EC Number | Cloned (Comment) | Organism |
---|---|---|
1.8.4.12 | expression of the wild-type and mutant forms of MsrB in Escherichia coli | Clostridium sp. |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.8.4.12 | selenium | the selenocysteine-containing Clostridium MsrB form exhibits 100fold higher activity than its Cys-containing form, revealing that selenocysteine provides the catalytic advantage of higher activity. A resolving Cys is required for the thioredoxin-dependent recycling process of the selenocysteine-containing form. Thus, thioredoxin can reduce the selenylsulfide bond, but its Trx-dependent recycling process is much less efficient compared to that for the disulfide bond in the Cys-containing form, demonstrating an obvious catalytic disadvantage | Clostridium sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.4.12 | Clostridium sp. | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.8.4.12 | - |
Clostridium sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.8.4.12 | MsrB | - |
Clostridium sp. |