Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ac-GLLGDFARRAKEKIGC + H2O
Ac-GLLGDFAR + RAKEKIGC
LL37 substrate mutant
-
-
?
Ac-GLLGDFFRKSKEKIGC + H2O
Ac-GLLGDFF + RKSKEKIGC
LL37 substrate mutant, enzyme mutant G216K/K217G shows negligible activity
-
-
?
Ac-GLLGDFFRRVKEKIGC + H2O
Ac-GLLGDFFR + RVKEKIGC
LL37 substrate mutant
-
-
?
dynorphin A + H2O
?
cleavage assay of OmpT protease performed with
-
-
?
N-acetyl-Ala-Arg-Arg-Ala-methylamide + H2O
?
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
-
-
?
WEEGGRRIGRGGK + H2O
?
used as a control substrate for determination of the activity of OmpT protease
-
-
?
WLAAKKGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAARRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAARRGRG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAASRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLARRRGAG + H2O
?
different cleavage sites between OmpT and OmpP protease determined
-
-
?
WLATRRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLRARRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLSARRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLSERRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
2-aminobenzoyl-AKKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
2-aminobenzoyl-AKRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
-
-
-
?
2-aminobenzoyl-ARKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
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
-
-
-
?
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
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
-
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
a fusion-motilin peptide + H2O
?
-
proteolytic cleavage by mutant D97M at R-R-R-A-R*-motilin
-
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
Abz-SLGR + KIQIK(Dnp)-NH2
-
-
-
?
acetyl-Ala-Lys-(D)Arg-Val-Gly-(beta)-Ala + H2O
?
-
-
-
?
alpha-Neo-endorphin + H2O
?
-
cleaved at Arg6-Lys7
-
-
?
aminobenzoyl-Ala-Arg-Arg-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
?
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
aminobenzoyl-ARRA-Tyr(NO2)-G + H2O
?
-
-
-
?
C18G + H2O
?
-
synthetic alpha-helical peptide, whose sequence has been optimized for maximal antibacterial activity
-
-
?
calf thymus histone H2B + H2o
?
-
-
strong fragmentation of histone H2B
-
?
calf thymus histone H3 + H2o
?
-
-
moderate fragmentation of histone H3
-
?
calf thymus histone H4 + H2o
?
-
-
slight fragmentation of histone H4
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
-
OmpT, proteolytic degradation
-
-
?
ColE2-Im2 protein complex + H2O
?
-
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
-
-
?
ELELYKRHHG + H2O
ELELYK + RHHG
-
-
-
?
ELRLYKAHHGSG + H2O
ELRLYK + AHHGSG
-
-
-
?
ELRLYKKHHGSG + H2O
ELRLYK + KHHGSG
-
-
-
?
ELRLYKRHHG + H2O
ELRLYK + RHHG
ELRLYKRHHGSG + H2O
ELRLYK + RHHGSG
-
-
-
?
ELRLYKSHHGSG + H2O
ELRLYK + SHHGSG
-
-
-
?
ELRLYRAHHGSG + H2O
ELRLYR + AHHGSG
-
-
-
?
ELRLYRCHHGSG + H2O
ELRLYR + CHHGSG
-
-
-
?
ELRLYRFHHGSG + H2O
ELRLYR + FHHGSG
-
-
-
?
ELRLYRIHHGSG + H2O
ELRLYR + IHHGSG
-
-
-
?
ELRLYRKHHGSG + H2O
ELRLYR + KHHGSG
-
-
-
?
ELRLYRLHHGSG + H2O
ELRLYR + LHHGSG
-
-
-
?
ELRLYRMHHGSG + H2O
ELRLYR + MHHGSG
-
-
-
?
ELRLYRNHHG + H2O
ELRLYR + NHHG
-
-
-
?
ELRLYRNHHGSG + H2O
ELR + LYR + NHHGSG
-
-
-
?
