Glutathione reductase (GR) expression and glutathione content were examined under oxidative stress conditions from the gram-positive clostridiale Enterococcus faecalis. The enzyme is found ubiquitously in gram-negative bacteria, and has been implicated in the defense against the oxidative burst response of the eukaryotic host immune system. We have purified to homogeneity the first GR from a gram-positive organism and demonstrated an increased expression of GR under hyperbaric oxygen conditions without a significant change in the total glutathione content. The kinetic parameters deduced for the E. faecalis GR are similar to those found for GR from yeast, E. col[, and human erythrocyte. The difference in the expression of the enzyme and substrate content suggest that the genes encoding the glutathione synthesizing enzymes are not linked to the oxygen-sensitive promoter of the glutathione reductase gene. Fur thermore, a critical examination of the kinetic parameters provides a plausible explanation for the distinction in the levels of expression of the substrate and.
|Original language||English (US)|
|Publication status||Published - Dec 1 1997|
ASJC Scopus subject areas
- Molecular Biology