title: Biophysical and folding parameters of trypanothione reductase from Leishmania infantum.
abstract: Out of various tropical diseases caused by trypanosomatids, leishmaniasis is a life-threatening disease caused by the leishmania parasite. We are targeting the thiol metabolic pathway of the parasite for drug development, and trypanothione reductase (TryR) is a key enzyme of this pathway. It is important to gather significant knowledge about biophysical and intrinsic properties of this enzyme which will be helpful in better understanding of this drug-target enzyme. We report here the modulation of activity and stability of TryR from Leishmania infantum in the presence of various denaturants and pHs. The enzyme is quite stable under high concentration of denaturants and showed better stability compared to TryR of Leishmania donovani, whose sequence differs at only on position (Ala363→Gly). Structural basis of the destabilizing effects is discussed.
authors: Department of Biotechnology, Indian Institute of Technology Guwahati, Guwahati, 781039, Assam, India.
authors: Anil Kumar
authors: AK
authors: Shukla
authors: Sanjukta
authors: S
authors: Patra
authors: Vikash Kumar
authors: VK
authors: Dubey
mesh_terms: D004795:Enzyme Stability / Q000235:genetics / Q000502:physiology; D018314:Leishmania infantum / Q000201:enzymology*; D009247:NADH, NADPH Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D009247:NADH, NADPH Oxidoreductases; C049608:trypanothione reductase