Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei.

@article{Budde2003KineticsAR,
  title={Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei.},
  author={Heike Budde and Leopold Floh{\'e} and H. Hecht and Birgit Hofmann and Matthias Stehr and Josef Wissing and Heinrich Luensdorf},
  journal={Biological chemistry},
  year={2003},
  volume={384 4},
  pages={619-33}
}
Tryparedoxin peroxidases (TXNPx) are peroxiredoxin-type enzymes that detoxify hydroperoxides in trypanosomatids. Reduction equivalents are provided by trypanothione [T(SH)2] via tryparedoxin (TXN). The T(SH)2-dependent peroxidase system was reconstituted from TXNPx and TXN of T. brucei brucei (TbTXN-Px and TbTXN). TbTXNPx efficiently reduces organic hydroperoxides and is specifically reduced by TbTXN, less efficiently by thioredoxin, but not by glutathione (GSH) or T(SH)2. The kinetic pattern… CONTINUE READING
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