Information on EC 3.4.23.49 - omptin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.23.49
-
RECOMMENDED NAME
GeneOntology No.
omptin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val.
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
150770-86-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enterohemorrhagic Escherichia coli, EHEC
-
-
Manually annotated by BRENDA team
enteropathogenic Escherichia coli, EPEC
-
-
Manually annotated by BRENDA team
gene ompT
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
M25
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli W3110
M25
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-AKKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
show the reaction diagram
2-aminobenzoyl-AKRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
show the reaction diagram
-
-
-
?
2-aminobenzoyl-ARKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
show the reaction diagram
2-aminobenzoyl-ARRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
2-aminobenzoyl-Ala-Arg + Arg-Ala-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
show the reaction diagram
-
-
-
?
2-aminobenzoyl-IRRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
2-aminobenzoyl-Ile-Arg + Arg-Ala-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
show the reaction diagram
2-aminobenzoyl-RRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
2-aminobenzoyl-L-Arg + Arg-Ala-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
show the reaction diagram
-
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
show the reaction diagram
a fusion-motilin peptide + H2O
?
show the reaction diagram
-
proteolytic cleavage by mutant D97M at R-R-R-A-R*-motilin
-
-
?
acetyl-Ala-Lys-(D)Arg-Val-Gly-(beta)-Ala + H2O
?
show the reaction diagram
-
-
-
?
alpha-Neo-endorphin + H2O
?
show the reaction diagram
-
cleaved at Arg6-Lys7
-
-
-
alpha-neoendorphin + H2O
?
show the reaction diagram
-
proteolytic cleavage site GFLR*KYPK
-
-
?
alpha2-antiplasmin + H2O
?
show the reaction diagram
ALYKKLLKKLLKSAKKLG + H2O
?
show the reaction diagram
aminobenzoyl-Ala-Arg-Arg-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
show the reaction diagram
-
-
-
?
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
show the reaction diagram
aminobenzoyl-ARRA-Tyr(NO2)-G + H2O
?
show the reaction diagram
-
-
-
?
C18G + H2O
?
show the reaction diagram
calf thymus histone H2B + H2o
?
show the reaction diagram
calf thymus histone H3 + H2o
?
show the reaction diagram
calf thymus histone H4 + H2o
?
show the reaction diagram
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
show the reaction diagram
ColE2-Im2 protein complex + H2O
?
show the reaction diagram
-
a small amount of the endonuclease colicin E2 associated with the cognate immunity protein Im2, is susceptible to proteolytic cleavage by omptin. The presence of outer membrane protein BtuB is required for ColE-Im2 cleavage by omptin. The amount of colicin cleaved is greatly enhanced when ColE2 is dissociated from Im2. Omptin cleaves the C-terminal DNase domain of the toxin. Strains that over-produce OmpT are less susceptible to infection by ColE2 than by ColE2-Im2
-
-
?
colicin E1 + H2O
?
show the reaction diagram
complement C3 + H2O
?
show the reaction diagram
-
Pla proteolyzes complement C3 which may amiliorate the host inflammatory response by abolishing its chemoattractant properties
-
-
?
dynorphin A + H2O
?
show the reaction diagram
dynorphin A(1-13) + H2O
GFLR + RIRPKWDNQ
show the reaction diagram
-
proteolytic cleavage site GFLR*RIRPK
-
-
?
ELELYKRHHG + H2O
ELELYK + RHHG
show the reaction diagram
-
-
-
?
ELRLYKAHHGSG + H2O
ELRLYK + AHHGSG
show the reaction diagram
-
-
-
?
ELRLYKKHHGSG + H2O
ELRLYK + KHHGSG
show the reaction diagram
-
-
-
?
ELRLYKRHHG + H2O
ELRLYK + RHHG
show the reaction diagram
ELRLYKRHHGSG + H2O
ELRLYK + RHHGSG
show the reaction diagram
-
-
-
?
ELRLYKSHHGSG + H2O
ELRLYK + SHHGSG
show the reaction diagram
-
-
-
?
ELRLYRAHHGSG + H2O
ELRLYR + AHHGSG
show the reaction diagram
-
-
-
?
