|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 220.127.116.11
Supersedes EC number: 18.104.22.168
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 22.214.171.124.
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
Singh03b: 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
Taylor03a: 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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