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Literature summary for 3.4.22.35 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

Inhibitors Comment Organism Structure
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)

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

Organism

Organism UniProt Comment Textmining
Entamoeba histolytica
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
trophozoite
-
Entamoeba histolytica
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Entamoeba histolytica cysteine-proteinase
-
Entamoeba histolytica