ELRLYRCHHGSG + H2O
ELRLYR + CHHGSG
show the reaction diagram
-
-
-
?
ELRLYRFHHGSG + H2O
ELRLYR + FHHGSG
show the reaction diagram
-
-
-
?
ELRLYRIHHGSG + H2O
ELRLYR + IHHGSG
show the reaction diagram
-
-
-
?
ELRLYRKHHGSG + H2O
ELRLYR + KHHGSG
show the reaction diagram
-
-
-
?
ELRLYRLHHGSG + H2O
ELRLYR + LHHGSG
show the reaction diagram
-
-
-
?
ELRLYRMHHGSG + H2O
ELRLYR + MHHGSG
show the reaction diagram
-
-
-
?
ELRLYRNHHG + H2O
ELRLYR + NHHG
show the reaction diagram
-
-
-
?
ELRLYRNHHGSG + H2O
ELR + LYR + NHHGSG
show the reaction diagram
-
-
-
?
ELRLYRPHHGSG + H2O
ELR + LYRPHHGSG
show the reaction diagram
-
-
-
?
ELRLYRQHHGSG + H2O
ELRLYR + QHHGSG
show the reaction diagram
-
-
-
?
ELRLYRRHHG + H2O
ELRLYR + RHHG
show the reaction diagram
-
-
-
?
ELRLYRRHHGSG + H2O
ELRLYR + RHHGSG
show the reaction diagram
-
-
-
?
ELRLYRSHHGSG + H2O
ELRLYR + SHHGSG
show the reaction diagram
-
-
-
?
ELRLYRTHHGSG + H2O
ELRLYR + THHGSG
show the reaction diagram
-
-
-
?
ELRLYRVHHGSG + H2O
ELRLYR + VHHGSG
show the reaction diagram
-
-
-
?
ELRLYRWHHGSG + H2O
ELR + LYR + WHHGSG
show the reaction diagram
-
-
-
?
ELRLYRYHHGSG + H2O
ELR + LYR + YHHGSG
show the reaction diagram
-
-
-
?
gamma-interferon + H2O
?
show the reaction diagram
-
proteolytic cleavage sites KTGK*RKRSQ and FRGR*RASQ
-
-
?
GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ + H2O
?
show the reaction diagram
H-NS + H2O
?
show the reaction diagram
-
ompT cleaves preferentially at a C-terminal site, cleaves H-NS primarily between residues at positions 88-89 of the protein
-
?
human adrenocorticotropic hormone + H2O
?
show the reaction diagram
-
proteolytic cleavage by mutant D97L at Ser24, release of the hormone
-
-
?
human antiprotease alpha2-antiplasmin + H2O
?
show the reaction diagram
human calcitonin precursor + H2O
?
show the reaction diagram
-
proteolytic cleavage by mutant D97H at an N-terminal Cys
-
-
?
human circulating complement proteins + H2O
?
show the reaction diagram
human creatin kinase + H2O
?
show the reaction diagram
-
proteolytic cleavage site DIYK*KLRDK
-
-
?
human Glu-plasminogen + H2O
plasmin + ?
show the reaction diagram
-
Pla activates Glu-plasminogen to plasmin, in vitro, TFPI is found to be a much better substrate for Pla than plasminogen
-
-
?
human plasminogen + H2O
?
show the reaction diagram
-
proteolytic cleavage site CPGR*VVGGC, activation
-
-
?
human proenzyme plasminogen + H2O
?
show the reaction diagram
human single-chain urokinase + H2O
?
show the reaction diagram
human tissue factor pathway inhibitor + H2O
?
show the reaction diagram
IAA-Arg-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
Inclusion bodies from E. coli solubilized by denaturation + H2O
?
show the reaction diagram
-
-
-
-
-
L-Ala-L-Arg-L-Arg-L-Ala + H2O
L-Ala-L-Arg + L-Arg-L-Ala
show the reaction diagram
-
model peptide substrate
-
-
?
