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Literature summary extracted from

  • Franco, E.; de Araujo Soares, R.M.; Meza, I.
    Specific and reversible inhibition of Entamoeba histolytica cysteine-proteinase activities by Zn2+: implications for adhesion and cell damage (1999), Arch. Med. Res., 30, 82-88.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.35 Zn2+ 77% inhibition of proteolytic activity at 2.5 mM, completely reversible by L-cystein, phenanthroline, and L-histidine, Zn2+ interferes with the fibronectin binding of the amoeba Entamoeba histolytica

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.22.35 protein + H2O Entamoeba histolytica
-
 peptides
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.35 Entamoeba histolytica
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.22.35 trophozoite
-
 Entamoeba histolytica
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.35 azocasein + H2O
-
 Entamoeba histolytica fragments of azocasein
-
 ?
3.4.22.35 Gelatin + H2O
-
 Entamoeba histolytica ?
-
 ?
3.4.22.35 additional information enzyme permits adhesion of trophozoites to cells via fibronectin binding, which can be inhibited by Zn2+ Entamoeba histolytica ?
-
 ?
3.4.22.35 protein + H2O
-
 Entamoeba histolytica peptides
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.22.35 Entamoeba histolytica cysteine-proteinase
-
 Entamoeba histolytica