1.8.4.12: peptide-methionine (R)-S-oxide reductase

This is an abbreviated version!
For detailed information about peptide-methionine (R)-S-oxide reductase, go to the full flat file.

Word Map on EC 1.8.4.12

Reaction

L-methionine (R)-sulfoxide
+
thioredoxin
=
L-methionine
+
thioredoxin disulfide
+
H2O

Synonyms

1-Cys methionine sulfoxide reductase B, 1-Cys MSRB, CBS-1, CBS1, cysteine-containing methionine-R-sulfoxide reductase, LOC100305558, LOC100798757, methionine sulfoxide reductase, methionine sulfoxide reductase B, methionine sulfoxide reductase B1, methionine sulfoxide reductase B2, methionine sulfoxide reductase B3, methionine sulfoxide reductase MsrB3, methionine sulfoxide reductases B, methionine sulfoxide reductases B2, methionine sulphoxide reductase, methionine-R-sulfoxide reductase, methionine-R-sulfoxide reductase B, methionine-R-sulfoxide reductase B2, More, MSR, MsrA/B, MsrA/MsrB, msrAB, MsrABTk, MsrB, MSRB1, MsrB2, MsrB3, MsrB3A, MSRB4, MsrB5, MsrB7, MsrB8, MsrBA, Mxr2, NtMsrB2, peptide methionine sulfoxide reductase, peptide methionine sulfoxide reductase type B, PilB, PilB protein, PMSR, Sel-X, selenocysteine-containing methionine-R-sulfoxide reductase, selenoprotein R, SelR, sulindac reductase, YeaA

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.4 With a disulfide as acceptor
                1.8.4.12 peptide-methionine (R)-S-oxide reductase

Systematic Name

Systematic Name on EC 1.8.4.12 - peptide-methionine (R)-S-oxide reductase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
SYSTEMATIC NAME
IUBMB Comments
peptide-methionine:thioredoxin-disulfide S-oxidoreductase [methionine (R)-S-oxide-forming]
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide [9]. While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater [10]. 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 1.8.4.11, peptide-methionine (S)-S-oxide reductase, are found within the same protein whereas in other species, they are separate proteins [3,5]. The reaction proceeds via a sulfenic-acid intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well [11]. The enzyme from some species contains selenocysteine and Zn2+.