3.4.23.49: omptin
This is an abbreviated version!
For detailed information about omptin, go to the full flat file.
Word Map on EC 3.4.23.49
-
3.4.23.49
-
furin
-
usp7
-
ubiquitin-specific
-
endoproteolytic
-
convertase
-
proproteins
-
deubiquitinating
-
prohormone
-
subtilisin-like
-
dibasic
-
yersinia
-
pestis
-
deubiquitinase
-
trans-golgi
-
propeptide
-
farnesylated
-
subtilisins
-
plague
-
kex2-like
-
lys-arg
-
proinsulins
-
prelamin
-
proregions
-
furin-like
-
flexneri
-
monobasic
-
deubiquitylation
-
exoprotease
-
zmpste24
-
isoprenylated
-
arg-arg
-
pharmacology
-
food industry
-
biotechnology
-
medicine
- 3.4.23.49
- furin
- usp7
-
ubiquitin-specific
-
endoproteolytic
-
convertase
- proproteins
-
deubiquitinating
-
prohormone
-
subtilisin-like
-
dibasic
- yersinia
- pestis
-
deubiquitinase
-
trans-golgi
- propeptide
-
farnesylated
- subtilisins
- plague
-
kex2-like
- lys-arg
- proinsulins
-
prelamin
-
proregions
-
furin-like
- flexneri
-
monobasic
-
deubiquitylation
-
exoprotease
- zmpste24
-
isoprenylated
- arg-arg
- pharmacology
- food industry
- biotechnology
- medicine
Reaction
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. =
Synonyms
bacterial outer-membrane protease, Citrobacter rodentium outer-membrane protease, CroP, E. coli protease VII, EC 3.4.21.87, endoprotease, Gene ompT proteins, More, OmpP, OmpP protease, ompT, OmpT protease, OmpT protein, Omptin, omptin protease, outer membrane protease, Outer membrane protein 3B, outer-membrane protease, outer-membrane protease T, PgtE, Pla, plaA, protease 7, Protease A, Protease VII, Protein a, Proteins, specific or class, gene ompT, SopA
ECTree
3.4.23.49 omptinAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.49 - omptin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-AKRA-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-KLKSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLK + SSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
2-aminobenzoyl-KLRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLR + SSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
2-aminobenzoyl-KLRSSVQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLR + SSVQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
2-aminobenzoyl-KMRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KMR + SSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
2-aminobenzoyl-KNRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KNR + SSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
2-aminobenzoyl-KQRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KQR + SSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
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
-
-
?
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
-
-
?
ALYKKLLKKLLKSAKKLG + H2O
?
synthetic alpha-antimicrobial peptide L-C18G, D-amino acids are not degraded by CroP
-
-
?
aminobenzoyl-Ala-Arg-Arg-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
?
cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP, a murine cathelicidin-related antimicrobial peptide
-
-
?
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
-
-
?
dynorphin A(1-13) + H2O
Tyr-Gly-Gly-Phe-Leu-Arg + Arg-Ile-Arg-Pro-Lys-Leu-Lys
-
proteolytic cleavage site GFLR*RIRPK
-
-
?
gamma-interferon + H2O
?
-
proteolytic cleavage sites KTGK*RKRSQ and FRGR*RASQ
-
-
?
gelatine + H2O
?
degradation
-
-
?
GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ + H2O
?
synthetic alpha-antimicrobial peptide CRAMP
-
-
?
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 creatin kinase + H2O
?
-
proteolytic cleavage site DIYK*KLRDK
-
-
?
human plasminogen + H2O
?
-
proteolytic cleavage site CPGR*VVGGC, activation
-
-
?
L-Ala-L-Arg-L-Arg-L-Ala + H2O
L-Ala-L-Arg + L-Arg-L-Ala
-
model peptide substrate
-
-
?
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
-
-
?
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 hormone + H2O
?
