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CATH Classification

Domain Context

CATH Clusters

Superfamily Glutaredoxin
Functional Family

Enzyme Information

1.8.4.11
Peptide-methionine (S)-S-oxide reductase.
based on mapping to UniProt Q9JWM8
(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.
1.8.4.12
Peptide-methionine (R)-S-oxide reductase.
based on mapping to UniProt Q9JWM8
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 (2)

Q9JWM8
MSRAB_NEIMA
Neisseria meningitidis Z2491
Peptide methionine sulfoxide reductase MsrA/MsrB
Q9JYM0
DSBD_NEIMB
Neisseria meningitidis MC58
Thiol:disulfide interchange protein DsbD

PDB Structure

PDB 2K9F
External Links
Method SOLUTION NMR
Organism
Primary Citation
Formation of the complex between DsbD and PilB N-terminal domains from Neisseria meningitidis necessitates an adaptability of nDsbD.
Quinternet, M., Tsan, P., Selme-Roussel, L., Jacob, C., Boschi-Muller, S., Branlant, G., Cung, M.T.
Structure
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