Oxidoreductases;
Acting on a sulfur group of donors;
With a disulfide as acceptor
BRITE hierarchy

peptide-L-methionine:thioredoxin-disulfide S-oxidoreductase [L-methionine (S)-S-oxide-forming]

(1) peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin [RN:R04120];
(2) L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin [RN:R07606]

R04120 R07606
Reaction

peptide-L-methionine [CPD:C03023];
thioredoxin disulfide [CPD:C00343];
H2O [CPD:C00001];
L-methionine [CPD:C00073]

The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid [9]. On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly [9]. The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.12, peptide-methionine (R)-S-oxide reductase, are found within the same protein whereas, in other species, they are separate proteins [1,4]. The reaction proceeds via a sulfenic-acid intermediate [5,10].

EC 1.8.4.11 created 2006