EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.8.4.11 | C86S/C206S | KM and kcat value are 19fold higher and 40fold slower compared to wild type, respectively. The Cys198-Cys206 disulfide bond is rather reduced by thioredoxin under steady-state conditions instead of the Cys51-Cys198 disulfide bond | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.8.4.11 | 0.19 | - |
thioredoxin | mutant C86S/C206S, pH 8.0, 25°C | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.4.11 | Escherichia coli | P0A744 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.4.11 | acetyl-L-methionine-(S)-S-oxide-NHMe + thioredoxin | - |
Escherichia coli | acetyl-L-methionine-NHMe + thioredoxin disulfide + H2O | - |
? | |
1.8.4.11 | additional information | enzyme catalyzes two reductase steps. In the presence of thioredoxin, the overall rate-limiting step is associated with the thioredoxin-recycling process, and MsrA accumulates under Cys51 sulfenic acid state. Formation of the second mol of Ac-L-Met-NHMe is rate-limiting in the absence of thioredoxin | Escherichia coli | ? | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.8.4.11 | 0.088 | - |
thioredoxin | mutant C86S/C206S, pH 8.0, 25°C | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.8.4.11 | thioredoxin | - |
Escherichia coli |