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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. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Citation

Katharina Tauber, Michael Fuchs, Johann H Sattler, Julia Pitzer, Desiree Pressnitz, Dominik Koszelewski, Kurt Faber, Jan Pfeffer, Thomas Haas, Wolfgang Kroutil. Artificial multi-enzyme networks for the asymmetric amination of sec-alcohols. Chemistry (Weinheim an der Bergstrasse, Germany). 2013 Mar 18;19(12):4030-5

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PMID: 23341101

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