LL-37 + H2O
?
show the reaction diagram
Mastoparan + H2O
?
show the reaction diagram
N-acetyl-Ala-Arg-Arg-Ala-methylamide + H2O
?
show the reaction diagram
fluctuations of outer-membrane protease OmpT in complex with its substrate Ala-Arg-Arg-Ala (ARRA) on microsecond timescale analyzed, effect of key point mutations at the active site studied
-
-
?
o-aminobenzoyl-Ala-Arg-Arg-Ala-3-nitrotyrosine-NH2 + H2O
?
show the reaction diagram
-
-
-
?
OmpT proteolytic site of the GFP + H2O
?
show the reaction diagram
-
the construction of two GFP variants with modified putative OmpT proteolytic sites by site directed mutagenesis is described. Such modified genes upon arabinose induction exhibit varied degrees of GFP fluorescence. While the mutation of K79G/R80A close to the fluorophore results in dramatic loss of fluorescence activity, the modification of K214A/R215A results in four fold enhanced fluorescence of GFP K214A/R215
-
-
?
PAI-1 + H2O
?
show the reaction diagram
-
a serpin
-
-
?
Parathyroid hormone + H2O
?
show the reaction diagram
-
proteolytic cleavage sites EWLR*KKLQD and WLRK*KLQDV
-
-
?
Parathyroid hormone13-34 + H2O
?
show the reaction diagram
-
human, cleaved at both Arg25-Lys26 and Lys26-Lys27
-
-
-
plasminogen + H2O
?
show the reaction diagram
-
poor substrate
no formation of plasmin light chain
-
?
plasminogen + H2O
heavy and light chain of plasmin + ?
show the reaction diagram
-
cleavage at an Arg-Val bond
-
-
Protein expressed from a fusion gene + H2O
?
show the reaction diagram
-
the fusion gene is constructed by ligating the genetic information for the C-terminal 60 amino acids of E. coli hemolysin to the ces gene for a cholesterol esterase/lipase from a Pseudomonas species, OmpT protease preferentially recognizes potential cleavage sites within the linker sequence
-
-
-
rabbit creatine kinase + H2O
?
show the reaction diagram
-
proteolytic cleavage sites DLYK*KLRDK and RGER*RAVEK
-
-
?
Rabbit muscle creatine kinase + H2O
?
show the reaction diagram
-
-
-
-
-
Recombinant human gamma-interferon + H2O
?
show the reaction diagram
-
cleavage between basic amino acids
-
-
-
RLELYKRHHG + H2O
RLELYK + RHHG
show the reaction diagram
-
-
-
?
RLRLYKRHHG + H2O
RLRLYK + RHHG
show the reaction diagram
-
-
-
?
RSANP + H2O
ANP + ?
show the reaction diagram
-
atrial natriuretic peptide
-
?
RSANPR + H2O
ANP + ?
show the reaction diagram
-
atrial natriuretic peptide
-
?
small-molecular-weight chromogenic peptides + H2O
?
show the reaction diagram
-
OmpT, proteolytic cleavage
-
-
?
T7 RNA polymerase + H2O
?
show the reaction diagram
Tryptophan synthase + H2O
?
show the reaction diagram
-
beta-subunit of E. coli enzyme, the wild-type beta-subunit is apparently very stable, the missense mutant beta(B8), carrying an amino acid switch from Gly to Arg at the residue 281, undergoes specific proteolytic cleavage, cleavage products of 30000 MW from the N-terminus and 13000 MW from the C-terminus are observed, cleavage is specific for the peptide bond Arg281-Met282
-
-
-
WCARVGKGRGR-NH2 + H2O
WCA + RVGKGRGR-NH2
show the reaction diagram
-
proteolytic cleavage of the peptide at the site A-R
-
-
?
WEEGGRRIGRGGK + H2O
?
show the reaction diagram
used as a control substrate for determination of the activity of OmpT protease
-
-
?
WEEGGRRIGRGGK-NH2 + H2O
WEEGGR + RIGRGGK-NH2
show the reaction diagram
-
proteolytic cleavage of the peptide at the site R-R, no activity of mutant S223R, preferred substrate of wild-type OmpT
-
-
?
