A chymotrypsin-catalyzed modification of rabbit muscle aldolase.
A chymotrypsin-catalyzed modification of rabbit muscle aldolase.
复制标题
胰凝乳蛋白酶催化的兔肌肉醛缩酶修饰。
DOI：
10.1016/s0021-9258(19)45185-5
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发表时间：
1972
期刊：
影响因子：
--
通讯作者：
A. Mehler
中科院分区：
文献类型：
--
作者：
C. F. Midelfort;A. Mehler
在二磷酸底物或底物类似物的存在下，兔肌肉醛缩酶通过胰凝乳蛋白酶进行有限的蛋白水解。唯一的产物是具有改性催化性质的酶和分别从α和β亚基的COOH末端去除的两个六肽。该酶产物具有类似于经羧肽酶A修饰的醛缩酶的催化性质，因为它保留了以果糖1-磷酸为底物的全部活性，但以果糖1，6-二磷酸为底物时失去了95%的原始活性。六肽的结构为Ile-Ser-Asn-His-Ala-Tyr（α亚基）和Ile-Ser-Asp-His-Ala-Tyr（β亚基），并且从成年动物获得的醛缩酶制剂中产生的量大致相等。
In the presence of a diphosphate substrate or substrate analogue, rabbit muscle aldolase undergoes a limited proteolysis by chymotrypsin. The sole products are an enzyme with modified catalytic properties and two hexapeptides removed from the COOH terminus of the α and β subunits, respectively. The enzyme product has catalytic properties similar to those of aldolase modified by carboxypeptidase A in that it retains full activity with fructose 1-phosphate as substrate but has lost 95% of the original activity with fructose 1,6-diphosphate as substrate. The hexapeptides have the structures Ile-Ser-Asn-His-Ala-Tyr (α subunit) and Ile-Ser-Asp-His-Ala-Tyr (β subunit) and are produced in approximately equal amounts from aldolase preparations obtained from adult animals.