ELRLYRPHHGSG + H2O
ELR + LYRPHHGSG
-
-
-
?
ELRLYRQHHGSG + H2O
ELRLYR + QHHGSG
-
-
-
?
ELRLYRRHHG + H2O
ELRLYR + RHHG
-
-
-
?
ELRLYRRHHGSG + H2O
ELRLYR + RHHGSG
-
-
-
?
ELRLYRSHHGSG + H2O
ELRLYR + SHHGSG
-
-
-
?
ELRLYRTHHGSG + H2O
ELRLYR + THHGSG
-
-
-
?
ELRLYRVHHGSG + H2O
ELRLYR + VHHGSG
-
-
-
?
ELRLYRWHHGSG + H2O
ELR + LYR + WHHGSG
-
-
-
?
ELRLYRYHHGSG + H2O
ELR + LYR + YHHGSG
-
-
-
?
H-NS + H2O
?
-
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
?
-
proteolytic cleavage by mutant D97L at Ser24, release of the hormone
-
-
?
human calcitonin precursor + H2O
?
-
proteolytic cleavage by mutant D97H at an N-terminal Cys
-
-
?
human LL-37 + H2O
?
a cathelicidin
-
-
?
human proenzyme plasminogen + H2O
?
-
low activity of OmpT in activation of the substrate, proteolytic cleavage
-
-
?
human single-chain urokinase + H2O
?
-
-
cleavage at the peptide bond Lys158-Ile159, the site cleaved also by the physiological activator human plasmin
-
?
human tissue factor pathway inhibitor + H2O
?
-
it is hypothesized that TFPI evolved sensitivity to proteolytic inactivation by bacterial omptins to potentiate procoagulant responses to bacterial infection which may contribute to the hemostatic imbalance in disseminated intravascular coagulation and other coagulopathies accompanying severe sepsis
-
-
?
IAA-Arg-Arg-p-nitroanilide + H2O
?
-
-
-
?
Inclusion bodies from E. coli solubilized by denaturation + H2O
?
-
-
-
-
?
L-Ala-L-Arg-L-Arg-L-Ala + H2O
L-Ala-L-Arg + L-Arg-L-Ala
-
model peptide substrate
-
-
?
LL-37 + H2O
?
-
human antimicrobial peptide of the cathelicidin family, cleavage occurs at dibasic sites
-
-
?
Mastoparan + H2O
?
-
cleavage at Lys11-Lys12
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
CRAMP
-
-
?
o-aminobenzoyl-Ala-Arg-Arg-Ala-3-nitrotyrosine-NH2 + H2O
?
-
-
-
?
OmpT proteolytic site of the GFP + H2O
?
-
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
-
-
?
Parathyroid hormone13-34 + H2O
?
-
human, cleaved at both Arg25-Lys26 and Lys26-Lys27
-
-
?
plasminogen + H2O
heavy and light chain of plasmin + ?
-
cleavage at an Arg-Val bond
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
Protein expressed from a fusion gene + H2O
?
-
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 muscle creatine kinase + H2O
?
-
-
-
-
?
Recombinant human gamma-interferon + H2O
?
-
cleavage between basic amino acids
-
-
?
RLELYKRHHG + H2O
RLELYK + RHHG
-
-
-
?
RLRLYKRHHG + H2O
RLRLYK + RHHG
-
-
-
?
RRELRLYRRHHG + H2O
?
-
-
-
-
?
RRLELYKRHHG + H2O
?
-
-
-
-
?
RSANP + H2O
ANP + ?
-
atrial natriuretic peptide
-
?
RSANPR + H2O
ANP + ?
-
atrial natriuretic peptide
-
?
small-molecular-weight chromogenic peptides + H2O
?
-
OmpT, proteolytic cleavage
-
-
?
T7 RNA polymerase + H2O
?
Tryptophan synthase + H2O
?
-
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
-
proteolytic cleavage of the peptide at the site A-R
-
-
?
