Active‐Site Mechanisms of the Carbonic Anhydrases a
Active‐Site Mechanisms of the Carbonic Anhydrases a
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碳酸酐酶的活性位点机制
DOI：
10.1111/j.1749-6632.1984.tb12316.x
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发表时间：
1984
影响因子：
5.2
通讯作者：
T. Deits
中科院分区：
文献类型：
--
作者：
Y. Pocker;T. Deits
在过去的二十年中，碳酸酐酶（CA）（EC 4.2.1.1）在持续阐明酶活性的基本原理方面发挥了重要作用。除了其内在的生理重要性，CA是一种非常方便的研究酶。分离的锌金属酶在溶液中和储存期间是稳定的;事实上，高活性形式CA 11可以耐受5.5至12范围内的pH值。由于其显著的催化能力和强大的结构，CA被转化为一个名副其实的“实验室”，其中酶催化被严格测试，并采用溶液化学的许多原则进行探索。
During the last twenty years, carbonic anhydrase (CA) (EC 4.2.1.1) has played a significant role in the continuing illumination of the principles underlying enzyme activity. In addition to its intrinsic physiological importance, CA is an extremely convenient enzyme for study. The isolated zinc metalloenzyme is stable in solution and during storage; in fact, the highly active form, CA 11, can tolerate pH values in the range 5.5 to 12. As a result of its pronounced catalytic power and robust constitution, CA was transformed into a veritable “laboratory” in which enzyme catalysis was rigorously tested and explored employing the numerous principles of solution chemistry.
溶剂氘同位素在人碳酸酐酶 II 催化氧 18 交换中的作用。
影响因子：
2.9
作者：
Tu,CK;Silverman,DN
通讯作者：
Silverman,DN