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Literature summary for 3.4.21.59 extracted from

  • Coffman, L.G.; Brown, J.C.; Johnson, D.A.; Parthasarathy, N.; DAgostino, R.B.; Lively, M.O.; Hua, X.; Tilley, S.L.; Muller-Esterl, W.; Willingham, M.C.; Torti, F.M.; Torti, S.V.
    Cleavage of high-molecular-weight kininogen by elastase and tryptase is inhibited by ferritin (2008), Am. J. Physiol. Lung Cell Mol. Physiol., 294, L505-L515.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
ferritin ferritin can retard the cleavage of both native oxidized high-molecular-weight kininogen by tryptase, initial rates of cleavage are reduced 45-75% in the presence of ferritin Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
high-molecular-weight kininogen + H2O
-
 Mus musculus ?
-
 ?
additional information ferritin is not a substrate for tryptase Mus musculus ?
-
 ?
N-benzyloxycarbonyl-Gly-Pro-Arg-p-nitroanilide + H2O
-
 Mus musculus ?
-
 ?