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• W2135788051 startingPage "3287" @default.
• W2135788051 abstract "Abstract Directed evolution utilizing iterative saturation mutagenesis (ISM) has been applied to the old yellow enzyme homologue YqjM in the quest to broaden its substrate scope, while controlling the enantioselectivity in the bioreduction of a set of substituted cyclopentenone and cyclohexenone derivatives. Guided by the known crystal structure of YqjM, 20 residues were selected as sites for saturation mutagenesis, a pooling strategy based on the method of Phizicky [M. R. Martzen, S. M. McCraith, S. L. Spinelli, F. M. Torres, S. Fields, E. J. Grayhack, E. M. Phizicky, Science 1999 , 286 , 1153–1155] being used in the GC screening process. The genes of some of the hits were subsequently employed as templates for randomization experiments at the other putative hot spots. Both ( R )‐ and ( S )‐selective variants were evolved using 3‐methylcyclohexenone as the model substrate in the asymmetric bioreduction of the olefinic functionality, only small mutant libraries and thus minimal screening effort being necessary. Some of the best mutants also proved to be excellent catalysts when testing other prochiral substrates without resorting to additional mutagenesis/screening experiments. Thus, the results constitute an important step forward in generalizing the utility of ISM as an efficient method in laboratory evolution of enzymes as catalysts in organic chemistry." @default.
• W2135788051 created "2016-06-24" @default.
• W2135788051 creator A5050231254 @default.
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• W2135788051 creator A5085683830 @default.
• W2135788051 date "2009-12-01" @default.
• W2135788051 modified "2023-10-18" @default.
• W2135788051 title "Directed Evolution of an Enantioselective Enoate-Reductase: Testing the Utility of Iterative Saturation Mutagenesis" @default.
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• W2135788051 doi "https://doi.org/10.1002/adsc.200900644" @default.
• W2135788051 hasPublicationYear "2009" @default.
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