CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.170 | Beta Complex |
|
2.170.150 | Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A |
|
2.170.150.20 | Peptide methionine sulfoxide reductase. |
Domain Context
CATH Clusters
| Superfamily | Peptide methionine sulfoxide reductase. |
| Functional Family | methionine-R-sulfoxide reductase B1 |
Enzyme Information
| 1.8.4.12 |
Peptide-methionine (R)-S-oxide reductase.
based on mapping to UniProt Q9NZV6
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (R)-S-oxide + thioredoxin.
-!- 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.
|
| 1.8.4.14 |
L-methionine (R)-S-oxide reductase.
based on mapping to UniProt Q9NZV6
L-methionine + thioredoxin disulfide + H(2)O = L-methionine (R)-S-oxide + thioredoxin.
-!- Unlike EC 1.8.4.12 this enzyme cannot use peptide-bound methionine (R)-S-oxide as a substrate. -!- Differs from EC 1.8.4.13, in that L-methionine (S)-S-oxide is not a substrate. -!- Formerly EC 1.8.4.5.
|
UniProtKB Entries (1)
| Q9NZV6 |
MSRB1_HUMAN
Homo sapiens
Methionine-R-sulfoxide reductase B1
|
PDB Structure
| PDB | 3MAO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal Structure of Human Methionine-R-Sulfoxide Reductase B1 (MsrB1)
To be Published
|