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Literature summary extracted from

  • Silva, C.C.F.; Menezes, M.C.; Palomino, M.; Oliveira, A.K.; Iwai, L.K.; Faria, M.; Portaro, F.V.
    Peptides derived from plasma proteins released by bothropasin, ametalloprotease present in the Bothrops jararaca venom (2017), Toxicon, 137, 65-72 .
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.49 Zn2+ zinc-dependent enzyme Bothrops jararaca

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.49 Bothrops jararaca O93523
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-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.49 venom
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 Bothrops jararaca
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.49 Fibrinogen + H2O 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 Bothrops jararaca ?
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 ?
3.4.24.49 Fibronectin + H2O 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 Bothrops jararaca ?
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 ?

General Information

EC Number General Information Comment Organism
3.4.24.49 physiological function beyond to the degradation of human proteins, bothropasin can generate bioactive peptides, which may participate in the envenoming process by Bothrops snakes Bothrops jararaca