The glutathione-dependent glyoxalase pathway in the yeast Saccharomyces cerevisiae.
Glyoxalase I (EC 4.4.1.5), which catalyzes the reaction methylglyoxal + GSH leads to S-lactoylglutathione, is a ubiquitous enzyme for which no clear physiological function has been shown. In the yeast Saccharomyces cerevisiae, methylglyoxal may derive from the spontaneous decay of intracellular glyceraldehyde-3-P, which may accumulate during growth on glycerol as the carbon source. The half-life time for the triose phosphate was found to be 4.6 h under physiological conditions (pH 6.2, 0.05 M phosphate at 30 degrees C). Glyoxalase I is induced by growth on glycerol or by the addition of methylglyoxal to the growth medium. The enzyme is also subject to carbon catabolite repression. A mutant strain, fully defective in glyoxalase I and bearing only one nuclear mutation, was obtained. The strain, which is killed by exposure to glycerol, excretes methylglyoxal into the medium. Growth of the mutant on glucose as carbon source appears to be similar to that of the wild type strain. This investigation has clearly demonstrated a physiological role of glyoxalase I in a eucaryotic cell.
D004790:Enzyme Induction; D005978:Glutathione / Q000494:pharmacology*; D005990:Glycerol / Q000494:pharmacology; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D007791:Lactoylglutathione Lyase / Q000502:physiology*; D008190:Lyases / Q000502:physiology*; D009154:Mutation; D010766:Phosphorylation; D011765:Pyruvaldehyde / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D014306:Trioses / Q000378:metabolism
D014306:Trioses; D011765:Pyruvaldehyde; D007770:L-Lactate Dehydrogenase; D008190:Lyases; D007791:Lactoylglutathione Lyase; D005978:Glutathione; D005990:Glycerol