3.4.24.74: fragilysin
This is an abbreviated version!
For detailed information about fragilysin, go to the full flat file.
Word Map on EC 3.4.24.74
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3.4.24.74
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staphylococcal
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aureus
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enterotoxigenic
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heat-labile
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superantigens
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heat-stable
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cholera
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diarrhea
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clostridium
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perfringens
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lymphocyte
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t-cells
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vaccine
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poisoning
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mucosal
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milk
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vibrio
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ifn-gamma
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outbreak
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serotype
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sta
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serogroups
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anergy
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foodborne
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enteropathogenic
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ganglioside
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gm1
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hydrophila
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exotoxin
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methicillin-resistant
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hemolysin
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cytotoxin
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ileal
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toxigenic
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stool
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agglutination
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emetic
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enterocolitica
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shiga
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toxin-producing
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retail
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coagulase
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rotavirus
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b-subunits
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medicine
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methicillin
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holotoxin
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antitoxin
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toxoid
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pyrogen
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anti-cd3
- 3.4.24.74
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staphylococcal
- aureus
- enterotoxigenic
-
heat-labile
-
superantigens
-
heat-stable
- cholera
-
diarrhea
- clostridium
- perfringens
- lymphocyte
- t-cells
- vaccine
- poisoning
- mucosal
- milk
- vibrio
- ifn-gamma
-
outbreak
-
serotype
- sta
-
serogroups
-
anergy
- foodborne
-
enteropathogenic
- ganglioside
- gm1
- hydrophila
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exotoxin
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methicillin-resistant
- hemolysin
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cytotoxin
- ileal
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toxigenic
-
stool
-
agglutination
-
emetic
- enterocolitica
-
shiga
-
toxin-producing
-
retail
- coagulase
- rotavirus
-
b-subunits
- medicine
- methicillin
-
holotoxin
- antitoxin
- toxoid
-
pyrogen
-
anti-cd3
Reaction
Broad proteolytic specificity, bonds hydrolysed including -Gly-/-Leu-, -Met-/-Leu-, -Phe-/-Leu-, -Cys-/-Leu-, Leu-/-Gly =
Synonyms
B. fragilis enterotoxin, Baceroides fragilis enterotoxin, Bacillus fragilis toxin, Bacteroides fragilis enterotoxin, Bacteroides fragilis enterotoxin-2, Bacteroides fragilis toxin, BFT, BFT-1, BFT-2, BFT-3, BFT2, Enterotoxin, FRA3, fragilysin-2, fragilysin-3, Korea-BFT, More, toxin-2
ECTree
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Substrates Products
Substrates Products on EC 3.4.24.74 - fragilysin
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REACTION DIAGRAM
acetyl-Ala-Lys-Lys-Ala-Lys-Leu-Thr-Ala-Leu-Val-NMe + H2O
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Actin + H2O
Fragements of actin
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initial cleavage at Gly-Met, followed by Thr-Leu
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?
Fibrinogen + H2O
Fragements of fibrinogen
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hydrolysis to a lesser degree than other substrates
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?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
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?
Tropomyosin + H2O
Fragements of tropomyosin
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hydrolysis to a lesser degree than other substrates
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E-cadherin + H2O
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cleavage of the zonula adherens protein
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E-cadherin + H2O
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neither human nor rat E-cadherin are the cellular receptor for BFT
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E-cadherin + H2O
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the enzyme hydrolyzes the extracellular domain of several protein substrate, e.g. of E-cadherin to interrupt the intercellular adhesion increasing the permeability of the epithelium, and causing intracellular redistribution of actin with morphologic changes and release of beta-catenin
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E-cadherin + H2O
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the enzyme hydrolyzes the extracellular domain of the substrate
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E-cadherin + H2O
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recombinant fragilysin isoforms cause E-cadherin cleavage of intact cells and do not cleave isolated E-cadherin
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E-cadherin + H2O
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the enzyme cleaves the extracellular domain of E-cadherin. Its cleavage then releases beta-catenin associated with the cytoplasmic domain of E-cadherin
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E-cadherin + H2O
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neither human nor rat E-cadherin are the cellular receptor for BFT
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the enzyme increases the paracellular permeability of the intestinal epithelium by digestion of the intestinal light junctions and cell-to-cell contacts, it does not disrupt cell membranes
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Proteins + H2O
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proteolytic action on the actin of the cytoskeleton
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Proteins + H2O
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active in lamb, rabbit, rat ileum and colon, it causes the production of fluids and hemorrhage, it increases the levels of Na+ and Cl- in intestinal loops due to tissue damage
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cleaves at Cys-Leu, Ser-Leu, Thr-Leu, Gly-Leu or Leu-Gly peptide bonds in a number of proteins
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additional information
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the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
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additional information
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the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
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additional information
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the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
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additional information
?
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the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and seceretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
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additional information
?
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the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
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?
additional information
?
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the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
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-
?
additional information
?
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the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
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additional information
?
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the cytopathic effect of the enzyme is only seen in cells that can form tight junction and polarized monolayers, the enzyme affects the barrier function of the epithelium and decreases the transpithelial electrical resistance of monolayers, overview, the enzyme stimulates the recruitment of polymorphs to the lamina propria and secretion of interleukin-8, epithelial neutrophil-activating peptide-78, and growth-related oncogene-alpha from colonocytes, overview
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additional information
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the enterotoxin has cytotoxic activity, however strains isolated from stool samples of calves with diarrhea contain the gene bft, but do not show cytotoxic activity against HT29 cells, overview
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additional information
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fragilysin is a zinc metalloprotease toxin with a C-terminal zinc-binding protease domain
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additional information
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fragilysin is a zinc metalloprotease toxin with a C-terminal zinc-binding protease domain
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additional information
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fragilysin is a zinc metalloprotease toxin with a C-terminal zinc-binding protease domain
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additional information
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fragilysin is a zinc metalloprotease toxin with a C-terminal zinc-binding protease domain
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additional information
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isozyme fargilysin-3 does not cleave azoalbumin
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additional information
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isozyme fargilysin-3 does not cleave azoalbumin
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additional information
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azocoll, azocasein and gelatin are not proteolytically cleaved by mature fragilysin-2
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additional information
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the recombinant enzyme does not cleave thioredoxin, gelatin, azocoll or azocasein both with and without Zn2+ ions
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additional information
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the recombinant enzyme does not cleave thioredoxin, gelatin, azocoll or azocasein both with and without Zn2+ ions
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additional information
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the enzyme does not demonstrate hemagglutination activity
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