
ARAARAARAFSTSA
-
pH 7.4, 30°C
0.0165
ARAARAARAFSVSA
-
pH 7.4, 30°C
0.0103 - 0.015
ARAARAARAFTSSA
0.0098 - 0.0101
ARAARAARAYGSTA
0.0108
ARAARAARAYSSTA
-
pH 7.4, 30°C
0.0079
ARAARAARAYSTTA
-
pH 7.4, 30°C
0.000063 - 0.00091
MDH1-21
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016 - 6.08
MDH1-21
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
-
7.5 - 9
-
-
8.5 - 9
-
rat
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
-
in vitro processing is markedly impaired below 12°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
beta subunit of MPP, not alpha subunit of MPP, Western blot of the mitochondrial subfractions
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44500
-
calculated
47000
gel filtration, recombinant enzyme
48000
-
native MAS1 protein, SDS-PAGE
51000
-
isoform MAS2, SDS-PAGE, isoform MAS1, predicted from DNA sequence
53000
-
isoform 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
100000
108000
additional information
-
amino acid sequence comparison on the basis of statistical analysis, FASTP program
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 25000, isoform Plsp1, SDS-PAGE; x * 29000, isoform Plsp2, SDS-PAGE
heterodimer
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42
-
drastic decrease in activity, activated enzyme is unstable and becomes partially denatured
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Detergents inactivate
-
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
-
Separation of the loosely associated subunits of MW 48000 and 51000 causes complete loss of activity
-
Sonication inactivates
-
Stable to 0.3-0.7 M urea
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, after quick-freezing in liquid nitrogen, at least 1 month
-
-70°C, in HEPES buffer, pH 7.4, in the presence of DTT, at least 6 months
-
-70°C, partially purified soluble matrix enzyme, several days
-
Stored in liquid nitrogen, up to 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 components, a catalytically active MW 55000 and a MW 52000 subunit in a 1:1 ratio
-
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
-
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
-
cytochrome bc1 complex
-
from isolated mitochondria
-
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
-
histidine-tagged MPP subunits
-
native enzyme partially by purification of mitochondria via sucrose gradient centrifugation
-
Ni-NTA agarose column chromatography
-
recombinant alpha- and beta-subunit separatly and as holoenzyme from Escherichia coli lysate
-
recombinant alpha-MPP and native beta-MPP
-
recombinant enzyme
-
recombinant MPP from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography, hydroxyapatite chromatography, and gel filtration
wild-type and mutant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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)
-
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)
-
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
-
DNA and amino acid sequence determination and analysis, expression in Saccharomyces cerevisiae strain JK9-3da/a
-
E73Q alpha/beta complex expressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli BL21 (DE3)
-
expressed in Escherichia coli Rosetta (DE3) pLysS cells
-
expressed in Escherichia coli; Neurospora crassa (alpha-MPP)
-
expressed in Escherichia coli; rat, alpha- and beta-subunit, expressed in Escherichia coli as fusion proteins with maltose-binding protein
-
expressed in Escherichia coli; Solanum tuberosum, subunits I-III
-
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
-
expression of wild-type enzyme and enzyme mutants in DELTA atp23cells
-
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
Neurospora crassa (alpha-MPP); Neurospora crassa (MPP)
-
Neurospora crassa and processing enhancing protein subunit
-
rat (MPP1 polypeptide)
-
Saccharomyces cerevisiae (MAS2)
-
Saccharomyces cerevisiae (wild-type MAS1)
-
sequence comparisons, overview, expression in Escherichia coli strain BL21(DE3)
wild-type and mutant enzyme overexpressed in Escherichia coli BL21(DE3)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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
H18A
-
constructed mutant
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
Show AA Sequence (590 entries)
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