Sohini Gupta1, Sabuj Saha2, Paushali Roy3, Protip Basu4, Sayak Ganguli5*
1Cell Biology, Molecular Biology, Genetics and Plant Biotechnology Laboratory, Post Graduate Department of Botany, Barasat Government College, Kolkata.
2Cell Biology, Molecular Biology, Genetics and Plant Biotechnology Laboratory, Post Graduate Department of Botany, Barasat Government College, Kolkata.
3DBT-Centre for Bioinformatics, Presidency College, Kolkata
4DBT-Centre for Bioinformatics, Presidency College, Kolkata
5DBT-Centre for Bioinformatics, Presidency College, Kolkata
* Corresponding Author : sayakbif@yahoo.com
Received : - Accepted : - Published : 15-06-2010
Volume : 2 Issue : 1 Pages : 20 - 30
Int J Bioinformatics Res 2.1 (2010):20-30
DOI : http://dx.doi.org/10.9735/0975-3087.2.1.20-30
Keywords : Ricinus communis L. Delaunay triangulation, glutathione peroxidase, oxidative stress, accessible
surface area, pocket identification
Conflict of Interest : None declared
Oxidative stress in plants causes the induction of several enzymes, including superoxide dismutase (EC 1.15.1.1), ascorbate peroxidase (EC 1.11.1.11) and glutathione reductase (EC 1.6.4.2). The first two are responsible for converting superoxide to H2O2 and its subsequent reduction to H2O, and the third is involved in recycling of ascorbate. Glutathione peroxidases (GPXs, EC 1.11.1.9) are a family of key enzymes involved in scavenging oxyradicals in animals. Only recently, indications for the existence of this enzyme in plants were reported. Genes with significant sequence homology to one member of the animal GPX family, namely phospholipid hydroperoxide glutathione peroxidase (PHGPX), were isolated from several plants. In this paper we report the homology modelling of the glutathione peroxidase protein from Ricinus communis L. and its interactions with its two substrates hydrogen peroxide and glutathione. Specific sites of interaction were identified and ligand binding pockets were also screened.
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