3.4.24.B38: ammodytagin
This is an abbreviated version!
For detailed information about ammodytagin, go to the full flat file.
Reaction
The enzyme hydrolyzes bovine insulin B-chain at positions Gln4-/-His5, His10-/-Leu11 and Tyr16-/-Leu17. The enzyme possesses potent azocaseinolytic activity. =
ECTree
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Substrates Products
Substrates Products on EC 3.4.24.B38 - ammodytagin
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REACTION DIAGRAM
bovine factor X + H2O
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cleavage occurs at position Gln49-/-Cys50 in the light chain and at position Asp173-/-Leu174 in the heavy chain
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bovine oxidized insulin B-chain + H2O
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the enzyme hydrolyzes at positions Gln4His5, His10Leu11 and Tyr16Leu17. No other peptide bond hydrolysis is detected after 30 min of incubation
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-
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human fibrinogen alpha-chain + H2O
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hydrolysis at multiple positions, including Ser220-/-Gln221, Lys413-/-Leu414, Glu422-/-Leu423 and Glu520-/-Phe521. Hydrolysis at lower rate (after 6 h) is detected at sites Asn109-/-Arg110, Arg23-/-Met240 and Arg491-/-His492
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-
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human fibrinogen beta-chain + H2O
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the fibrinogen beta-chain is cleaved much slower than the alpha-chain
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-
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Nidogen + H2O
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in Matrigel Growth Factor Reduced, nidogen is cleaved at positions Val422-/-Phe423 and Tyr352-/-Asn353
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the enzyme acts as a strong hemorrhagin in both rats and mice. Laminin is not cleaved even after 24 h treatment with ammodytagin. No cleavage of the human fibrinogen gamma-chain
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additional information
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the enzyme acts as a strong hemorrhagin in both rats and mice. Laminin is not cleaved even after 24 h treatment with ammodytagin. No cleavage of the human fibrinogen gamma-chain
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