L-methionine (R)-S-oxide reductase
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In enzymology, a L-methionine (R)-S-oxide reductase (EC 1.8.4.14) is an enzyme that catalyzes the chemical reaction
- L-methionine + thioredoxin disulfide + H2O L-methionine (R)-S-oxide + thioredoxin
The 3 substrates of this enzyme are L-methionine, thioredoxin disulfide, and H2O, whereas its two products are L-methionine (R)-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 [L-methionine (R)-S-oxide-forming]. Other names in common use include fRMsr, FRMsr, free met-R-(o) reductase, and free-methionine (R)-S-oxide reductase. This enzyme participates in methionine metabolism.
[edit] References
- IUBMB entry for 1.8.4.14
- BRENDA references for 1.8.4.14 (Recommended.)
- PubMed references for 1.8.4.14
- PubMed Central references for 1.8.4.14
- Google Scholar references for 1.8.4.14
- Etienne F, Spector D, Brot N, Weissbach H (2003). "A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide". Biochem. Biophys. Res. Commun. 300: 378–82. doi: . PMID 12504094.