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Peptide-methionine (R)-S-oxide reductase

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Peptide-methionine (R)-S-oxide reductase
Identifiers
EC no.1.8.4.12
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BRENDABRENDA entry
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In enzymology, a peptide-methionine (R)-S-oxide reductase (EC 1.8.4.12) is an enzyme that catalyzes the chemical reaction

peptide-L-methionine + thioredoxin disulfide + H2O {\displaystyle \rightleftharpoons } peptide-L-methionine (R)-S-oxide + thioredoxin

The 3 substrates of this enzyme are peptide-L-methionine, thioredoxin disulfide, and H2O, whereas its two products are peptide-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 peptide-methionine:thioredoxin-disulfide S-oxidoreductase . Other names in common use include MsrB, methionine sulfoxide reductase (ambiguous), pMSR, methionine S-oxide reductase (ambiguous), selenoprotein R, methionine S-oxide reductase (R-form oxidizing), methionine sulfoxide reductase B, SelR, SelX, PilB, and pRMsr.

References

Oxidoreductases: sulfur oxidoreductases (EC 1.8)
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
Enzymes
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Regulation
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