-
proteolytic cleavage sites EWLR*KKLQD and WLRK*KLQDV
-
-
?
Parathyroid hormone13-34 + H2O
?
-
human, cleaved at both Arg25-Lys26 and Lys26-Lys27
-
-
?
plasminogen + H2O
?
-
poor substrate
no formation of plasmin light chain
-
?
plasminogen + H2O
heavy and light chain of plasmin + ?
-
cleavage at an Arg-Val bond
-
?
plasminogen activator inhibitor-1 + H2O
?
inactivation
-
-
?
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 creatine kinase + H2O
?
-
proteolytic cleavage sites DLYK*KLRDK and RGER*RAVEK
-
-
?
Recombinant human gamma-interferon + H2O
?
-
cleavage between basic amino acids
-
-
?
small-molecular-weight chromogenic peptides + H2O
?
-
OmpT, proteolytic cleavage
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
Escherichia coli EPEC / E2348/69
-
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
Escherichia coli EPEC / E2348/69
-
FRET-substrate, derived from the protein C2 of the classical complement pathway. Poor substrate
-
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
Abz-SLGR + KIQIK(Dnp)-NH2
-
-
-
-
?
alpha2-antiplasmin + H2O
?
inactivation
-
-
?
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
-
?
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
?
C18G + H2O
?
-
synthetic alpha-helical peptide, whose sequence has been optimized for maximal antibacterial activity
-
-
?
C18G + H2O
?
-
synthetic alpha-helical peptide, whose sequence has been optimized for maximal antibacterial activity
-
-
?
C18G + H2O
?
Escherichia coli EPEC / E2348/69
-
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
-
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
-
-
-
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
-
proteolytic degradation
-
-
?
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
-
-
?
dynorphin A + H2O
?
-
proteolytic cleavage, commercial peptide substrate
-
-
?
dynorphin A + H2O
?
cleavage assay of OmpT protease performed with
-
-
?
factor B + H2O
?
-
PgtE generates B fragments of approximately 57 kDa and 28 kDa under non-reducing conditions, while under reducing conditions, the cleavage pattern is different lacking the 28 kDa fragment. PgtE cleaves H near both termini. Mapping of cleavage sites in factor H, overview
-
-
?
factor B + H2O
?
-
PgtE generates B fragments of approximately 57 kDa and 28 kDa under non-reducing conditions, while under reducing conditions, the cleavage pattern is different lacking the 28 kDa fragment. PgtE cleaves H near both termini. Mapping of cleavage sites in factor H, overview
-
-
?
factor H + H2O
?
-
factor H is cleaved at both N- and C-termini, while the central region resists proteolysis
-
-
?
factor H + H2O
?
-
factor H is cleaved at both N- and C-termini, while the central region resists proteolysis
-
-
?
Gelatin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
?
human antiprotease alpha2-antiplasmin + H2O
?
-
involved in infection and pathogenesis
-
-
?
human antiprotease alpha2-antiplasmin + H2O
?
-
inactivation of the substrate by proteolytic cleavage
-
-
?
human circulating complement proteins + H2O
?
-
activation of the substrate
-
-
?
human circulating complement proteins + H2O
?
-
activation of the substrate by proteolytic cleavage
-
-
?
human proenzyme plasminogen + H2O
?
-
low activity of OmpT in activation of the substrate, proteolytic cleavage
-
-
?
human proenzyme plasminogen + H2O
?
-
activation of the substrate by proteolytic cleavage
-
-
?
human proenzyme plasminogen + H2O
?
-
activation of the substrate by proteolytic cleavage
-
-
?
human proenzyme plasminogen + H2O
?
-
involved in pathogenic tissue invasion or nutrition
-
-
?
human single-chain urokinase + H2O
?
-
-
cleavage at the peptide bond Lys158-Ile159, the site cleaved also by the physiological activator human plasmin
-
?
human single-chain urokinase + H2O
?
