Enhancing activity and controlling stereoselectivity in a designed PLP-dependent aldolase

被引:36
作者
Toscano, Miguel D. [1 ]
Mueller, Manuel M. [1 ]
Hilvert, Donald [1 ]
机构
[1] ETH, Organ Chem Lab, CH-8093 Zurich, Switzerland
关键词
aldolases; amino acids; biocatalysis; rational design; stereoselectivity;
D O I
10.1002/anie.200700710
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码:4468 / 4470
页数:3
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