Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function.

@article{Lin2007FreeMR,
  title={Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function.},
  author={Zhidong Lin and Lynnette C. Johnson and Herbert Weissbach and Nathan Brot and Mark O. Lively and W Todd Lowther},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 23},
  pages={
          9597-602
        }
}
The reduction of methionine sulfoxide (MetO) is mediated by methionine sulfoxide reductases (Msr). The MsrA and MsrB families can reduce free MetO and MetO within a peptide or protein context. This process is stereospecific with the S- and R-forms of MetO repaired by MsrA and MsrB, respectively. Cell extracts from an MsrA(-)B(-) knockout of Escherichia coli have several remaining Msr activities. This study has identified an enzyme specific for the free form of Met-(R)-O, fRMsr, through… CONTINUE READING

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