-
-
cleavage at the peptide bond Lys158-Ile159, the site cleaved also by the physiological activator human plasmin
-
?
human single-chain urokinase + H2O
?
-
-
cleavage at the peptide bond Lys158-Ile159, the site cleaved also by the physiological activator human plasmin
-
?
human single-chain urokinase + H2O
?
-
cleavage at the peptide bond Lys158-Ile159, the site cleaved also by the physiological activator human plasmin. Enzyme addtionally displays activity of EC 3.4.23.48
-
?
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
-
-
?
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
-
-
?
LL-37 + H2O
?
-
human antimicrobial peptide of the cathelicidin family, cleavage occurs at dibasic sites
-
-
?
LL-37 + H2O
?
-
human antimicrobial peptide of the cathelicidin family, cleavage occurs at dibasic sites
-
-
?
LL-37 + H2O
?
Escherichia coli EPEC / E2348/69
-
human antimicrobial peptide of the cathelicidin family, cleavage occurs at dibasic sites
-
-
?
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
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP, rapid, almost complete degradation
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium ATCC 51459
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium ATCC 51459
-
CRAMP, rapid, almost complete degradation
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium DBS 100
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium DBS 100
-
CRAMP, rapid, almost complete degradation
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
CRAMP
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin. PgtE addresses the control systems rather than direct plasminogen activation
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin. PgtE addresses the control systems rather than direct plasminogen activation
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin. PgtE addresses the control systems rather than direct plasminogen activation
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin
-
-
?
T7 RNA polymerase + H2O
?
-
cleavage at Lys-Arg173, Lys-Lys180, and Arg-Lys392
-
-
?
T7 RNA polymerase + H2O
?
-
proteolytic cleavage sites QLNK*RVGHV, HVYK*KAFMQ, and DRAR*KSRRI
-
-
?
TAFI + H2O
TAFIa + ?
TAFI is secreted into plasma as a procarboxypeptidase, it is a regulatory protein linking the coagulation and fibrinolytic systems, and TAFI is protective in septic yersionosis. PptE cleaves at the C-terminal region of TAFI and reduces its activation to TAFIa
-
-
?
TAFI + H2O
TAFIa + ?
cleaves at the C-terminal region of TAFI
-
-
?
tissue factor pathway inhibitor + H2O
?
-
-
-
?
tissue factor pathway inhibitor + H2O
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme PgtE cleaves the tissue factor pathway inhibitor, TFPI
-
-
?
tissue factor pathway inhibitor + H2O
?
-
-
-
?
tissue factor pathway inhibitor + H2O
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme PgtE cleaves the tissue factor pathway inhibitor, TFPI
-
-
?
tissue factor pathway inhibitor + H2O
?
-
-
-
?
tissue factor pathway inhibitor + H2O
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme PgtE cleaves the tissue factor pathway inhibitor, TFPI
-
-
?
WLAAKKGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAAKKGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAARRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAARRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAARRGRG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAARRGRG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAASRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAASRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLARRRGAG + H2O
?
different cleavage sites between OmpP and OmpT protease determined
-
-
?
