Overcoming Thermodynamic and Kinetic Limitations of Aldolase-Catalyzed Reactions by Applying Multienzymatic Dynamic Kinetic Asymmetric Transformations


  • The Österreichische Forschungsförderungsgesellschaft (FFG), the Province of Styria, the Styrian Business Promotion Agency (SFG), the City of Graz, the Fonds zur Förderung der wissenschaftlichen Forschung (FWF, project W901-B05 DK Molecular Enzymology), and the European Commission (within the framework of a Marie-Curie Industrial Host Fellowship to M.S. and M.W.) are acknowledged for financial support. We would like to thank Marcel Wubbolts, Theo Sonke, and Kurt Faber for stimulating discussions, as well as to Karl Gruber and Michael Uhl for the model of L-threonine aldolase in the Table of Contents graphic.


original image

Dynamic and successful: The asymmetric synthesis of 2-amino-1-phenylethanol was achieved by aminomethylation of benzaldehyde in the presence of the two enzymes L-threonine aldolase and L-tyrosine decarboxylase in a novel one-pot, two-enzyme process (see scheme). A modified method with three enzymes led to the enantioenriched amino alcohol in very high yield.