Leakage of glutathione from bacterial cells caused by inhibition of gamma-glutamyltranspeptidase.
Glutathione leaked from cells of Proteus mirabilis grown in medium containing an inhibitor of gamma-glutamyltranspeptidase. In medium containing 100 mM L-serine and borate, up to 300 microM glutathione accumulated. L-Serine in the medium was consumed during the logarithmic phase of growth, gamma-glutamyltranspeptidase activity was restored, and glutathione decreased in the medium. In the presence of 2 mM 6-diazo-5-oxo-L-norleucine, cells increased normally, gamma-glutamyltranspeptidase was inhibited completely, and the maximum concentration of glutathione which accumulated in the medium was 20 microM. The glutathione content of cells rose before leakage began. Glutathione leaked from intact cells of other bacteria, although to a lesser extent than was seen with P. mirabilis.
D018407:Bacterial Physiological Phenomena; D005978:Glutathione / Q000378:metabolism / Q000502:physiology*; D007700:Kinetics; D011513:Proteus mirabilis / Q000201:enzymology / Q000502:physiology*; D013045:Species Specificity; D005723:gamma-Glutamyltransferase / Q000037:antagonists & inhibitors*
D005723:gamma-Glutamyltransferase; D005978:Glutathione