L-methionine (S)-S-oxide reductase

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In enzymology, a L-methionine (S)-S-oxide reductase (EC 1.8.4.13) is an enzyme that catalyzes the chemical reaction

L-methionine + thioredoxin disulfide + H₂O $\rightleftharpoons$ L-methionine (S)-S-oxide + thioredoxin

The 3 substrates of this enzyme are L-methionine, thioredoxin disulfide, and H₂O, whereas its two products are L-methionine (S)-S-oxide and thioredoxin.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is L-methionine:thioredoxin-disulfide S-oxidoreductase. Other names in common use include fSMsr, methyl sulfoxide reductase I and II, acetylmethionine sulfoxide reductase, methionine sulfoxide reductase, L-methionine:oxidized-thioredoxin S-oxidoreductase, methionine-S-oxide reductase, and free-methionine (S)-S-oxide reductase. This enzyme participates in methionine metabolism.

[edit] References

IUBMB entry for 1.8.4.13
BRENDA references for 1.8.4.13 (Recommended.)
PubMed references for 1.8.4.13
PubMed Central references for 1.8.4.13
Google Scholar references for 1.8.4.13
Black S, Harte EM, Hudson B and Wartofsky L (1960). "A specific enzymatic reduction of L-(-)methionine sulfoxide and a related nonspecific reduction of diulfides". J. Biol. Chem. 235: 2910–2916.
Ejiri SI, Weissbach H, Brot N (1979). "Reduction of methionine sulfoxide to methionine by Escherichia coli". J. Bacteriol. 139: 161–4. PMID 37234.
Ejiri SI, Weissbach H, Brot N (1980). "The purification of methionine sulfoxide reductase from Escherichia coli". Anal. Biochem. 102: 393–8. doi:10.1016/0003-2697(80)90173-6. PMID 6999943.
Weissbach H, Resnick L, Brot N (2005). "Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage". Biochim. Biophys. Acta. 1703: 203–12. PMID 15680228.