Directed evolution and axial chirality: optimization of the enantioselectivity of Pseudomonas aeruginosa lipase towards the kinetic resolution of a racemic allene
Literature Information
José Daniel Carballeira, Patrik Krumlinde, Marco Bocola, Andreas Vogel, Manfred T. Reetz, Jan-E. Bäckvall
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 π–π stacking.
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