Literature DB >> 23341101

Artificial multi-enzyme networks for the asymmetric amination of sec-alcohols.

Katharina Tauber1, Michael Fuchs, Johann H Sattler, Julia Pitzer, Desiree Pressnitz, Dominik Koszelewski, Kurt Faber, Jan Pfeffer, Thomas Haas, Wolfgang Kroutil.   

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

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Year:  2013        PMID: 23341101     DOI: 10.1002/chem.201202666

Source DB:  PubMed          Journal:  Chemistry        ISSN: 0947-6539            Impact factor:   5.236


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