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Literature summary extracted from

  • Ogasawara, Y.; Lacourciere, G.M.; Ishii, K.; Stadtman, T.C.
    Characterization of potential selenium-binding proteins in the selenophosphate synthetase system (2005), Proc. Natl. Acad. Sci. USA, 102, 1012-1016.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.9.3 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

EC Number Organism UniProt Comment Textmining
2.7.9.3 Haemophilus influenzae
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-
-

Synonyms

EC Number Synonyms Comment Organism
2.7.9.3 selenophosphate synthetase
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 Haemophilus influenzae