Correlation Engine 2.0
Clear Search sequence regions

Sizes of these terms reflect their relevance to your search.

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.


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

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 23341101

View Full Text