Any feedback?
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. |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
