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Literature summary for 2.7.9.3 extracted from
- Characterization of potential selenium-binding proteins in the selenophosphate synthetase system (2005), Proc. Natl. Acad. Sci. USA, 102, 1012-1016.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| selenium-binding protein | 3-mercaptopyruvate sulfurtransferase and GAPDH have more suitable potentials as a physiological selenium-delivery protein than rhodanese. In the presence of a selenium-binding protein, a low level of selenodiglutathione formed from SeO32- and glutathione could effectively replace the high concentrations of selenide routinely used as substrate in the selenophosphate synthetase in vitro assays | Haemophilus influenzae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haemophilus influenzae | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| selenophosphate synthetase | - |
Haemophilus influenzae |
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