In silico studies on tryparedoxin peroxidase of Leishmania infantum: structural aspects.
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.
Singh
Bishal Kumar
BK
Department of Biotechnology, Indian Institute of Technology Guwahati-781039, Assam, India.
Dubey
Vikash Kumar
VK
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*
D015800:Protozoan Proteins; D010544:Peroxidases; C110959:tryparedoxin peroxidase