KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state and reductase step kinetic parameters of wild-type and mutated MsrAs | Neisseria meningitidis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Neisseria meningitidis | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | Neisseria meningitidis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-L-methionine-(S)-S-oxide-NHMe + thioredoxin | - |
Neisseria meningitidis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
methionine sulfoxide reductase A | - |
Neisseria meningitidis |
MsrA | - |
Neisseria meningitidis |