Binding of peroxiredoxin 6 to substrate determines differential phospholipid hydroperoxide peroxidase and phospholipase A(2) activities.

@article{Manevich2009BindingOP,
  title={Binding of peroxiredoxin 6 to substrate determines differential phospholipid hydroperoxide peroxidase and phospholipase A(2) activities.},
  author={Yefim Manevich and Tea Shuvaeva and Chandra Dodia and Altaf S. Kazi and Sheldon I. Feinstein and Aron B. Fisher},
  journal={Archives of biochemistry and biophysics},
  year={2009},
  volume={485 2},
  pages={139-49}
}
Peroxiredoxin 6 (Prdx6) differs from other mammalian peroxiredoxins both in its ability to reduce phospholipid hydroperoxides at neutral pH and in having phospholipase A(2) (PLA(2)) activity that is maximal at acidic pH. We previously showed an active site C47 for peroxidase activity and a catalytic triad S32-H26-D140 necessary for binding of phospholipid and PLA(2) activity. This study evaluated binding of reduced and oxidized phospholipid hydroperoxide to Prdx6 at cytosolic pH. Incubation of… CONTINUE READING
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