The Enzymatic Asymmetric Conjugate Umpolung Reaction

Authors

  • Carola Dresen Dr.,

    1. Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany), Fax: (+49) 761-203-6351
    Search for more papers by this author
  • Michael Richter Dr.,

    1. Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany), Fax: (+49) 761-203-6351
    2. Laboratory for Biomaterials, Empa, Swiss Federal Laboratories for Materials Science and Technology, Lerchenfeldstrasse 5, 9014 St. Gallen (Switzerland)
    Search for more papers by this author
  • Martina Pohl Prof. Dr.,

    1. Institut für Biotechnologie 2, Forschungszentrum Jülich GmbH, 52425 Jülich (Germany)
    Search for more papers by this author
  • Steffen Lüdeke Dr.,

    1. Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany), Fax: (+49) 761-203-6351
    Search for more papers by this author
  • Michael Müller Prof. Dr.

    1. Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany), Fax: (+49) 761-203-6351
    Search for more papers by this author

  • We thank E. Breitling for skillful technical support and V. Brecht for measurement of NMR spectra. We are grateful to Prof. Georg Fuchs for helpful discussions. We would like to acknowledge the use of the computing resources provided by the Black Forest Grid Initiative.

Abstract

original image

The Stetter reaction employs synthetically useful umpolung reactivity to provide catalytic access to 1,4-bifunctional molecules. The first enzymatic 1,4-addition is described, with the ThDP-dependent enzyme PigD, which makes the challenging asymmetric intermolecular Stetter reaction accessible.

Ancillary