WEEGGRRIGRGGK + H2O
?
used as a control substrate for determination of the activity of OmpT protease
-
-
?
WEEGGRRIGRGGK-NH2 + H2O
WEEGGR + RIGRGGK-NH2
-
proteolytic cleavage of the peptide at the site R-R, no activity of mutant S223R, preferred substrate of wild-type OmpT
-
-
?
WLAAKKGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAARRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAARRGRG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAASRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLARRRGAG + H2O
?
different cleavage sites between OmpP and OmpT protease determined
-
-
?
WLATRRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLRARRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLSARRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLSERRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
additional information
?
-
colicin E1 + H2O
?
function in degradation of colicin at the cell surface to protect sensitive cells from infection by colicins suggested
-
-
?
colicin E1 + H2O
?
cleavage by involvement of OmpT proteases determined by SDS-PAGE, processing site determined
-
-
?
LL37 + H2O
?
a human antimicrobial peptide of the cathelicidin family
-
-
?
LL37 + H2O
?
a human antimicrobial peptide of the cathelicidin family, wild-type LL37 sequence has 2 dibasic sites that can be cleaved by OmpT
-
-
?
2-aminobenzoyl-AKKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
-
-
-
-
?
2-aminobenzoyl-AKKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
-
-
-
?
2-aminobenzoyl-ARKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
-
-
-
-
?
2-aminobenzoyl-ARKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
-
FRET-substrate, derived from the protein C2 of the classical complement pathway
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
-
FRET-substrate, derived from the protein C2 of the classical complement pathway. Poor substrate
-
-
?
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
-
?
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
?
dynorphin A + H2O
?
-
-
-
?
dynorphin A + H2O
?
-
-
-
?
dynorphin A + H2O
?
-
cleavage at Arg6-Arg7
-
-
?
dynorphin A + H2O
?
-
proteolytic cleavage, commercial peptide substrate
-
-
?
ELRLYKRHHG + H2O
ELRLYK + RHHG
-
-
-
?
ELRLYKRHHG + H2O
ELRLYK + RHHG
-
-
-
?
T7 RNA polymerase + H2O
?
-
-
-
-
?
T7 RNA polymerase + H2O
?
-
cleavage at Lys-Arg173, Lys-Lys180, and Arg-Lys392
-
-
?
additional information
?
-
OmpT shown to be one of the critical outer membrane protein responsible for chloramphenicol resistance, analysis by comparative proteomics and mutant investigation
-
-
?
additional information
?
-
studies on application of the infectivity-modulated phage display IMOP, applied to determine substrate specificity, protease ompT exemplary tested indicating enrichment of double-arginine motifs, IMOP system shown to improve previous techniques basing on phage display
-
-
?
additional information
?
-
analysis of protease activity for the preferred residues at the cleavage site (P1, P1') and nearest-neighbor positions (P2, P2') and their positional interdependence revealed FRRV as the optimal peptide with the highest OmpT activity. Substituting FRRV into a fragment of LL37, a natural substrate of OmpT, leads to a greater than 400fold improvement in OmpT catalytic efficiency. Wild-type and mutant OmpT display significant differences in their substrate specificities. Substrate consensus sequence screening, substrate specificity, overview. Twelve tetrapeptides display higher activity for wild-type OmpT than does the ARRA peptide, which has an activity of 91.0%, kinetic comparison of peptide substrates that are inserted into the LL37 fragment
-
-
?
additional information
?
-
-
not cleaved: insulin B-chain, parathyroid hormone 13-26 and 26-34, small synthetic substrates e.g. Lys-Lys-Leu-Gln-Asp-Val-His-Asn-Phe
-
-
?
additional information
?
-
-
t-butyloxycarbonyl-Leu-Gly-Arg 4-methylcoumarin 7-amide
-
-
?
additional information
?
