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Literature summary for 3.4.22.35 extracted from

  • Scholze, H.; Schulte, W.
    On the specificity of a cysteine proteinase from Entamoeba histolytica (1988), Biomed. Biochim. Acta, 47, 115-123.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Natural and synthetic inhibitors of cysteine proteinases
-
Entamoeba histolytica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27000
-
1 * 27000, Entamoeba histolytica, SDS-PAGE Entamoeba histolytica

Organism

Organism UniProt Comment Textmining
Entamoeba histolytica
-
virulent strain HMI:IMSS
-

Purification (Commentary)

Purification (Comment) Organism
-
Entamoeba histolytica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Collagen type I + H2O digestion with an initial attack at the alpha2-chain Entamoeba histolytica ?
-
?
additional information with unblocked tetrapeptides as substrates, peptidyl dipeptidase activity of the amoeba enzyme requires an arginine at the P2 position. Lysine cannot substitute for arginine Entamoeba histolytica ?
-
?
additional information splits blocked and unblocked peptide analogs with 2-naphthylamide moieties, cleavability is enhanced by the presence of basic residues, such as arginine or lysine, near the acyl end of the substrate Entamoeba histolytica ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 27000, Entamoeba histolytica, SDS-PAGE Entamoeba histolytica