Yasutake A, Miyazaki K, Aoyagi H, Kato T, Izumiya N
Int J Pept Protein Res. 1980 Jul;16(1):61-5.
Four stereoisomers of a cyclic depsidipeptide containing a lysine and a 2-hydroxy-3-phenylpropanoic acid (Hpp) residue have been synthesized and their susceptibility toward trypsin examined. Trypsin hydrolyzed cyclo(-L-Lys-L-Hpp-) (I-LL) and cyclo(-L-Lys-D-Hpp-) (I-LD) rapidly and cyclo(-D-Lys-L-Hpp-) (I-DL) and cyclo(-D-Lys-D-Hpp-) (I-DD) very slowly. Proteolytic coefficients of these substrates and a reference compound are shown as follows: I-LL, 112; I-LD, 34; I-DL, 0.34; I-DD, 0.11, and Ac-L-Lys-OEt, 44. Possible mode of actin of trypsin on these substrates was discussed.
已经合成了一种含有赖氨酸和2-羟基-3-苯基丙酸（Hpp）残基的环状缩二肽的四种立体异构体，并检测了它们对胰蛋白酶的敏感性。胰蛋白酶能快速水解环（-L-赖氨酸-L-Hpp-）（I-LL）和环（-L-赖氨酸-D-Hpp-）（I-LD），而环（-D-赖氨酸-L-Hpp-）（I-DL）和环（-D-赖氨酸-D-Hpp-）（I-DD）的水解速度非常慢。这些底物和一种参考化合物的蛋白水解系数如下：I-LL为112；I-LD为34；I-DL为0.34；I-DD为0.11，而乙酰-L-赖氨酸乙酯为44。文中讨论了胰蛋白酶对这些底物的可能作用模式。
