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Literature summary extracted from

  • Huson, L.E.; Authie, E.; Boulange, A.F.; Goldring, J.P.; Coetzer, T.H.
    Modulation of the immunogenicity of the Trypanosoma congolense cysteine protease, congopain, through complexation with alpha2-macroglobulin (2009), Vet. Res., 40, 52.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.51 additional information in general immunoglobulin G fractions isolated from rabbits immunised with rabbit apha2-macroglobulin-recombinant catalytic domain of congopain-complexes are the most inhibitory towards the proteolytic activity of congopain. Antibodies produced by rabbits immunised with recombinant catalytic domain of congopain in Freund's adjuvant are generally found to weakly inhibit congopain with a maximum of 40% Trypanosoma congolense

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.51 Trypanosoma congolense
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.22.51
-
 Trypanosoma congolense

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.51 benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
-
 Trypanosoma congolense benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.22.51 congopain
-
 Trypanosoma congolense