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- W2964132024 abstract "Leishmania is an intracellular parasite responsible for the group of Leishmaniasis diseases. The quest for a therapy has led many researchers to believe that the trypanothione-mediated hydroperoxide metabolism is the Achilles heel for these trypanosomatids, since they are exposed to ROS (Reactive Oxygen Species) both endogenously and exogenously and possess very limited systems to cope up with this oxidative stress. This pathway comprises of a cascade of three oxidoreductases acting in sync to transfer reducing equivalents from NADPH to the hydroperoxides; the terminal being Tryparedoxin Peroxidase which was first elucidated in the insect-infecting pathogen, Crithidia fasciculata by Nogoceke et al in 1997. Screening of a partial genomic library with a 270 bp fragment obtained from the PCR on L. donovani genomic DNA with primers designed from highly conserved regions of peroxiredoxins gave a sequence that showed high homology to known peroxidases of peroxiredoxin type. The protein was expressed and kinetics were studied. Therefore, this work clearly shows the presence of Tryparedoxin Peroxidase in the deadly human pathogen, Leishmania donovani. Also the study of the active site residues would enable the design of rational drug inhibitors. To this end, ten mutants were designed based on multiple sequence alignments and some intelligent derivations. The mutants indicated that in this enzyme the catalytic triad comprises of three residues- wherein the N-terminal cysteine is activated by hydrogen bonding with the -OH group of a threonine and forced into dissociation by the guanidino group of arginine." @default.
- W2964132024 created "2019-07-30" @default.
- W2964132024 creator A5057877759 @default.
- W2964132024 date "2004-05-24" @default.
- W2964132024 modified "2023-09-24" @default.
- W2964132024 title "Leishmania donovani Tryparedoxin Peroxidase" @default.
- W2964132024 doi "https://doi.org/10.24355/dbbs.084-200511080100-420" @default.
- W2964132024 hasPublicationYear "2004" @default.
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