| Official Name |
|---|
| Peptide-methionine (R)-S-oxide reductase.
|
| Alternative Name(s) |
|---|
| Methionine S-oxide reductase. |
| Methionine S-oxide reductase (R-form oxidizing). |
| Methionine sulfoxide reductase. |
| Methionine sulfoxide reductase B. |
| Selenoprotein R. |
| Reaction catalysed |
|---|
| Peptide-L-methionine + thioredoxin disulfide + H(2)O <=> peptide-L-methionine (R)-S-oxide + thioredoxin |
| Cofactor(s) |
|---|
| Selenium; Zinc.
|
| Comment(s) |
|---|
- The reaction occurs in the reverse direction to that shown above.
- Exhibits high specificity for reduction of the R-form of methionine
S-oxide, with higher activity being observed with L-methionine
S-oxide than with D-methionine S-oxide.
- While both free and protein-bound methionine (R)-S-oxide act as
substrates, the activity with the peptide-bound form is far greater.
- 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.
- For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but
thionein works well.
|
| Cross-references |
|---|
| BRENDA | 1.8.4.12 |
| PUMA2 | 1.8.4.12 |
| PRIAM enzyme-specific profiles | 1.8.4.12 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.8.4.12 |
| IUBMB Enzyme Nomenclature | 1.8.4.12 |
| IntEnz | 1.8.4.12 |
| MEDLINE | Find literature relating to 1.8.4.12 |
| MetaCyc | 1.8.4.12 |
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