Directed evolution and axial chirality:: optimization of the enantioselectivity of Pseudomonas aeruginosa lipase towards the kinetic resolution of a racemic allene

被引:40
作者
Carballeira, Jose Daniel
Krumlinde, Patrik
Bocola, Marco
Vogel, Andreas
Reetz, Manfred T.
Baeckvall, Jan-E.
机构
[1] Max Planck Inst Kohlenforsch, D-45470 Mulheim, Germany
[2] Stockholm Univ, Arrhenius Lab, Dept Organ Chem, SE-10691 Stockholm, Sweden
关键词
D O I
10.1039/b700849j
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Directed evolution of Pseudomonas aeruginosa lipase by the use of combinatorial active site saturation test ( CAST) criteria provided a highly enantioselective mutant (Leu162Phe) for kinetic resolution of an axially chiral allene, p-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate ( E = 111); the high enantioselectivity of the Leu162Phe mutant was rationalized by pi - pi stacking.
引用
收藏
页码:1913 / 1915
页数:3
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