CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

1.8.4.11
Peptide-methionine (S)-S-oxide reductase.
based on mapping to UniProt P0A744
(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)

P0A744
MSRA_ECOLI
Escherichia coli K-12
Peptide methionine sulfoxide reductase MsrA

PDB Structure

PDB 2GT3
External Links
Method SOLUTION NMR
Organism
Primary Citation
Solution Structure and Backbone Dynamics of the Reduced Form and an Oxidized Form of E. coli Methionine Sulfoxide Reductase A (MsrA): Structural Insight of the MsrA Catalytic Cycle.
Coudevylle, N., Antoine, M., Bouguet-Bonnet, S., Mutzenhardt, P., Boschi-Muller, S., Branlant, G., Cung, M.T.
J.Mol.Biol.