Methionine sulfoxide reductase in antioxidant defense

doi:10.1016/S0076-6879(99)00130-5

Methods in Enzymology

Volume 300, 1999, Pages 239-244

https://doi.org/10.1016/S0076-6879(99)00130-5 Get rights and content

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Cells contain methionine sulfoxide reductases (MsrA) that catalyze the thioredoxin-dependent reduction of methionine sulfoxide [Met(O)] back to methionine (Met). The oxidation of methionine residues of some proteins may lead either to activation or to inactivation of their biological activities, whereas the oxidation of one or more methionine residues in other proteins may have-tittle or no effect on biological function. This has led to the suggestion that MsrA may have multiple biological functions: (1) it may serve to repair oxidative protein damage of some proteins, (2) it may play an important role in the regulation of enzyme activities by facilitating the interconversion of specific methionine residues of these proteins between oxidized and reduced forms, and (3) MsrA might also serve as an antioxidant enzyme to protect some enzymes from oxidative damage by various reactive oxygen species (ROS). The ability of MsrA to repair oxidative damage in vivo may be of singular importance if methionine residues serve as antioxidants. The chapter describes the expression and purification of recombinant eukaryotic MsrA.

References (16)

W. Vogt
Free Radical Biol. Med.
(1995)
N. Brot et al.
Arch. Biochem. Biophys.
(1983)
N. Brot et al.
Methods in Enzymology
(1984)
N. Brot et al.
Anal. Biochem.
(1982)
V.Y. Reddy et al.
J. Biol. Chem.
(1994)
R.L. Levine et al.
T.M. Wizemann et al.
M.W. Swaim et al.
J. Leukocyte Biol.
(1988)

There are more references available in the full text version of this article.

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Methionine sulfoxide reductase in antioxidant defense

Publisher Summary

Free Radical Biol. Med.

Arch. Biochem. Biophys.

Methods in Enzymology

Anal. Biochem.

J. Biol. Chem.

J. Leukocyte Biol.