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• W1986573849 endingPage "1802" @default.
• W1986573849 startingPage "1797" @default.
• W1986573849 abstract "An aminomutase, naturally catalyzing the interconversion of (S)-α-phenylalanine and (R)-β-phenylalanine, was converted into an ammonia lyase catalyzing the nonoxidative deamination of phenylalanine to cinnamic acid by a rational single-point mutation. It could be shown by crystal structures and kinetic data that the flexibility of the lid that covers the active site decides whether the enzyme acts as a lyase or a mutase. An Arg92Ser mutation destabilized the closed conformation of the lid structure and converted the mutase into a lyase that exhibited up to 44-fold increased reaction rates in the enantioselective deamination of (R)-β-phenylalanine. In addition, the amination rates of cinnamic acid yielding optically pure (S)-α- and (R)-β-phenylalanine were doubled. The applicability of the mutant enzyme for kinetic resolution and asymmetric amination could be shown by biocatalysis on a preparative scale." @default.
• W1986573849 created "2016-06-24" @default.
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• W1986573849 date "2013-04-02" @default.
• W1986573849 modified "2023-10-16" @default.
• W1986573849 title "Redesign of a Phenylalanine Aminomutase into a Phenylalanine Ammonia Lyase" @default.
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• W1986573849 doi "https://doi.org/10.1002/cctc.201200871" @default.
• W1986573849 hasPublicationYear "2013" @default.
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