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 | Peptide methionine sulfoxide reductase MsrB |
Enzyme Information
1.8.4.12 |
Peptide-methionine (R)-S-oxide reductase.
based on mapping to UniProt O26807
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.
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UniProtKB Entries (1)
O26807 |
MSRB_METTH
Methanothermobacter thermautotrophicus str. Delta H
Peptide methionine sulfoxide reductase MsrB
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PDB Structure
PDB | 2K8D |
External Links | |
Method | SOLUTION NMR |
Organism | |
Primary Citation |
Structure-function relationship in an archaebacterial methionine sulphoxide reductase B.
Mol.Microbiol.
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