Generic placeholder image

Current Pharmaceutical Biotechnology

Editor-in-Chief

ISSN (Print): 1389-2010
ISSN (Online): 1873-4316

In Silico Studies on Tryparedoxin Peroxidase of Leishmania infantum: Structural Aspects

Author(s): Bishal Kumar Singh and Vikash Kumar Dubey

Volume 10, Issue 6, 2009

Page: [626 - 630] Pages: 5

DOI: 10.2174/138920109789069305

Price: $65

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.

Keywords: Drug design, Structure-Function, Peroxidase activity, Homology Modelling


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy