Active site mutagenesis and phospholipid hydroperoxide reductase activity of poplar type II peroxiredoxin.

@article{Rouhier2004ActiveSM,
  title={Active site mutagenesis and phospholipid hydroperoxide reductase activity of poplar type II peroxiredoxin.},
  author={Nicolas Rouhier and Eric Gelhaye and Catherine Corbier and Jean Pierre Jacquot},
  journal={Physiologia plantarum},
  year={2004},
  volume={120 1},
  pages={
          57-62
        }
}
The nature of the active site and the substrate specificity of poplar type II peroxiredoxin, an enzyme which preferentially uses glutaredoxin as an electron donor, were investigated in this study. The type II peroxiredoxin is able to use phospholipid hydroperoxide nearly as efficiently as hydrogen peroxide. Two of the hyper-conserved amino acid residues in peroxiredoxins have been altered, by site-directed mutagenesis, generating the mutants T48V and R129Q. The two mutant proteins are inactive… CONTINUE READING
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