Synthesis and kinetic evaluation of S- and N-substituted cysteinylglycines as inhibitors of glyoxalase I

Abstract

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. All title compounds exhibited noncompetitive inhibition of yeast glyoxalase I. A kinetic evaluation under Yonetani-Thorell conditions established the existence of 2 binding sites on the glyoxalase I enzyme.