CATH Classification

Domain Context

CATH Clusters

Superfamily Glutaredoxin
Functional Family Multifunctional fusion protein

Enzyme Information

1.8.4.12
Peptide-methionine (R)-S-oxide reductase.
based on mapping to UniProt P14930
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.
1.8.4.11
Peptide-methionine (S)-S-oxide reductase.
based on mapping to UniProt P14930
(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)

P14930
MSRAB_NEIGO
Neisseria gonorrhoeae
Peptide methionine sulfoxide reductase MsrA/MsrB

PDB Structure

PDB 2H30
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The Thioredoxin Domain of Neisseria gonorrhoeae PilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases.
Brot, N., Collet, J.F., Johnson, L.C., Jonsson, T.J., Weissbach, H., Lowther, W.T.
J.Biol.Chem.