Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase
Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase
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DOI：
10.1021/ja065064
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发表时间：
2007-01-31
影响因子：
15
通讯作者：
Guo, Zhihong
中科院分区：
文献类型：
--
作者：
Jiang, Ming;Guo, Zhihong
大分子拥挤被发现显着提高肠杆菌素特异性异分支酸合酶的内在催化效率，通过诱导酶的结构变化。这一发现提供了第一个实验证据，即在不存在拥挤易感大分子缔合的情况下，大分子拥挤直接影响蛋白质的结构和功能。
Macromolecular crowding was found to significantly enhance the intrinsic catalytic efficiency of the enterobactin-specific isochorismate synthase by inducing structural change in the enzyme. This finding provides the first experimental evidence that macromolecular crowding directly affects protein structure and function in the absence of crowding-susceptible macromolecular association.