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.
Copyright © 2011 Elsevier Inc. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Bacterial Agents / pharmacology
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Bacitracin / pharmacology
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Entamoeba histolytica / drug effects
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Entamoeba histolytica / enzymology*
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Hydrogen-Ion Concentration
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Inhibitory Concentration 50
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Insulin / metabolism
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Molecular Chaperones / metabolism
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Muramidase / chemistry
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Muramidase / metabolism
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Oxidoreductases / metabolism
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Protein Disulfide-Isomerases / antagonists & inhibitors
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Protein Disulfide-Isomerases / chemistry
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Protein Disulfide-Isomerases / metabolism*
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Protein Folding
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Ribonuclease, Pancreatic / chemistry
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Ribonuclease, Pancreatic / metabolism
Substances
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Anti-Bacterial Agents
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Insulin
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Molecular Chaperones
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Bacitracin
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Oxidoreductases
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Ribonuclease, Pancreatic
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Muramidase
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Protein Disulfide-Isomerases