CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

1.8.4.11
Peptide-methionine (S)-S-oxide reductase.
based on mapping to UniProt P40029
(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 1.8.4.6.

UniProtKB Entries (1)

P40029
MSRA_YEAST
Saccharomyces cerevisiae S288C
Peptide methionine sulfoxide reductase

PDB Structure

PDB 3PIL
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural plasticity of the thioredoxin recognition site of yeast methionine S-sulfoxide reductase Mxr1
Ma, X.X., Guo, P.C., Shi, W.W., Luo, M., Tan, X.F., Chen, Y., Zhou, C.Z.
J.Biol.Chem.