PMID:12604343

Citation	Spector, D, Etienne, F, Brot, N and Weissbach, H (2003) New membrane-associated and soluble peptide methionine sulfoxide reductases in Escherichia coli. Biochem. Biophys. Res. Commun. 302:284-9
Abstract	It is known that reactive oxygen species can oxidize methionine residues in proteins in a non-stereospecific manner, and cells have mechanisms to reverse this damage. MsrA and MsrB are members of the methionine sulfoxide family of enzymes that specifically reduce the S and R forms, respectively, of methionine sulfoxide in proteins. However, in Escherichia coli the level of MsrB activity is very low which suggested that there may be other enzymes capable of reducing the R epimer of methionine sulfoxide in proteins. Employing a msrA/B double mutant, a new peptide methionine sulfoxide reductase activity has been found associated with membrane vesicles from E. coli. Both the R and S forms of N-acetylmethionine sulfoxide, D-ala-met(o)-enkephalin and methionine sulfoxide, are reduced by this membrane associated activity. The reaction requires NADPH and may explain, in part, how the R form of methionine sulfoxide in proteins is reduced in E. coli. In addition, a new soluble Msr activity was also detected in the soluble extracts of the double mutant that specifically reduces the S epimer of met(o) in proteins.
Links	PubMed
Keywords	Cell Membrane/enzymology; Escherichia coli/enzymology; Methionine Sulfoxide Reductases; Oxidation-Reduction; Oxidoreductases/classification; Oxidoreductases/genetics; Oxidoreductases/metabolism; Peptides/metabolism; Solubility
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