CATH Classification

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.

UniProtKB Entries (1)

O26807
MSRB_METTH
Methanothermobacter thermautotrophicus str. Delta H
Peptide methionine sulfoxide reductase MsrB

PDB Structure

PDB 2K8D
External Links
Method SOLUTION NMR
Organism
Primary Citation
Structure-function relationship in an archaebacterial methionine sulphoxide reductase B.
Carella, M., Becher, J., Ohlenschlager, O., Ramachandran, R., Guhrs, K.H., Wellenreuther, G., Meyer-Klaucke, W., Heinemann, S.H., Gorlach, M.
Mol.Microbiol.
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