Enhancing activity and controlling stereoselectivity in a designed PLP-dependent aldolase.
Enhancing activity and controlling stereoselectivity in a designed PLP-dependent aldolase.
复制标题
增强设计的 PLP 依赖性醛缩酶的活性并控制立体选择性。
DOI：
10.1002/anie.200700710
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发表时间：
2007
影响因子：
--
通讯作者：
D. Hilvert
中科院分区：
文献类型：
--
作者：
M. Toscano;Manuel M Müller;D. Hilvert
Chop and Change：定点突变已被用来优化一种工程的依赖于磷酸的吡哆醛缩醛酶的活性，并逆转其在D-β-苯丝氨酸裂解中固有的苏氨酸选择性。活性中心残基的修饰产生了显著的逆转醛醇活性，在效率和选择性方面与天然酶相比是有利的。
Chop and change: Site-directed mutagenesis has been employed to optimize the activity of an engineered pyridoxal phosphate-dependent aldolase and to invert its inherent threo selectivity in the cleavage of D-β-phenylserines. The modification of the active-site residues generates significant retroaldol activity that compares favorably with that of natural enzymes in terms of efficiency and selectivity.