Growth inhibitory properties of aromatic alpha-ketoaldehydes toward bacteria and yeast. Comparison of inhibition and glyoxalase I activity.
The alpha-ketoaldehydes methylglyoxal and substituted phenylglyoxals are similar in their abilities to inhibit the growth of Escherichia coli and yeast. When logarithmically growing cells are added to media containing 0.3-1 mM alpha-ketoaldehyde, growth stops for several hours, after which normal growth resumes. The period of growth inhibition does not appear to show any correlation with the ability of glyoxalase I to detoxify these alpha-ketoaldehydes. E. coli and yeast glyoxalase I show markedly different substrate specificities. For example, although both enzymes show broad specificity for both aliphatic and aromatic alpha-ketoaldehydes, 2,4,6-trimethylphenylglyoxal is a substrate for the E. coli enzyme but not for the yeast enzyme. Nevertheless, this alpha-ketoaldehyde inhibits the growth of both E. coli and yeast, similar to the other alpha-ketoaldehydes. Enzymes other than glyoxalase I must play a major role in the metabolism of these alpha-ketoaldehydes during the period of growth inhibition.
D000447:Aldehydes / Q000494:pharmacology*; D003864:Depression, Chemical; D004926:Escherichia coli / Q000201:enzymology* / Q000254:growth & development; D005978:Glutathione / Q000494:pharmacology; D006037:Glyoxal / Q000031:analogs & derivatives / Q000494:pharmacology; D007700:Kinetics; D007791:Lactoylglutathione Lyase / Q000378:metabolism*; D008190:Lyases / Q000378:metabolism*; D011765:Pyruvaldehyde / Q000494:pharmacology; D015003:Yeasts / Q000201:enzymology* / Q000254:growth & development
D000447:Aldehydes; D006037:Glyoxal; D011765:Pyruvaldehyde; D008190:Lyases; D007791:Lactoylglutathione Lyase; D005978:Glutathione