组氨酸-57已被甲基化的α-胰凝乳蛋白酶的催化活性。
Catalytic activity of -chymotrypsin in which histidine-57 has been methylated.
作者信息
Henderson R
出版信息
Biochem J. 1971 Aug;124(1):13-8. doi: 10.1042/bj1240013.
Abstract
The properties of a derivative of alpha-chymotrypsin in which histidine-57 has been methylated have been examined. Although the modified enzyme binds substrate with the same affinity as does native alpha-chymotrypsin, acylation and deacylation occur at much decreased rates. As for native alpha-chymotrypsin, a basic group of pK(a) approx. 7 is involved in both acylation and deacylation. The significance of these results is considered in relation to the normal function of histidine-57.
摘要
已对组氨酸-57被甲基化的α-胰凝乳蛋白酶衍生物的性质进行了研究。尽管修饰后的酶与天然α-胰凝乳蛋白酶以相同的亲和力结合底物，但酰化和脱酰化的速率却大幅降低。与天然α-胰凝乳蛋白酶一样，一个pK(a)约为7的碱性基团参与了酰化和脱酰化过程。结合组氨酸-57的正常功能对这些结果的意义进行了探讨。
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