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. 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.
Original language | English (US) |
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Pages (from-to) | 77-80 |
Number of pages | 4 |
Journal | Journal of medicinal chemistry |
Volume | 20 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1 1977 |