Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity.

@article{Moskovitz2000IdentificationAC,
  title={Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity.},
  author={Jackob Moskovitz and Jacqueline Poston and Barbara S. Berlett and N J Nosworthy and Roman H. Szczepanowski and Earl R. Stadtman},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 19},
  pages={14167-72}
}
Peptide methionine sulfoxide reductases (MsrA) from many different organisms share a consensus amino acid sequence (GCFWG) that could play an important role in their active site. Site-directed single substitution of each of these amino acids except glycines in the yeast MsrA resulted in total loss of enzyme activity. Nevertheless, all the recombinant MsrA mutants and native proteins had a very similar circular dichroism spectrum. The demonstration that either treatment with iodoacetamide or… CONTINUE READING

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