| L-methionine (S)-S-oxide reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.4.13 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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 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.
References
- Black S, Harte EM, Hudson B, 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 (1): 161–4. PMC 216841. PMID 37234.
- Ejiri SI, Weissbach H, Brot N (1980). "The purification of methionine sulfoxide reductase from Escherichia coli". Anal. Biochem. 102 (2): 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 (2): 203–12. doi:10.1016/j.bbapap.2004.10.004. PMID 15680228.