WLAAKKGAG + H2O
?
show the reaction diagram
WLAARRGAG + H2O
?
show the reaction diagram
WLAARRGRG + H2O
?
show the reaction diagram
WLAASRGAG + H2O
?
show the reaction diagram
WLARRRGAG + H2O
?
show the reaction diagram
WLATRRGAG + H2O
?
show the reaction diagram
WLRARRGAG + H2O
?
show the reaction diagram
WLSARRGAG + H2O
?
show the reaction diagram
WLSERRGAG + H2O
?
show the reaction diagram
ZF-RNase-3 + H2O
?
show the reaction diagram
zymogen factor VII + H2O
factor VIIa
show the reaction diagram
-
Pla proteolytically converts zymogen factor VII to the active form, factor VIIa. Pla activates factor VII about twice as fast as it activates plasminogen
-
-
?
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
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
show the reaction diagram
ColE2-Im2 protein complex + H2O
?
show the reaction diagram
-
a small amount of the endonuclease colicin E2 associated with the cognate immunity protein Im2, is susceptible to proteolytic cleavage by omptin. The presence of outer membrane protein BtuB is required for ColE-Im2 cleavage by omptin. The amount of colicin cleaved is greatly enhanced when ColE2 is dissociated from Im2. Omptin cleaves the C-terminal DNase domain of the toxin. Strains that over-produce OmpT are less susceptible to infection by ColE2 than by ColE2-Im2
-
-
?
colicin E1 + H2O
?
show the reaction diagram
-
function in degradation of colicin at the cell surface to protect sensitive cells from infection by colicins suggested
-
-
?
human antiprotease alpha2-antiplasmin + H2O
?
show the reaction diagram
-
involved in infection and pathogenesis
-
-
?
human circulating complement proteins + H2O
?
show the reaction diagram
-
activation of the substrate
-
-
?
human plasminogen + H2O
?
show the reaction diagram
-
proteolytic cleavage site CPGR*VVGGC, activation
-
-
?
human proenzyme plasminogen + H2O
?
show the reaction diagram
small-molecular-weight chromogenic peptides + H2O
?
show the reaction diagram
-
OmpT, proteolytic cleavage
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-aminobenzoyl-A-(L)R-(D)R-A-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
-
arginine
-
-
benzamidine
-
-
calf thymus histone H2B
-
growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 3.8 microM. Histone H2B penetrates the cell membrane of JCM5491 OmpT+ cells
-
calf thymus histone H3
-
growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 10 microM. Histones H3 and H4 remain on the cell surface and subsequently disrupt the cell membrane structure with bleb formation in a manner similar to general antimicrobial peptides
-
calf thymus histone H4
-
growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 12.7 microM. Histones H3 and H4 remain on the cell surface and subsequently disrupt the cell membrane structure with bleb formation in a manner similar to general antimicrobial peptides
-
CuCl2
-
significant inhibition at 1 mM
diisopropylfluorophosphate
lipopolysaccharide
NaCl
-
optimal activity in absence of NaCl, 80% inhibition by 0.15 M NaCl
phenylmethylsulfonyl fluoride
tosyl-L-phenylalanine chloromethyl ketone
-
-
ZnCl2
-
significant inhibition at 1 mM
additional information
-
not: EDTA, phenylmethylsulfonyl fluoride
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
enhances activity
bacterial lipopolysaccharide
-
LPS is required for the enzymatic activity of omptins, and in particular, LPS with short O-antigen side chains (rough LPS) is required for omptin activity toward many exogenous macromolecular substrates. It is thought that an extended O-antigen side chain (smooth LPS) sterically interferes with substrate binding
-
EDTA
-
enhances activity
lipopolysaccharide
lipopolysaccharides
-
Phospholipids
-
lipid-protein interactions
tosyl-L-Lys chloromethyl ketone
-
increases activity
Urea
-
optimal concentration: 4-5 M, inclusion bodies from Escherichia coli as substrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.052
2-aminobenzoyl-AKKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.0083
2-aminobenzoyl-AKRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.0104
2-aminobenzoyl-ARKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.0031
2-aminobenzoyl-ARRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.0036
2-aminobenzoyl-IRRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.0013
2-aminobenzoyl-RRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.56
ELELYKRHHG
-
pH 7.0, 25°C
0.03
ELRLYKRHHG
0.16
ELRLYRNHHG
-
pH 8.3, 37°C
0.53 - 0.79
IAA-Arg-Arg-p-nitroanilide