-
-
preference for denatured substrates
-
-
?
additional information
?
-
-
endopeptidase specifically recognizing and cleaving consecutive basic residues
-
-
?
additional information
?
-
-
able to process recombinant fusion proteins such as cholesterol esterase/lipase, cholera toxin B subunit, and recombinant Staphylococcus aureus V8 protease derivative, peptides containing an acidic residue at P2 or P2' are not substrates, RD-ELRLYRDHHG is no substrate
-
?
additional information
?
-
-
little or no reaction with aminobenzoylfluorophore-ARIA-(dinitrophenyl)diaminopropionic acid quencher-G and aminobenzoylfluorophore-ARRIA-3-(dinitrophenyl)diaminopropionic acid quencher-G, acetyl-3-(dinitrophenyl)diaminopropionic acid-Ala-Arg-Arg-Ala-Lys(aminobenzoyl)-Gly is no substrate, no hydrolytic activity toward aminobenzoylfluorophore-A-(D)R-(L)R-A-3-(dinitrophenyl)diaminopropionic acid quencher-G, aminobenzoylfluorophore-A-(L)R-(D)R-A-3-(dinitrophenyl)diaminopropionic acid quencher-G and aminobenzoylfluorophore-A-(D)R-(D)R-A-3-(dinitrophenyl)diaminopropionic acid quencher-G
-
?
additional information
?
-
-
activity under extreme denaturing condition
-
-
?
additional information
?
-
-
cleaves peptides between two consecutive basic amino acids
-
?
additional information
?
-
-
cleaves peptides between two consecutive basic amino acids
-
?
additional information
?
-
-
cleaves peptides between two consecutive basic amino acids
-
?
additional information
?
-
-
enzyme is suggested to be involved in urinary tract disease, in DNA excision repair, and in the breakdown of antimicrobial peptides, but its actual biological function remains to be elucidated
-
?
additional information
?
-
-
the enzyme is involved in cell defense and induced production of TNFalpha, especially in clinical isolates, the enzyme is not stimulated by toll-like receptors 2 and 4 signalling
-
-
?
additional information
?
-
-
the multifunctional enzyme has a virulence-associated function in protein degradation
-
-
?
additional information
?
-
-
protein-lipid interactions on model membranes and human mononuclear cells, overview
-
-
?
additional information
?
-
-
substrate specificity, OmpT shows no activity with antiprotease alpha2-antiplasmin, minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme
-
-
?
additional information
?
-
EHEC OmpT degrades LL-37 and CRAMP at similar rates. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions
-
-
?
additional information
?
-
-
EHEC OmpT degrades LL-37 and CRAMP at similar rates. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
comparative proteome analysis of chloramphenicol-resistant Escherichia coli, two-dimensional electrophoresis, MALDI-TOF mass spectroscopy and Western blotting performed, differential protein expression profiles with and without chloramphenicol treatment shown, antimicrobial susceptibility tested, OmpT protease identified as critically altered protein in chloramphenicol-resistant Escherichia coli, mutant analysis performed
additional information
effects of OmpT protease on colony-forming ability and production of fibrous protein polymers determined, involvement of OmpT protease in protein quality control within the cell discussed
additional information
phage display applied to analyse substrate specificity of OmpT protease in comparison to OmpP protease, different substrate specificities between OmpT and OmpP proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
phage display applied to analyse substrate specificity of OmpT protease in comparison to OmpP protease, different substrate specificities between OmpT and OmpP proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
-
phage display applied to analyse substrate specificity of OmpT protease in comparison to OmpP protease, different substrate specificities between OmpT and OmpP proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
strains expressing OmpT protease shown to cleave colicin E1 at the residues K84 and K95 in the N-terminal translocation domain, leading to the removal of the TolQA box essential for cytotoxicity of colicin E1, in vivo data indicating effects of OmpT protease on colicin E1 cell-killing activity shown
additional information
structural and functional relationships for wild-type and mutated OmpT proteins investigated, relevant case of the Michaelis complex of the outer-membrane protease T (OmpT) analyzed by a hybrid molecular mechanics/coarse-grained (MM/CG) approach, structural explanation for decreased catalytic activity of the mutants S99A and H212A given
