Synthesis and kinetic evaluation of S- and N-substituted cysteinylglycines as inhibitors of glyoxalase I.
Eight S- and N-substituted L-cysteinylglycines were prepared by condensation of S-benzyl-L-cysteinylglycine or S-(p-bromobenzyl)-L-cysteinylglycine with glutaric anhydride, succinic anhydride, or the appropriately blocked and activated amino acids. In contrast to the previously prepared S-substituted glutathiones, all of the title compounds exhibited noncompetitive inhibition of yeast glyoxalase I. A kinetic evaluation under Yonetani-Thorell conditions established the existence of two binding sites on the glyoxalase I enzyme.
D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D003545:Cysteine / Q000031:analogs & derivatives; D004151:Dipeptides / Q000138:chemical synthesis*; D005069:Evaluation Studies as Topic; D005998:Glycine / Q000031:analogs & derivatives; D007700:Kinetics; D007791:Lactoylglutathione Lyase / Q000037:antagonists & inhibitors*; D008190:Lyases / Q000037:antagonists & inhibitors*
D004151:Dipeptides; D008190:Lyases; D007791:Lactoylglutathione Lyase; D003545:Cysteine; D005998:Glycine