0.0003 - 0.0011
o-aminobenzoyl-Ala-Arg-Arg-Ala-3-nitrotyrosine-NH2
0.000058 - 0.0036
plasminogen
-
0.0067
RRELRLYRRHHG
-
pH 8.3, 37°C
0.0065
RRLELYKRHHG
-
pH 7.0, 25°C
0.0073 - 0.016
WCARVGKGRGR-NH2
0.023 - 0.055
WEEGGRRIGRGGK
0.055 - 0.26
WEEGGRRIGRGGK-NH2
0.216 - 0.478
WLAAKKGAG
0.059 - 0.11
WLAARRGAG
0.11 - 0.35
WLAARRGRG
0.16 - 0.41
WLAASRGAG
0.008 - 0.19
WLARRRGAG
0.15 - 0.72
WLATRRGAG
0.012 - 0.032
WLRARRGAG
0.057 - 0.11
WLSARRGAG
0.24 - 0.74
WLSERRGAG
additional information
additional information
-
kinetics for phage display generated peptide substrates, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2380
2-aminobenzoyl-AKKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
Escherichia coli
-
pH 8.3, 37°C
738
2-aminobenzoyl-AKRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
Escherichia coli
-
pH 8.3, 37°C
612
2-aminobenzoyl-ARKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
Escherichia coli
-
pH 8.3, 37°C
192
2-aminobenzoyl-ARRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
Escherichia coli
-
pH 8.3, 37°C
84
2-aminobenzoyl-IRRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
Escherichia coli
-
pH 8.3, 37°C
78
2-aminobenzoyl-RRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
Escherichia coli
-
pH 8.3, 37°C
2400
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly
Escherichia coli
-
pH 8.3, 37°C
660
ELELYKRHHG
Escherichia coli
-
pH 7.0, 25°C
3720
ELRLYKRHHG
23.4
ELRLYRNHHG
Escherichia coli
-
pH 8.3, 37°C
1560
ELRLYRRHHG
Escherichia coli
-
pH 8.3, 37°C
0.0035
human Glu-plasminogen
Yersinia pestis
-
pH not specified in the publication, temperature not specified in the publication
-
18 - 24
IAA-Arg-Arg-p-nitroanilide
96 - 2460
o-aminobenzoyl-Ala-Arg-Arg-Ala-3-nitrotyrosine-NH2
378
RLELYKRHHG
Escherichia coli
-
pH 7.0, 25°C
372
RLRLYKRHHG
Escherichia coli
-
pH 7.0, 25°C
0.031 - 2.3
WCARVGKGRGR-NH2
3.4 - 8.8
WEEGGRRIGRGGK
0.0005 - 8.8
WEEGGRRIGRGGK-NH2
1.2 - 13
WLAAKKGAG
8 - 13
WLAARRGAG
130 - 900
WLAARRGRG
0.03 - 0.17
WLAASRGAG
1.2 - 2.2
WLARRRGAG
5 - 9
WLATRRGAG
5 - 37
WLRARRGAG
67 - 168
WLSARRGAG
0.6 - 1.5
WLSERRGAG
additional information
additional information
Escherichia coli K-12
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
2-aminobenzoyl-A-(L)R-(D)R-A-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
plasminogen
6.1
activity assay at; activity assay at
7.2
-
assay at
additional information
-
proteolytic cleavage observed only under neutral conditions
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6
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4: 95% of maximal activity, 6.0: 25% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 45
-
37°C: 40% of maximal activity, 45°C: maximal activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
integral membrane protease, outer membrane, membrane bound
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
SDS-PAGE
33480
-
ESI-MS,positive-ion-mode electrospray ionization mass spectrometry
35540
mass spectrometry
35567
-
x * 35567, calculation from nucleotide sequence
36000
-
x * 36000, SDS-PAGE
180000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
-
-
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
comparison of the structure of Pla and the modeled structure of protease Epo of the plant pathogenic Erwinia pyrifoliae
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hanging drop vapour diffusion method, space group P3(2)21, unit cell parameters a : B : 98.39 A, c : 165.70 A
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PDB 1I78 crystal structure analysis with reversal of mutations A99S, K261G, and G217K required for crystallization
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structure analysis
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
urea
-
ompT is associated in inclusion bodies and active in the presence of high concentrations
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli AN1 cells
-
recombinant protein, gel filtration and SDS-PAGE
-
recombinant wild-type and mutant enzymes
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21, mutation in OmpT protein characterized in BL21 producing fusion protein GST-Sup35NM
expressed in Escherichia coli XL1-Blue, additional strains and plasmids listed, construction of phage libraries and substrate phage described; expressed in Escherichia coli XL1-Blue, additional strains and plasmids listed, construction of phage libraries and substrate phage described
expression in Escherichia coli
expression of wild-type and mutant enzymes
