CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.1060 | Peptide Methionine Sulfoxide Reductase; Chain A |
|
3.30.1060.10 | Peptide methionine sulphoxide reductase MsrA |
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
J.Biol.Chem.
|
