African Journal of Biotechnology Vol. 5 (21), pp. 2009-2013, 2 November 2006   

ISSN 1684–5315 © 2006 Academic Journals        

Full Length Research Paper

Plasmodium and host glutathione reductase: molecular function and biological process

Viroj Wiwanitkit

Department of Laboratory Medicine, Faculty of Medicine, Chulalongkorn University, Bangkok Thailand 10330. E-mail: wviroj@pioneer.netserv.chula.ac.th.

Accepted 15 September, 2006

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.

Key words: Human, Plamodium falciparum, glutathione reductase, function.