-
gene ompT is located on the chromosome and a cryptic prophage, gene ompP is 95 kb F-plasmid-encoded, phylogenetic tree of the omptin family
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gene ompT, phage display metod used for substrate specificity analysis, expression in Escherichia coli AN1 cells
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gene pla is 9.5 kb plasmid pPCP1 encoded, phylogenetic tree of the omptin family
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inserted into pET-32a, expressed in Escherichia coli
inserted into pTrc99A, expressed in Escherichia coli, additional strains and plasmids of the study listed
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overexpressed without its signal sequence in Escherichia coli K-12 strain DH5alpha using a T7 system
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overexpression of wild-type and mutant enzymes strain W3110 M25
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recombinant expression of OmpT in inclusion bodies
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the gene pgtE is encoded on the chromosome, phylogenetic tree of the omptin family
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the gene plaA is 36 kb plasmid pEP36 encoded, phylogenetic tree of the omptin family
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the gene sopA is 210 kb virulence plasmid pWR100-encoded, phylogenetic tree of the omptin family
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
croP trancription is reduced in DELTAPhoPQ (two-component system composed of the sensor kinase PhoQ and the cognate response regulator PhoP), indicating that croP expression is partly under under the control of PhoP
expression of the ompT gene is higher in EHEC strains than in EPEC strains
OmpT expression levels are higher at 37°C than at 30°C
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D208A
-
introduced as silent mutation in plasmids, transformation with plasmids
D208G
-
site-directed mutagenesis, the mutant enzyme shows increased specificity for the A-R cleavage site compared to the wild-type enzyme
D210A
-
introduced as silent mutation in plasmids, transformation with plasmids
D43A
-
introduced as silent mutation in plasmids, transformation with plasmids
D83A
-
introduced as silent mutation in plasmids, transformation with plasmids
D85A
-
introduced as silent mutation in plasmids, transformation with plasmids
D97C
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97F
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97H
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, preference for human calcitonin precursor, substrate specificity with fusion protein, overview
D97L
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, preference for human adrenocarticotropic hormone, substrate specificity with fusion protein, overview
D97M
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, preference for a fusion peptide substrate with the sequence R-R-R-A-R*-motilin, substrate specificity with fusion protein, overview
D97N
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97Q
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97S
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97T
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
E111A
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introduced as silent mutation in plasmids, transformation with plasmids
E136A
-
introduced as silent mutation in plasmids, transformation with plasmids
E193A
-
introduced as silent mutation in plasmids, transformation with plasmids
E250A
-
introduced as silent mutation in plasmids, transformation with plasmids
E27A
-
introduced as silent mutation in plasmids, transformation with plasmids
G216K/K217G
-
recombinant ompT variant in order to abolish autoproteolysis
H212A
-
molecular mechanics/coarse-grained (MM/CG) simulation applied
S223R
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site-directed mutagenesis, the mutant enzyme shows increased specificity for the A-R cleavage site and overall reduced activity compared to the wild-type enzyme
S99A
-
molecular mechanics/coarse-grained (MM/CG) simulation applied
S99A/G216K/K217G
-
recombinant ompT variant in order to abolish autoproteolysis
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
medicine
pharmacology
studies on treatment of infection by antibiotic-resistant bacteria
Show AA Sequence (181 entries)
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