Excretion of glutathione by methylglyoxal-resistant Escherichia coli.
A methylglyoxal-resistant mutant of Escherichia coli B excreted glutathione into the growth medium, especially during growth on medium containing methylglyoxal. In the presence of methylglyoxal, the total amount of glutathione excreted was increased about 50-fold over that of the wild-type strain. The resistant mutant had high activities of two enzyme systems: a glutathione-forming enzyme system (consisting of gamma-glutamylcysteine synthetase and glutathione synthetase) and a glyoxalase system (consisting of glyoxalase I and glyoxalase II). Methylglyoxal resistance appeared to be due to the simultaneous increase in the activities of these two enzyme systems.
D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D005978:Glutathione / Q000096:biosynthesis*; D007791:Lactoylglutathione Lyase / Q000378:metabolism; D008190:Lyases / Q000378:metabolism; D009154:Mutation; D010453:Peptide Synthases / Q000378:metabolism; D011765:Pyruvaldehyde / Q000494:pharmacology
D011765:Pyruvaldehyde; D008190:Lyases; D007791:Lactoylglutathione Lyase; D010453:Peptide Synthases; D005978:Glutathione