胃蛋白酶活性位点的一个天冬氨酸残基。七肽的分离与序列分析。
An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide.
作者信息
Bayliss R S, Knowles J R, Wybrandt G B
出版信息
Biochem J. 1969 Jun;113(2):377-86. doi: 10.1042/bj1130377.
Abstract
Pepsin reacts stoicheiometrically with the active-site-directed irreversible inhibitor N-diazoacetyl-l-phenylalanine methyl ester, with concomitant loss of all proteolytic and peptidolytic activity. The reagent esterifies a unique aspartic acid residue in pepsin, which is in the sequence:Ile-Val-Asp-Thr-Gly-Thr-Ser
摘要
胃蛋白酶与活性位点导向的不可逆抑制剂N-重氮乙酰基-L-苯丙氨酸甲酯发生化学计量反应，同时所有蛋白水解和肽水解活性丧失。该试剂使胃蛋白酶中一个独特的天冬氨酸残基酯化，其序列为：异亮氨酸-缬氨酸-天冬氨酸-苏氨酸-甘氨酸-苏氨酸-丝氨酸
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本文引用的文献
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Specific inactivation of pepsin by a diazo ketone.重氮酮对胃蛋白酶的特异性失活作用。
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Stereochemical investigation of the active center of pepsin using a new inactivator.使用新型失活剂对胃蛋白酶活性中心进行立体化学研究。
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