3.4.24.73: jararhagin
This is an abbreviated version!
For detailed information about jararhagin, go to the full flat file.
Word Map on EC 3.4.24.73
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3.4.24.73
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bothrops
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jararaca
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metalloproteinases
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disintegrin-like
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svmps
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cysteine-rich
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envenom
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disintegrins
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viper
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collagen-induced
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alpha2beta1
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snakebite
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antivenoms
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marsupialis
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atrolysin
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trigramin
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atrox
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reprolysin
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didelphis
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hemorrhagins
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medicine
- 3.4.24.73
- bothrops
- jararaca
- metalloproteinases
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disintegrin-like
-
svmps
-
cysteine-rich
-
envenom
-
disintegrins
- viper
-
collagen-induced
- alpha2beta1
-
snakebite
- antivenoms
- marsupialis
- atrolysin
-
trigramin
- atrox
-
reprolysin
-
didelphis
-
hemorrhagins
- medicine
Reaction
Hydrolysis of -His10-/-Leu-, -Ala14-/-Leu-, -Tyr16-/-Leu-and -Phe24-/-Phe- bonds in insulin B chain =
Synonyms
haemolytic factor-2, hemorrhagic svMP, HF2, HF2-proteinase, Jar, Jar-C, jararafibrase 1, jararhagin, jararhagin-c, JF1, JG, More, PIII snake venom metalloprotease, PIII snake venom metalloproteinase, PIII SVMP, rCDJARA, snake venom metalloproteinase, snake venom metalloproteinase-disintegrin, soluble haemorrhagic snake venom metalloproteinase, SVMP
ECTree
3.4.24.73 jararhaginAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.73 - jararhagin
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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
alpha2 subunit I domain of the platelet surface alpha2beta1 integrin + H2O
?
-
-
-
-
?
alpha2-Plasmin inhibitor + H2O
Inactivated alpha2-plasmin inhibitor
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-
-
?
FVNQHLCGSHLVEALYVCGERGFFYTPKA + H2O
FVNQHLCGSH + Lys-Val-Glu-Ala + Lys + YVCGERGF + FYTPKA
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-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
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cleavage at 4 peptide bonds
-
?
collagen XII + H2O
?
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bovine substrate, the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains, cleavage pattern, overview
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-
?
collagen XII + H2O
?
-
the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis
-
-
?
collagen XIV + H2O
?
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bovine substrate, a fibril-associated collagen with interrupted triple helices, the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains, cleavage pattern, overview
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-
?
collagen XIV + H2O
?
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the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis
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-
?
matrilin 1 + H2O
?
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bovine substrate, the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains
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-
?
matrilin 1 + H2O
?
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the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis
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-
?
matrilin 3 + H2O
?
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the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis
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-
?
matrilin 3 + H2O
?
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the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains, cleavage pattern, overview
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-
?
matrilin 4 + H2O
?
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the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis
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-
?
matrilin 4 + H2O
?
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the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains
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-
?
Type I collagen + H2O
?
bovine and chicken substrates, the enzyme binds with high affinity to the intact triple helix collagen structure affecting the collagen suprastructure
-
-
?
von Willebrand factor + H2O
?
-
binding between jararhagin cysteine-rich domain and Von Willebrand factor A1 domain leads to inhibition of Von Willebrand factor platelet aggregation activity, overview
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-
?
von Willebrand factor + H2O
?
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Von Willebrand factor A1 domain interacts with the enzyme's cysteine-rich domain, which promotes site-specific proteolysis, jararhagin cleaves the substrate at sites adjacent to the A1 domain
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-
?
von Willebrand factor + H2O
?
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mapping of Von Willebrand factor A domain binding sites on the enzyme's cysteine-rich domain, binding between jararhagin cysteine-rich domain and Von Willebrand factor A1 domain, protein-protein interactions, molecular modeling, overview
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-
?
von Willebrand factor + H2O
?
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Von Willebrand factor A1 domain interacts with the enzyme's cysteine-rich domain, which promotes site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains
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-
?
additional information
?
-
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possesses proteolytic and hemorrhagic activity
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?
additional information
?
-
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possesses proteolytic and hemorrhagic activity
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?
additional information
?
-
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possesses proteolytic and hemorrhagic activity
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?
additional information
?
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possesses proteolytic and hemorrhagic activity
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-
?
additional information
?
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in vitro induces strongly fibrinolytic activity in plasma of guinea pig, horse, dog, rabbit and human (not in plasma of rat, mouse, hamster, goat, sheep, pig or bovine), it increases tissue-type plasminogen activator activity by dissociation of a complex of this activator with type 1 plasminogen activator inhibitor and inactivation of alpha2-plasmin inhibitor
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?
additional information
?
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main hemorrhagic metalloproteinase in Bothrops jararaca venom
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?
additional information
?
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jararhagin blocks type I collagen-induced platelet aggregation by binding to the alpha2beta1 integrin and inhibiting collagen-mediated intracellular signaling events, in contrast to observation in platelets enzyme binding to the integrin receptor alpha2beta1 in fibroblasts produces collagen-like cell signaling events such as up-regulation of matrix metalloproteinase-1 and membrane-type matrix metalloproteinase-1, in fibroblasts enzyme functions as a collagen-mimetic substrate that binds to and activates integrins
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?
additional information
?
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low doses of the toxin jararhagin induce interstitial edema and increase the metabolic rate and red blood cells in Swiss mice, histology of lungs and kidney, overview, at high doses it causes hemorrhage, inflammation, necrosis and edema
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?
additional information
?
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the enzyme is a hemorrhagic P-III snake venom metalloproteinase
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?
additional information
?
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the enzyme is a hemorrhagic P-III snake venom metalloproteinase, collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases, the multidomain enzyme binds to collagen via disintegrin-like and cysteine-rich domains allocate motifs that enable catalytic degradation of extracellular matrix components leading to disruption of capillary vessels
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?
additional information
?
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the enzyme is a P-III snake venom metalloproteinase and a potent hemorrhagin
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?
additional information
?
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the enzyme is a P-III snake venom metalloproteinase and a potent hemorrhagin, it causes capillary vessel basement membrane damage in vitro and in vivo, degradation of extracellular matrix components in skeletal muscle cells and endothelial cells, overview
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?
additional information
?
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the enzyme is a P-III snake venom metalloproteinase and a potent hemorrhagin, it induces strong pro-inflammatory response increasing the number of rolling leukocytes within capillary vessels, jararhagin induces apoptosis and release of angiostatin-like peptides in human endothelial cells, overview
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?
additional information
?
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the enzyme inhibits collagen-induced platelet aggregation with an IC50 value of 300 nM
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?
additional information
?
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the enzyme's disintegrin-like/cysteine-rich domains target it to to key extracellular matrix proteins or cell surface proteins, overview
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?
additional information
?
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the snake venom hemorrhagic metalloproteinase causes capillary vessel basement membrane damage in vitro and in vivo, overview
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?
additional information
?
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jararhagin toxin binding to collagen appears to be sufficient to inhibit collagen-induced platelet aggregation in the human host
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?
additional information
?
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different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to alpha2beta1 integrin, a collagen receptor, and collagen from host K-562 cells, analysis using monoclonal antibodies and recombinant jararhagin fragments, jararhagin binding to collagen and alpha2beta1 integrin occurs by two independent motifs located on disintegrin-like and cysteine-rich domains, respectively, detailed overview
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?
