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Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

Enzymes and Genes:
methionine sulfoxide reductase AInferred from experiment: msrA

Supersedes EC number:

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: peptide-methionine (S)-S-oxide reductase

Enzyme Commission Synonyms: MsrA, methionine sulfoxide reductase (ambiguous), methionine sulphoxide reductase A, methionine S-oxide reductase (ambiguous), methionine S-oxide reductase (S-form oxidizing), methionine sulfoxide reductase A, peptide methionine sulfoxide reductase

Enzyme Commission Summary:
The reaction occurs in the reverse direction to that shown above. Exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid. On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly. Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. The reaction proceeds via a sulfenic-acid intermediate. Formerly EC

Citations: [Brot81, Olry02, Vougier03, Kauffmann05, Ezraty05, Weissbach05, BoschiMuller05, Singh03, Taylor03, Moskovitz02]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


BoschiMuller05: Boschi-Muller S, Olry A, Antoine M, Branlant G (2005). "The enzymology and biochemistry of methionine sulfoxide reductases." Biochim Biophys Acta 1703(2);231-8. PMID: 15680231

Brot81: Brot N, Weissbach L, Werth J, Weissbach H (1981). "Enzymatic reduction of protein-bound methionine sulfoxide." Proc Natl Acad Sci U S A 78(4);2155-8. PMID: 7017726

Ezraty05: Ezraty B, Aussel L, Barras F (2005). "Methionine sulfoxide reductases in prokaryotes." Biochim Biophys Acta 1703(2);221-9. PMID: 15680230

Kauffmann05: Kauffmann B, Aubry A, Favier F (2005). "The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions." Biochim Biophys Acta 1703(2);249-60. PMID: 15680233

Moskovitz02: Moskovitz J, Singh VK, Requena J, Wilkinson BJ, Jayaswal RK, Stadtman ER (2002). "Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity." Biochem Biophys Res Commun 290(1);62-5. PMID: 11779133

Olry02: Olry A, Boschi-Muller S, Marraud M, Sanglier-Cianferani S, Van Dorsselear A, Branlant G (2002). "Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis." J Biol Chem 277(14);12016-22. PMID: 11812798

Singh03: Singh VK, Moskovitz J (2003). "Multiple methionine sulfoxide reductase genes in Staphylococcus aureus: expression of activity and roles in tolerance of oxidative stress." Microbiology 149(Pt 10);2739-47. PMID: 14523107

Taylor03: Taylor AB, Benglis DM, Dhandayuthapani S, Hart PJ (2003). "Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine." J Bacteriol 185(14);4119-26. PMID: 12837786

Vougier03: Vougier S, Mary J, Friguet B (2003). "Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells." Biochem J 373(Pt 2);531-7. PMID: 12693988

Weissbach05: Weissbach H, Resnick L, Brot N (2005). "Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage." Biochim Biophys Acta 1703(2);203-12. PMID: 15680228

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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