Inhibitors of glyoxalase I in vitro.
Inhibition in vitro of human red blood cell glyoxalase I activity was measured by the decrease in the rate of formation of S-D-lactoyl-glutathione as determined by the change in absorbance at 240 nm. The percentage activity remaining was determined after addition of various potential inhibitor compounds and the concentration for 50% activity was obtained by graphical interpolation. The inhibitors were selected on the basis of their similarity to a possible transition-state enediol intermediate of methylglyoxal. The most effective inhibitors were dihydroxycoumarins with a 50% inhibition of 0.03 mM. Inhibition of methylglyoxal catabolism suggests possible application as chemotherapeutic agents based on the inhibitor characteristics of methylglyoxal.
D001205:Ascorbic Acid / Q000494:pharmacology; D003374:Coumarins / Q000494:pharmacology; D004912:Erythrocytes / Q000201:enzymology; D004929:Esculin / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D007791:Lactoylglutathione Lyase / Q000037:antagonists & inhibitors*; D008190:Lyases / Q000037:antagonists & inhibitors*; D014364:Tryptophan / Q000494:pharmacology
D003374:Coumarins; D004929:Esculin; D014364:Tryptophan; C030123:coumarin; D008190:Lyases; D007791:Lactoylglutathione Lyase; D001205:Ascorbic Acid