WLARRRGAG + H2O
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different cleavage sites between OmpT and OmpP protease determined
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WLATRRGAG + H2O
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differences in substrate specificity between OmpP and OmpT proteases determined
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WLATRRGAG + H2O
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differences in substrate specificity between OmpT and OmpP proteases determined
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WLRARRGAG + H2O
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differences in substrate specificity between OmpP and OmpT proteases determined
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WLRARRGAG + H2O
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differences in substrate specificity between OmpT and OmpP proteases determined
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WLSARRGAG + H2O
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differences in substrate specificity between OmpP and OmpT proteases determined
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WLSARRGAG + H2O
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differences in substrate specificity between OmpT and OmpP proteases determined
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WLSERRGAG + H2O
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differences in substrate specificity between OmpP and OmpT proteases determined
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WLSERRGAG + H2O
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differences in substrate specificity between OmpT and OmpP proteases determined
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ZF-RNase-3 + H2O
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when ZF-RNase-3 is added to Escherichia coli cultures, it is cleaved at a specific Arg-Arg peptide bond, thus engendering two peptide fragments. The larger fragment (residues 31-124), produced by proteolysis and reduction of a disulfide, is recognized as the actual bactericidal agent
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ZF-RNase-3 + H2O
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when ZF-RNase-3 is added to Escherichia coli cultures, it is cleaved at a specific Arg-Arg peptide bond, thus engendering two peptide fragments. The larger fragment (residues 31-124), produced by proteolysis and reduction of a disulfide, is recognized as the actual bactericidal agent
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additional information
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Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. 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. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs)
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additional information
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purified enzyme CroP readily cleaves both a synthetic fluorescence resonance energy transfer substrate and the murine cathelicidin-related antimicrobial peptide, while it poorly activates plasminogen into active plasmin
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additional information
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Citrobacter rodentium ATCC 51459
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Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. 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. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs)
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?
additional information
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Citrobacter rodentium DBS 100
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Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. 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. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs)
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?
additional information
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the multifunctional enzyme has virulence-associated functions
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additional information
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minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme
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additional information
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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
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additional information
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t-butyloxycarbonyl-Leu-Gly-Arg 4-methylcoumarin 7-amide
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additional information
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endopeptidase specifically recognizing and cleaving consecutive basic residues
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additional information
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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
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additional information
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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
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?
additional information
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activity under extreme denaturing condition
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additional information
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cleaves peptides between two consecutive basic amino acids
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additional information
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cleaves peptides between two consecutive basic amino acids
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additional information
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cleaves peptides between two consecutive basic amino acids
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?
additional information
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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
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?
additional information
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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
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?
additional information
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the multifunctional enzyme has a virulence-associated function in protein degradation
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?
additional information
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protein-lipid interactions on model membranes and human mononuclear cells, overview
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?
additional information
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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
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?
additional information
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OmpT shown to be one of the critical outer membrane protein responsible for chloramphenicol resistance, analysis by comparative proteomics and mutant investigation
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?
additional information
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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
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?
additional information
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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
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?
additional information
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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
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?
additional information
?
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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
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?
additional information
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Escherichia coli EDL933
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
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?
additional information
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enzyme displays restriction of catalysis at the S1 subsite, with a preference for lysine, arginine, leucine, tyrosine, and phenylalanine residues. No hydrolysis of the substrate peptide is observed with amino acids A, D, E, H, I, M, N, P, Q, S, T, V, or W in the S1 position. At S2 and S1' subsites, the enzyme exhibits a good acceptance of amino acids L, M, E, D, R and S, Y, Q, respectively
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?
additional information
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the enzyme is important in the intracellular phases of salmonellosis, the multifunctional enzyme has virulence-associated functions
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?
additional information
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minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme
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?
additional information
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substrate specificity of PgtE, determination of cleavage sites and sequences, overview
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additional information
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PgtE cleaves both B and H, whereas its close homologue Pla of Yersinia pestis (EC 3.4.23.48) cleaves only H
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additional information
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PgtE cleaves both B and H, whereas its close homologue Pla of Yersinia pestis (EC 3.4.23.48) cleaves only H
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?
additional information
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the enzyme is important in the intracellular phases of shigellosis, the multifunctional enzyme has virulence-associated functions
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?
additional information
?
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minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme
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?
additional information
?
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substrate specificity, the multifunctional enzyme has virulence-associated functions for invasion of human epithelial cells, its binding to laminin localizes the uncontrolled plasmin activity onto basement membranes, the enzyme is involved in spread of the bacterium through tissue barriers due to its adhesive function
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additional information
?
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no proteolytic cleavage of laminin or of small-molecular-weight chromogenic peptides, minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme
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?
