胰蛋白酶和蜜环菌蛋白酶在ε-N-甲酰赖氨酸残基处的切割作用。
Cleavage by trypsin and by the proteinase from Armillaria mellea at epsilon-N-formyl-lysine residues.
作者信息
Barry F P, Doonan S, Ross C A
出版信息
Biochem J. 1981 Mar 1;193(3):737-42. doi: 10.1042/bj1930737.
Abstract
Kinetic studies were made of the hydrolysis by trypsin of alpha-N-acetylglycyl-L-lysine methyl ester and of its neutral analogue alpha-N-acetylglycyl-epsilon-N-formyl-L-lysine methyl ester. The latter substance is a moderately good substrate for trypsin, and this observation is discussed in terms of the substrate specifically of the enzyme. The actions of trypsin and of the lysine-specific proteinase from Armillaria mellea on both a native and a formylated polypeptide substrate were compared. Both enzymes were found to hydrolyse specifically bonds to epsilon-N-formyl-lysine in the formylated substrate.
摘要
对α-N-乙酰甘氨酰-L-赖氨酸甲酯及其中性类似物α-N-乙酰甘氨酰-ε-N-甲酰-L-赖氨酸甲酯被胰蛋白酶水解的过程进行了动力学研究。后一种物质是胰蛋白酶的中等良好底物，本文根据该酶的底物特异性对这一观察结果进行了讨论。比较了胰蛋白酶和蜜环菌赖氨酸特异性蛋白酶对天然和甲酰化多肽底物的作用。发现这两种酶都能特异性水解甲酰化底物中与ε-N-甲酰赖氨酸相连的键。
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