additional information
-
structural and functional relationships for wild-type and mutated OmpT proteins investigated, relevant case of the Michaelis complex of the outer-membrane protease T (OmpT) analyzed by a hybrid molecular mechanics/coarse-grained (MM/CG) approach, structural explanation for decreased catalytic activity of the mutants S99A and H212A given
additional information
studies on development of a new substrate phage system, construction of a random hexapeptide library described, selection of the phage display library with OmpT protease to demonstrate application of the infectivity-modulated phage display IMOP
additional information
-
-
additional information
-
enzyme-LPS activity in endotoxin units
additional information
phage display applied to analyse substrate specificity of OmpP protease in comparison to OmpT protease, different substrate specificities between OmpP and OmpT proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
phage display applied to analyse substrate specificity of OmpP protease in comparison to OmpT protease, different substrate specificities between OmpP and OmpT proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
-
phage display applied to analyse substrate specificity of OmpP protease in comparison to OmpT protease, different substrate specificities between OmpP and OmpT proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
G216K/K217G
site-directed mutagenesis, mutation to remove the dibasic proteolysis site. The mutant has a circa 30% lower activity than wild-type OmpT
H212A
molecular mechanics/coarse-grained (MM/CG) simulation applied
S99A
molecular mechanics/coarse-grained (MM/CG) simulation applied
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
-
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
-
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
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97T
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
E111A
-
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
S223R
-
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/G216K/K217G
-
recombinant ompT variant in order to abolish autoproteolysis
D97A
-
introduced as silent mutation in plasmids, transformation with plasmids
D97A
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
additional information
complementation of strain BL21 producing fusion protein GST-Sup35NM with the wild-type OmpT-gene restores colony-forming ability
additional information
referring to the classical Lpp-OmpA (LOA) display system, the signal peptide and nine amino acids of the mature outer membrane prolipoprotein Lpp are fused to the transmembrane domain comprising five beta-strands of truncated OmpT to generate a Lpp-OmpT (LOT) display system. The C-terminal fusion strategy is used to fuse a small peptide (His tag) and red fluorescent protein (mCherry) to the C-terminus of LOT. Exposed histidine tags present in recombinant proteins form complexes with transition metal ions such as Ni2+, Zn2+, Cu2+, and Fe3+. Adsorption analysis of cells expressing the chimeric mutant protein using Cu2+, adhesion of surface engineered cells to Cu2+-chelating sepharose beads, method evaluation, overview
additional information
-
referring to the classical Lpp-OmpA (LOA) display system, the signal peptide and nine amino acids of the mature outer membrane prolipoprotein Lpp are fused to the transmembrane domain comprising five beta-strands of truncated OmpT to generate a Lpp-OmpT (LOT) display system. The C-terminal fusion strategy is used to fuse a small peptide (His tag) and red fluorescent protein (mCherry) to the C-terminus of LOT. Exposed histidine tags present in recombinant proteins form complexes with transition metal ions such as Ni2+, Zn2+, Cu2+, and Fe3+. Adsorption analysis of cells expressing the chimeric mutant protein using Cu2+, adhesion of surface engineered cells to Cu2+-chelating sepharose beads, method evaluation, overview
additional information
-
random mutagenesis of gene ompT, screening for mutant variants with altered cleavage specificity, e.g. mutant variants 1.2.19 and 1.3.19 exhibits higher specificity for the cleavage site A-R and lower specificity for R-R than the wild-type
additional information
generation of a deletion mutant DELTAompT
additional information
-
generation of a deletion mutant DELTAompT
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Sugimura, K.; Nishihara, T.
Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues: identity of protease VII and OmpT
J. Bacteriol.
170
5625-5632
1988
Escherichia coli
brenda
Hanke, C.; Hess, J.; Schumacher, G.; Goebel, W.
Processing by OmpT of fusion proteins carrying the HlyA transport signal during secretion by the Escherichia coli hemolysin transport system
Mol. Gen. Genet.
233
42-48
1992
Escherichia coli
brenda
Grodberg, J.; Lundrigan, M.D.; Toledo, D.L.; Mangel, W.F.; Dunn, J.J.
Complete nucleotide sequence and deduced amino acid sequence of the ompT gene of Escherichia coli K-12
Nucleic Acids Res.
16
1209
1988
Escherichia coli
brenda
Mangel, W.F.; Toledo, D.L.; Brown, M.T.; Worzalla, K.; Lee, M.; Dunn, J.J.
Omptin: an Escherichia coli outer membrane proteinase that activates plasminogen
Methods Enzymol.
244
384-399
1994
Escherichia coli
brenda
White, C.B.; Chen, Q.; Kenyon, G.L.; Babbitt, P.C.
A novel activity of OmpT. Proteolysis under extreme denaturing conditions
J. Biol. Chem.
270
12990-12994
1995
Escherichia coli
brenda
Zhao, G.P.; Somerville, R.L.
An amino acid switch (Gly281-->Arg) within the hinge region of the tryptophan synthase beta subunit creates a novel cleavage site for the OmpT protease and selectively diminishes affinity toward a specific monoclonal antibody
J. Biol. Chem.
268
14912-14920
1993
Escherichia coli
brenda
Dekker, N.; Cox, R.C.; Kramer, R.A.; Egmond, M.R.
Substrate specificity of the integral membrane protease ompT determined by spatially addressed peptide libraries
Biochemistry
40
1694-1701
2001
Escherichia coli
brenda
Goldberg, M.D.; Canvin, J.R.; Freestone, P.; Andersen, C.; Laoudj, D.; Williams, P.H.; Holland, I.B.; Norris, V.
Artifactual cleavage of E. coli H-NS by OmpT
Biochimie
79
315-322
1997
Escherichia coli
brenda
Okuno, K.; Yabuta, M.; Kawanishi, K.; Ohsuye, K.; Ooi, T.; Kinoshita, S.
Substrate specificity at the P1' site of Escherichia coli OmpT under denaturing conditions
Biosci. Biotechnol. Biochem.
66
127-134
2002
Escherichia coli, no activity in Escherichia coli, no activity in Escherichia coli W3110 / ATCC 27325
brenda
Okuno, K.; Yabuta, M.; Ohsuye, K.; Ooi, T.; Kinoshita, S.
An analysis of target preferences of Escherichia coli outer-membrane endoprotease OmpT for use in therapeutic peptide production: efficient cleavage of substrates with basic amino acids at the P4 and P6 positions
Biotechnol. Appl. Biochem.
36
77-84
2002
Escherichia coli, no activity in Escherichia coli, no activity in Escherichia coli W3110 / ATCC 27325
brenda
Vandeputte-Rutten, L.; Kramer, R.A.; Kroon, J.; Dekker, N.; Egmond, M.R.; Gros, P.
Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
EMBO J.
20
5033-5039
2001
Escherichia coli
brenda
Kramer, R.A.; Zandwijken, D.; Egmond, M.R.; Dekker, N.
In vitro folding, purification and characterization of Escherichia coli outer membrane protease OmpT
Eur. J. Biochem.
267
885-893
2000
Escherichia coli
brenda
Kramer, R.A.; Vandeputte-Rutten, L.; de Roon, G.J.; Gros, P.; Dekker, N.; Egmond, M.R.
Identification of essential acidic residues of outer membrane protease OmpT supports a novel active site
FEBS Lett.
