CATH Classification

Domain Context

CATH Clusters

Superfamily Peptide methionine sulphoxide reductase MsrA
Functional Family Peptide methionine sulfoxide reductase MsrA

Enzyme Information
Peptide-methionine (S)-S-oxide reductase.
based on mapping to UniProt P54149
(1) Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (S)-S-oxide + thioredoxin. (2) L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S- oxide + thioredoxin.
-!- The reaction occurs in the reverse direction to that shown above. -!- 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. -!- On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly. -!- 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. -!- The reaction proceeds via a sulfenic-acid intermediate. -!- Formerly EC

UniProtKB Entries (1)

Bos taurus
Mitochondrial peptide methionine sulfoxide reductase

PDB Structure

External Links
Organism Escherichia
Primary Citation
Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme.
Lowther, W.T., Brot, N., Weissbach, H., Matthews, B.W.