| Literature DB >> 23341101 |
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.Entities:
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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