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
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3.4.23.49
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furin
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usp7
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ubiquitin-specific
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endoproteolytic
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convertase
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proproteins
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deubiquitinating
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prohormone
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subtilisin-like
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dibasic
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yersinia
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pestis
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deubiquitinase
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trans-golgi
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propeptide
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farnesylated
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subtilisins
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plague
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kex2-like
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lys-arg
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proinsulins
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prelamin
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proregions
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furin-like
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flexneri
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monobasic
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deubiquitylation
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exoprotease
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zmpste24
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isoprenylated
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arg-arg
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pharmacology
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food industry
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biotechnology
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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
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Natural Substrates Products
Natural Substrates Products on EC 3.4.23.49 - omptin
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REACTION DIAGRAM
alpha2-antiplasmin + H2O
?
inactivation
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-
?
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
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-
?
colicin E1 + H2O
?
function in degradation of colicin at the cell surface to protect sensitive cells from infection by colicins suggested
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-
?
gelatine + H2O
?
degradation
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-
?
human antiprotease alpha2-antiplasmin + H2O
?
-
involved in infection and pathogenesis
-
-
?
human circulating complement proteins + H2O
?
-
activation of the substrate
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-
?
human plasminogen + H2O
?
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proteolytic cleavage site CPGR*VVGGC, activation
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-
?
LL37 + H2O
?
a human antimicrobial peptide of the cathelicidin family
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-
?
plasminogen activator inhibitor-1 + H2O
?
inactivation
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-
?
small-molecular-weight chromogenic peptides + H2O
?
-
OmpT, proteolytic cleavage
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-
?
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
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-
?
?
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OmpT, proteolytic degradation
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-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
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-
-
-
?
factor H + H2O
?
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factor H is cleaved at both N- and C-termini, while the central region resists proteolysis
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-
?
factor H + H2O
?
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factor H is cleaved at both N- and C-termini, while the central region resists proteolysis
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-
?
?
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low activity of OmpT in activation of the substrate, proteolytic cleavage
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-
?
human proenzyme plasminogen + H2O
?
-
activation of the substrate by proteolytic cleavage
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-
?
human proenzyme plasminogen + H2O
?
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involved in pathogenic tissue invasion or nutrition
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-
?
?
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CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium ATCC 51459
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CRAMP
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-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium DBS 100
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CRAMP
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-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
CRAMP
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-
?
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
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-
?
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
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-
?
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
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-
?
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme PgtE cleaves the tissue factor pathway inhibitor, TFPI
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-
?
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
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-
?
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
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-
?
?
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-
the multifunctional enzyme has virulence-associated functions
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-
?
additional information
?
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-
activity under extreme denaturing condition
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-
?
additional information
?
-
-
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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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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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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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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-
?