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 Q92Y45
(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)

Q92Y45
MSRA3_RHIME
Sinorhizobium meliloti 1021
Peptide methionine sulfoxide reductase MsrA 3

PDB Structure

PDB 4GWB
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of putative Peptide methionine sulfoxide reductase from Sinorhizobium meliloti 1021
Malashkevich, V.N., Bhosle, R., Toro, R., Hillerich, B., Gizzi, A., Garforth, S., Kar, A., Chan, M.K., Lafluer, J., Patel, H., Matikainen, B., Chamala, S., Lim, S., Celikgil, A., Villegas, G., Evans, B., Zenchek, W., Love, J., Fiser, A., Khafizov, K., Seidel, R., Bonanno, J.B., Almo, S.C.
To be Published