Peptide methionine sulfoxide reductase: biochemistry and physiological role
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Updated: Oct 8, 2026

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
1Hospital for Special Surgery, Weill Medical College of Cornell University New York, NY 10021, USA.
Abstract:
The oxidation of methionine to methionine sulfoxide both in vivo and in vitro can lead to the loss of biological activity in a variety of proteins. This loss of activity can be reversed by an enzyme called methionine sulfoxide reductase. The gene for this enzyme has been cloned and sequenced from a variety of prokaryotic and eukaryotic cells, and the deduced amino acid sequence is very highly conserved. The mechanism of action of the bovine enzyme has been shown to involve a critical cysteine residue located at position 72 of the protein. In addition to its role as a "repair" enzyme, other evidence suggests that the enzyme may be involved in bacterial adherence and regulation of protein activity.
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