| EC |
1.8.4.14 |
| Accepted name: |
L-methionine (R)-S-oxide reductase |
| Reaction: |
L-methionine + thioredoxin disulfide + H2O = L-methionine (R)-S-oxide + thioredoxin |
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For diagram of reaction, click here and for mechanism of reaction, click here |
| Other name(s): |
fRMsr; FRMsr; free met-R-(o) reductase; free-methionine (R)-S-oxide reductase |
| Systematic name: |
L-methionine:thioredoxin-disulfide S-oxidoreductase [L-methionine (R)-S-oxide-forming] |
| Comments: |
Requires NADPH. Unlike EC 1.8.4.12, peptide-methionine (R)-S-oxide reductase, this enzyme cannot use peptide-bound methionine (R)-S-oxide as a substrate [1]. Differs from EC 1.8.4.13, L-methionine (S)-S-oxide in that L-methionine (S)-S-oxide is not a substrate. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 945954-12-1 |
| References: |
| 1. |
Etienne, F., Spector, D., Brot, N. and Weissbach, H. A methionine sulfoxide reductase in Escherichia coli that reduces the R
enantiomer of methionine sulfoxide. Biochem. Biophys. Res. Commun. 300 (2003) 378–382. [DOI] [PMID: 12504094] |
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| [EC 1.8.4.14 created 1984 as EC 1.8.4.5, part transferred 2006 to EC 1.8.4.14] |
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