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Literature summary for 1.8.4.12 extracted from
- An anaerobic bacterial MsrB model reveals catalytic mechanisms, advantages, and disadvantages provided by selenocysteine and cysteine in reduction of methionine-R-sulfoxide (2008), Arch. Biochem. Biophys., 478, 175-180.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the wild-type and mutant forms of MsrB in Escherichia coli | Clostridium sp. |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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. |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium sp. | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Clostridium sp. |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MsrB | - |
Clostridium sp. |
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