title: In silico studies on tryparedoxin peroxidase of Leishmania infantum: structural aspects.
abstract: Tryparedoxin peroxidase (TryP) is a key enzyme of the trypanothione-dependent metabolism for removal of oxidative stress in leishmania. These enzymes function as antioxidants through their peroxidase and peroxynitrite reductase activities. Inhibitors of this enzyme are presumed to be antilesihmania drugs and structural studies are prerequisite of rational drug design. We have constructed three dimensional structure of TryP of Leishmania infantum using comparative modeling. Structural analysis reveals several interesting features. Moreover, it shows remarkable structural difference with human host glutathione peroxidase, an enzyme involved in similar function and TryP from Leishmania major.
authors.affiliation: Department of Biotechnology, Indian Institute of Technology Guwahati-781039, Assam, India.
authors.forename: Bishal Kumar
authors.initials: BK
authors.lastname: Singh
authors.forename: Vikash Kumar
authors.initials: VK
authors.lastname: Dubey
mesh_terms: D003198:Computer Simulation; D018314:Leishmania infantum / Q000201:enzymology*; D008956:Models, Chemical; D008958:Models, Molecular; D010544:Peroxidases / Q000737:chemistry* / Q000648:ultrastructure*; D011487:Protein Conformation; D015800:Protozoan Proteins / Q000737:chemistry* / Q000648:ultrastructure*
chemical_list: D015800:Protozoan Proteins; D010544:Peroxidases; C110959:tryparedoxin peroxidase