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
Current Pharmaceutical Biotechnology
Title: In Silico Studies on Tryparedoxin Peroxidase of Leishmania infantum: Structural Aspects
Volume: 10 Issue: 6
Author(s): Bishal Kumar Singh and Vikash Kumar Dubey
Affiliation:
Keywords: Drug design, Structure-Function, Peroxidase activity, Homology Modelling
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.
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Cite this article as:
Singh Kumar Bishal and Dubey Kumar Vikash, In Silico Studies on Tryparedoxin Peroxidase of Leishmania infantum: Structural Aspects, Current Pharmaceutical Biotechnology 2009; 10 (6) . https://dx.doi.org/10.2174/138920109789069305
DOI https://dx.doi.org/10.2174/138920109789069305 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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