Lamden L A, Bartlett P A
Biochem Biophys Res Commun. 1983 May 16;112(3):1085-90. doi: 10.1016/0006-291x(83)91729-1.
Phosphonic acid analogs of N-Cbz-alanine and N-Cbz-phenylalanine have been converted to the ester and amide fluoridates and evaluated as inactivators of elastase (EC 3.4.21.11) and chymotrypsin (EC 3.4.21.1). These inhibitors, which mimic the natural peptide substrates, are the most potent inactivators of elastase and chymotrypsin yet reported, showing a modest selectivity which correlates with the substrate specificity of the two enzymes.
N - 苄氧羰基丙氨酸和N - 苄氧羰基苯丙氨酸的膦酸类似物已被转化为酯和酰胺氟化物，并作为弹性蛋白酶（EC 3.4.21.11）和胰凝乳蛋白酶（EC 3.4.21.1）的失活剂进行评估。这些模拟天然肽底物的抑制剂是迄今为止报道的弹性蛋白酶和胰凝乳蛋白酶最有效的失活剂，显示出适度的选择性，这与两种酶的底物特异性相关。
