Rational Protein Design of ThDP-Dependent Enzymes—Engineering Stereoselectivity (pages 406–412)
Dörte Gocke, Lydia Walter, Ekaterina Gauchenova, Geraldine Kolter, Michael Knoll, Catrine L. Berthold, Gunter Schneider, Jürgen Pleiss, Michael Müller and Martina Pohl
Version of Record online: 25 JAN 2008 | DOI: 10.1002/cbic.200700598
Switching enantiomers: When thiamin diphosphate-dependent enzymes catalyze CC 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).