Entamoeba histolytica: biochemical characterization of a protein disulfide isomerase |
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Authors: | Ramos Marco A Mares Rosa E Magaña Paloma D Rivas Israel D Meléndez-López Samuel G |
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Institution: | Facultad de Ciencias Químicas e Ingeniería, Universidad Autónoma de Baja California, Calzada Tecnológico 14418, Tijuana, Baja California 22390, Mexico |
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Abstract: | Protein disulfide isomerase (PDI) enzymes are eukaryotic oxidoreductases that catalyze oxidation, reduction and isomerization of disulfide bonds in polypeptide substrates. Here, we report the biochemical characterization of a PDI enzyme from the protozoan parasite Entamoeba histolytica (EhPDI). Our results show that EhPDI behaves mainly as an oxidase/isomerase and can be inhibited by bacitracin, a known PDI inhibitor; moreover, it exhibits chaperone-like activity. Albeit its physiological role in the life style of the parasite (including virulence and survival) remains to be studied, EhPDI could represent a potential drug target for anti-amebic therapy. |
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Keywords: | Abbreviations: Eh Entamoeba histolytica ER endoplasmic reticulum PDI protein disulfide isomerase LZM lysozyme |
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