From Wikipedia, the free encyclopedia
L-methionine (R)-S-oxide reductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.8.4.14 | ||||||||
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 (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.
References
[edit]- 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 (2): 378–82. doi:10.1016/S0006-291X(02)02870-X. PMID 12504094.
Oxidoreductases: sulfur oxidoreductases (EC 1.8) | |
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1.8.1: NAD or NADP | |
1.8.2: cytochrome | |
1.8.3: oxygen | |
1.8.4: disulfide | |
1.8.5: quinone | |
1.8.98: Other, known | |
1.8.99: Other |
Activity | |
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Regulation | |
Classification | |
Kinetics | |
Types |
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