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Artificial Multi‐Enzyme Networks for the Asymmetric Amination of sec‐Alcohols
Authors:Katharina Tauber  Michael Fuchs  Johann H Sattler  Julia Pitzer  Desiree Pressnitz  Dr Dominik Koszelewski  Prof Kurt Faber  Jan Pfeffer  Thomas Haas  Prof Wolfgang Kroutil
Institution:1. Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, 8010 Graz (Austria), Fax: (+43)?316‐380‐9840;2. ACIB GmbH, c/o Heinrichstrasse 28, 8010 Graz (Austria);3. Evonik Industries AG, CREAVIS Technologies & Innovation, Paul‐Baumann‐Strasse 1, 45772 Marl (Germany)
Abstract:Various artificial network designs that involve biocatalysts were tested for the asymmetric amination of sec‐alcohols to the corresponding α‐chiral primary amines. The artificial systems tested involved three to five redox enzymes and were exemplary of a range of different sec‐alcohol substrates. Alcohols were oxidised to the corresponding ketone by an alcohol dehydrogenase. The ketones were subsequently aminated by employing a ω‐transaminase. Of special interest were redox‐neutral designs in which the hydride abstracted in the oxidation step was reused in the amination step of the cascade. Under optimised conditions up to 91 % conversion of an alcohol to the amine was achieved.
Keywords:alcohols  amines  domino reactions  enzymes  oxidation
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