Plasmodium and host glutathione reductase: molecular function and biological process

Abstract

Glutathione (GSH) is a cysteine-containing tripeptide with reducing and nucleophilic properties which play an important role in cellular protection from oxidative damage of lipids, proteins and nucleic acids. Glutathione reductase (GR) is an NADPH-dependent enzyme that reduces oxidized glutathione (GSSG) to GSH. Naturally, GR is present in human and in Plasmodium spp. However, the function of the GR in malarial infection is not well characterized. Here, the author used a new gene ontology technology to predict the molecular function and biological process. Using GoFigure server, the molecular function and biological process in human and P. falciparum GR is predicted. Comparing to the human GR, the P. falciparum GR has similar molecular functions as gluthathione disulfide reductase activity, oxidoreductase activity, disulfide oxidoreductase activity and metal ion binding.