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Dörte Gocke, Lydia Walter, Ekaterina Gauchenova, Geraldine Kolter, Michael Knoll, Catrine L. Berthold, Gunter Schneider, Jürgen Pleiss, Michael Müller and Martina Pohl Rational Protein Design of ThDP-Dependent Enzymes—Engineering Stereoselectivity ChemBioChem 9

Version of Record online: 25 JAN 2008 | DOI: 10.1002/cbic.200700598

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Switching enantiomers: When thiamin diphosphate-dependent enzymes catalyze C[BOND]C bond formation with aldehydes to form 2-hydroxyketones they are usually strictly R selective. Using a structure-guided approach we have identified the molecular reason for their latent inherent S selectivity, which now opens up access to the in silico design of S-selective biocatalysts (see figure).

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