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

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

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
Volume434
Issue number2
DOIs
Publication statusPublished - 2005 Feb 15

Fingerprint

Cloning
Caenorhabditis elegans
Methionine
Organism Cloning
Oxidoreductases
Antioxidants
Enzymes
sulfoxide
Dithiothreitol
NADP
Enzyme activity
Isomers
Escherichia coli
Proteins
Cats
Genes
methionine sulfoxide
methionine sulfoxide reductase
Oxidation
Kinetics

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Cloning and characterization of antioxidant enzyme methionine sulfoxide-S-reductase from Caenorhabditis elegans. / Lee, Byung Cheon; Lee, Yong Kwon; Lee, Hojoung; Stadtman, Earl R.; Lee, Kweon Haeng; Chung, Namhyun.

In: Archives of Biochemistry and Biophysics, Vol. 434, No. 2, 15.02.2005, p. 275-281.

Research output: Contribution to journalArticle

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