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
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hemorrhagic
- metalloproteinases
-
svmps
-
envenom
-
snakebite
-
disintegrins
-
disintegrin-like
- jararhagin
- antivenoms
- atrox
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viperid
- asper
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fibrinogenolytic
- trimeresurus
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agkistrodon
- flavoviridis
- echis
- atrolysin
- protobothrops
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pitviper
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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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Substrates Products on EC 3.4.24.49 - bothropasin
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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
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
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cleavage of His5-Leu, His10-Leu, Ala14-Leu, Tyr16-Leu and Phe24-Phe
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?
Fibrin + H2O
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the enzyme specifically cleaves the alpha-polymer and alpha-chain of the fibrin molecule, in contrast gamma-gamma dimer and beta-chain of the fibrin are found to be resistant to the enzyme
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?
Fibrinogen + H2O
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identification of peptides generated by bothropasin proteolytic activity. Among the fibrinogen derived peptides identified by mass spectrometry, analogous of endogenous products like the fibrinopeptides A and B are found, as well as other sequences described in the literature with vasoactive or antiangiogenic properties
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Fibronectin + H2O
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identification of peptides generated by bothropasin proteolytic activity. For most of the peptides no biological activity is described. Exceptionally a peptide that is known as a bond site for B cells is found
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additional information
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comparison of hemorrhagic, caseinolytic and fibrinogenolytic activities of metalloproteinases HF3, bothropasin, the DC protein and metalloproteinase BJ-PI. Hemorrhagic activity of bothropasin is 0.006 mg to produce a hemorrhagic area of 1 cm2. Fibrinogenolytic activity of bothropasin is 9.8 units/mg
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?
additional information
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comparison of hemorrhagic, caseinolytic and fibrinogenolytic activities of metalloproteinases HF3, bothropasin, the DC protein and metalloproteinase BJ-PI. Hemorrhagic activity of bothropasin is 0.006 mg to produce a hemorrhagic area of 1 cm2. Fibrinogenolytic activity of bothropasin is 9.8 units/mg
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additional information
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bothropasin degradation profiles of fibrinogen, fibronectin, vitronectin, von Willebrand factor, collagens IV and VI, laminin and Matrigel in comparison to the other three snake venom metalloproteinases of Bothrops jararaca, binding to plasma and extracellular matrix proteins, overview. Collagen I is degraded only by bothropasin
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