EC Number   |
Reaction |
Reference |
|---|
  1.8.4.11 | L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O |
reaction mechanism, modeling of substrate binding at the active site, Cys72 is involved |
659992 |
| 1.8.4.11 | L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin |
proposed catalytic mechanism of the reductase step of MsrA |
684715 |
| 1.8.4.11 | peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin |
- |
- |
| 1.8.4.11 | peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin |
catalytic mechanism, Cys72 is essential for activity forming disulfide bonds with either Cys218 or Cys227 |
394100 |
| 1.8.4.11 | peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin |
catalytic mechanism, rate-limiting reduction of the Cys51-Cys198 disulfide bond by thioredoxin and formation of the thiosulfenic acid intermediate on Cys51 |
659275 |
| 1.8.4.11 | peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin |
presence of at least two binding subsites. The first one, whose contribution is major in the efficiency of the reductase step and in which the epsilon-methyl group of MetSO binds, is the hydrophobic pocket formed by Phe52 and Trp53, the position of the indole ring being stabilized by interactions with His186 and Tyr189. The second subsite composed of Asp129 and Tyr197 contributes to the binding of the main chain of the substrate but to a lesser extent |
687569 |
