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Issue 19, 2007
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Directed evolution and axial chirality: optimization of the enantioselectivity of Pseudomonas aeruginosa lipase towards the kinetic resolution of a racemic allene

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Abstract

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.

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

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Publication details

The article was received on 18 Jan 2007, accepted on 02 Feb 2007 and first published on 21 Feb 2007


Article type: Communication
DOI: 10.1039/B700849J
Citation: Chem. Commun., 2007, 1913-1915
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    Directed evolution and axial chirality: optimization of the enantioselectivity of Pseudomonas aeruginosa lipase towards the kinetic resolution of a racemic allene

    J. D. Carballeira, P. Krumlinde, M. Bocola, A. Vogel, M. T. Reetz and Jan-E. Bäckvall, Chem. Commun., 2007, 1913
    DOI: 10.1039/B700849J

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