Lyon P A, Vince R
J Med Chem. 1977 Jan;20(1):77-88. doi: 10.1021/jm00211a015.
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.
通过将S-苄基-L-半胱氨酰甘氨酸或S-(对溴苄基)-L-半胱氨酰甘氨酸与戊二酸酐、琥珀酸酐或适当保护和活化的氨基酸缩合，制备了8种S-和N-取代的L-半胱氨酰甘氨酸。与先前制备的S-取代谷胱甘肽不同，所有标题化合物均表现出对酵母乙二醛酶I的非竞争性抑制作用。在米氏条件下的动力学评估确定了乙二醛酶I酶上存在两个结合位点。