505
426-430
2001
Escherichia coli
brenda
Okuno, K.; Yabuta, M.; Ooi, T.; Kinoshita, S.
Utilization of Escherichia coli outer-membrane endoprotease OmpT variants as processing enzymes for production of peptides from designer fusion proteins
Appl. Environ. Microbiol.
70
76-86
2004
Escherichia coli
brenda
Baaden, M.; Sansom, M.S.
OmpT: molecular dynamics simulations of an outer membrane enzyme
Biophys. J.
87
2942-2953
2004
Escherichia coli
brenda
Brandenburg, K.; Garidel, P.; Schromm, A.B.; Andra, J.; Kramer, A.; Egmond, M.; Wiese, A.
Investigation into the interaction of the bacterial protease OmpT with outer membrane lipids and biological activity of OmpT:lipopolysaccharide complexes
Eur. Biophys. J.
34
28-41
2005
Escherichia coli
brenda
Kukkonen, M.; Korhonen, T.K.
The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis
Int. J. Med. Microbiol.
294
7-14
2004
Erwinia pyrifoliae, Escherichia coli, Salmonella enterica, Shigella flexneri, Yersinia pestis
brenda
Varadarajan, N.; Gam, J.; Olsen, M.J.; Georgiou, G.; Iverson, B.L.
Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity
Proc. Natl. Acad. Sci. USA
102
6855-6860
2005
Escherichia coli
brenda
Neri, M.; Baaden, M.; Carnevale, V.; Anselmi, C.; Maritan, A.; Carloni, P.
Microseconds dynamics simulations of the outer-membrane protease T
Biophys. J.
94
71-78
2008
Escherichia coli (P09169), Escherichia coli
brenda
Ono, B.; Kimiduka, H.; Kubota, M.; Okuno, K.; Yabuta, M.
Role of the ompT mutation in stimulated decrease in colony-forming ability due to intracellular protein aggregate formation in Escherichia coli strain BL21
Biosci. Biotechnol. Biochem.
71
504-512
2007
Escherichia coli (P09169)
brenda
Chaparro-Riggers, J.F.; Breves, R.; Maurer, K.H.; Bornscheuer, U.
Modulation of infectivity in phage display as a tool to determine the substrate specificity of proteases
Chembiochem
7
965-970
2006
Escherichia coli (P09169)
brenda
Masi, M.; Vuong, P.; Humbard, M.; Malone, K.; Misra, R.
Initial steps of colicin E1 import across the outer membrane of Escherichia coli
J. Bacteriol.
189
2667-2676
2007
Escherichia coli (P09169)
brenda
Hwang, B.Y.; Varadarajan, N.; Li, H.; Rodriguez, S.; Iverson, B.L.; Georgiou, G.
Substrate specificity of the Escherichia coli outer membrane protease OmpP
J. Bacteriol.
189
522-530
2007
Escherichia coli (P09169), Escherichia coli (P34210), Escherichia coli
brenda
Li, H.; Lin, X.M.; Wang, S.Y.; Peng, X.X.
Identification and antibody-therapeutic targeting of chloramphenicol-resistant outer membrane proteins in Escherichia coli
J. Proteome Res.
6
3628-3636
2007
Escherichia coli (P09169)
brenda
Duche, D.; Issouf, M.; Lloubes, R.
Immunity protein protects colicin E2 from OmpT protease
J. Biochem.
145
95-101
2009
Escherichia coli
brenda
Yun, T.; Cott, J.; Tapping, R.; Slauch, J.; Morrissey, J.
Proteolytic inactivation of tissue factor pathway inhibitor by bacterial omptins
Blood
113
1139-1148
2009
Escherichia coli, Salmonella enterica
brenda
Salunkhe, S.S.; Raiker, V.A.; Rewanwar, S.; Kotwal, P.; Kumar, A.; Padmanabhan, S.
Enhanced fluorescent properties of an OmpT site deleted mutant of green fluorescent protein
Microb. Cell Fact.
