3.4.24.B34: Vipera ammodytes ammodytes metalloproteinase VaF1
This is an abbreviated version!
For detailed information about Vipera ammodytes ammodytes metalloproteinase VaF1, go to the full flat file.
Reaction
Cleavage of the Lys413-/-Leu414 bond of alpha-chain of human fibrinogen. Cleavage of Ala14-/-Leu15 and Tyr16-/-Leu17 in insulin B chain. Non-hemorrhagic proteinase =
Synonyms
VaF1
ECTree
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Substrates Products
Substrates Products on EC 3.4.24.B34 - Vipera ammodytes ammodytes metalloproteinase VaF1
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REACTION DIAGRAM
bovine factor X + H2O
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slow degradation. The heavy chain offactor X is more susceptible to hydrolysis by the enzyme than the light chain whose hydrolysis is observed only after prolonged incubation
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bovine plasminogen + H2O
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slow degradation. Very limited proteolysis, giving rise to multiple products with molecular masses between 40 and 60 kDa
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bovine prothrombin + H2O
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slow degradation. Two major cleavage products, of 60 and 28 kDa, accumulate after extended incubation. N-terminal sequencing shows them to be prethrombin-1 and fragment 1, indicating the cleavage of prothrombin at the Ser157-/-Gly158 bond
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human fibrinogen alpha-chain + H2O
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cleavage of the Lys413-/-Leu414 bond of alpha-chain of fibrinogen. Fibrinogen beta- and gamma-chains remain intact even after 3 h incubation
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insulin B chain + H2O
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cleavage of two peptide bonds is detected, Ala14-/-Leu15 and Tyr16-/-Leu17
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Nidogen + H2O
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hydrolysis at the Ser322-/-Phe323 bond
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hydrolysis of fibrinogen, factor X, prothrombin and plasminogen, plasma proteins involved in blood coagulation
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additional information
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non-hemorrhagic proteinase. No degradation of fibrin. Laminin resists hydrolysis by the enzyme, even after 24 h incubation
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