Cloning and characterization of antioxidant enzyme methionine sulfoxide-S-reductase from Caenorhabditis elegans

Byung Cheon Lee, Yong Kwon Lee, Hojoung Lee, Earl R. Stadtman, Kweon Haeng Lee, Namhyun Chung

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Methionine (Met) residues in proteins are susceptible to oxidation. The resulting methionine sulfoxide can be reduced back to methionine by methionine sulfoxide-S-reductase (MsrA). The MsrA gene, isolated from Caenorhabditis elegans, was cloned and expressed in Escherichia coli. The resultant enzyme was able to revert both free Met and Met in proteins in the presence of either NADPH or dithiothreitol (DTT). However, approximately seven times higher enzyme activity was observed in the presence of DTT than of NADPH. The enzyme had an absolute specificity for the reduction of l-methionine-S-sulfoxide but no specificity for the R isomer. K m and k cat values for the enzyme were ∼1.18 mM and 3.64 min -1, respectively. Other kinetics properties of the enzyme were also evaluated.

Original languageEnglish
Pages (from-to)275-281
Number of pages7
JournalArchives of Biochemistry and Biophysics
Issue number2
Publication statusPublished - 2005 Feb 15



  • Caenorhabditis elegans
  • Catalytic efficiency
  • Methionine sulfoxide
  • Methionine-S-sulfoxide reductase
  • MsrA

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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