9
26
2010
Escherichia coli
brenda
Thomassin, J.L.; Brannon, J.R.; Gibbs, B.F.; Gruenheid, S.; Le Moual, H.
OmpT outer membrane proteases of enterohemorrhagic and enteropathogenic Escherichia coli contribute differently to the degradation of Human LL-37
Infect. Immun.
80
483-492
2012
Escherichia coli, Escherichia coli EHEC O157:H7, Escherichia coli EPEC / E2348/69
brenda
Hui, C.Y.; Guo, Y.; He, Q.S.; Peng, L.; Wu, S.C.; Cao, H.; Huang, S.H.
Escherichia coli outer membrane protease OmpT confers resistance to urinary cationic peptides
Microbiol. Immunol.
54
452-459
2010
Escherichia coli, Escherichia coli E44
brenda
Tagai, C.; Morita, S.; Shiraishi, T.; Miyaji, K.; Iwamuro, S.
Antimicrobial properties of arginine- and lysine-rich histones and involvement of bacterial outer membrane protease T in their differential mode of actions
Peptides
32
2003-2009
2011
Escherichia coli, Escherichia coli JCM 5491
brenda
Jaervinen, H.M.; Laakkonen, L.; Haiko, J.; Johansson, T.; Juuti, K.; Suomalainen, M.; Buchrieser, C.; Kalkkinen, N.; Korhonen, T.K.
Human single-chain urokinase is activated by the omptins PgtE of Salmonella enterica and Pla of Yersinia pestis despite mutations of active site residues
Mol. Microbiol.
89
507-517
2013
Escherichia coli, Salmonella enterica, Salmonella enterica 14028R, Yersinia pestis (P17811), Yersinia pestis
brenda
Wood, S.E.; Sinsinbar, G.; Gudlur, S.; Nallani, M.; Huang, C.F.; Liedberg, B.; Mrksich, M.
A bottom-up proteomic approach to identify substrate specificity of outer-membrane protease OmpT
Angew. Chem. Int. Ed. Engl.
56
16531-16535
2017
Escherichia coli (P09169)
brenda
Hui, C.Y.; Guo, Y.; Liu, L.; Zheng, H.Q.; Wu, H.M.; Zhang, L.Z.; Zhang, W.
Development of a novel bacterial surface display system using truncated OmpT as an anchoring motif
Biotechnol. Lett.
41
763-777
2019
Escherichia coli (P09169), Escherichia coli
brenda
Brannon, J.R.; Burk, D.L.; Leclerc, J.M.; Thomassin, J.L.; Portt, A.; Berghuis, A.M.; Gruenheid, S.; Le Moual, H.
Inhibition of outer membrane proteases of the omptin family by aprotinin
Infect. Immun.
83
2300-2311
2015
Citrobacter rodentium, Escherichia coli (P09169), Escherichia coli
brenda
Brannon, J.R.; Thomassin, J.L.; Gruenheid, S.; Le Moual, H.
Antimicrobial peptide conformation as a structural determinant of omptin protease specificity
J. Bacteriol.
197
3583-3591
2015
Citrobacter rodentium, Escherichia coli (P58603), Escherichia coli, Citrobacter rodentium ATCC 51459, Citrobacter rodentium DBS 100, Escherichia coli EDL933 (P58603)
brenda
Feodorova, V.A.; Lyapina, A.M.; Zaitsev, S.S.; Khizhnyakova, M.A.; Sayapina, L.V.; Ulianova, O.V.; Ulyanov, S.S.; Motin, V.L.
New promising targets for synthetic omptin-based peptide vaccine against Gram-negative pathogens
Vaccines (Basel)
7
36
2019
Salmonella enterica subsp. enterica serovar Typhimurium (P06185), Escherichia coli (P09169), Escherichia coli (P34210), Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (P06185), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (P06185)
brenda