3.4.24.49: bothropasin
This is an abbreviated version!
For detailed information about bothropasin, go to the full flat file.
Word Map on EC 3.4.24.49
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3.4.24.49
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hemorrhagic
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metalloproteinases
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svmps
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envenom
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snakebite
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disintegrins
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disintegrin-like
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jararhagin
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antivenoms
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atrox
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viperid
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asper
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fibrinogenolytic
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trimeresurus
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agkistrodon
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flavoviridis
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echis
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atrolysin
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protobothrops
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pitviper
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reprolysins
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ammodytes
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adamalysins
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medicine
- 3.4.24.49
-
hemorrhagic
- metalloproteinases
-
svmps
-
envenom
-
snakebite
-
disintegrins
-
disintegrin-like
- jararhagin
- antivenoms
- atrox
-
viperid
- asper
-
fibrinogenolytic
- trimeresurus
-
agkistrodon
- flavoviridis
- echis
- atrolysin
- protobothrops
-
pitviper
-
reprolysins
- ammodytes
- adamalysins
- medicine
Reaction
Cleavage of His5-/-Leu, His10-/-Leu, Ala14-/-Leu, Tyr16-/-Leu and Phe24-/-Phe in insulin B chain =
Synonyms
Bothrops jararaca snake venom metalloproteinase, HF3, Proteinase, Bothrops jararaca venom metallo-, snake venom metalloproteinase, SVMP
ECTree
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General Information
General Information on EC 3.4.24.49 - bothropasin
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physiological function
additional information
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role of the non-catalytic domains of snake venom metalloproteinases, interaction of four snake venom metalloproteinases of different domain compositions and glycosylation levels, from Bothrops jararaca venom, with plasma and extracellular matrix proteins, overview
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haemorrhagic effect of bothropasin on mouse skin, overview
physiological function
in the enzyme-treated mouse skin there is evidence of degradation of extracellular matrix (collagens and proteoglycans), cytosolic, cytoskeleton, and plasma protein as well as activation of collagenase
physiological function
beyond to the degradation of human proteins, bothropasin can generate bioactive peptides, which may participate in the envenoming process by Bothrops snakes