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亮氨酸氨肽酶对硫代肽的作用

The behaviour of leucine aminopeptidase towards thionopeptides.

作者信息

Beattie R E, Elmore D T, Williams C H, Guthrie D J

机构信息

Department of Biochemistry, Queen's University, Belfast, Northern Ireland, U.K.

出版信息

Biochem J. 1987 Jul 1;245(1):285-8. doi: 10.1042/bj2450285.

Abstract

Thionoleucine S-anilide (Leut-anilide), Leut-Gly-OEt and Leut-Phe-OMe were synthesized and shown to be competitive inhibitors of leucine aminopeptidase from pig kidney. The kinetics of inhibition were determined in the presence of leucine 4-methylcoumarin-7-amide as substrate. Although the compounds showed only moderate inhibitory potency, it was found that all were resistant to hydrolysis by the enzyme, in contrast with the reported behaviour of some thionopeptide analogues of substrates for other Zn2+-peptidases such as carboxypeptidase A and angiotensin-converting enzyme.

摘要

合成了硫代亮氨酸S-苯胺(亮氨酸苯胺)、亮氨酰-甘氨酸乙酯和亮氨酰-苯丙氨酸甲酯,并证明它们是猪肾亮氨酸氨肽酶的竞争性抑制剂。在以亮氨酸4-甲基香豆素-7-酰胺为底物的情况下测定了抑制动力学。尽管这些化合物仅表现出中等的抑制效力,但发现它们都能抵抗该酶的水解,这与报道的其他锌离子肽酶(如羧肽酶A和血管紧张素转换酶)底物的一些硫代肽类似物的行为形成对比。

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