title: Artificial multi-enzyme networks for the asymmetric amination of sec-alcohols.
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.
authors: Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, 8010 Graz, Austria.
authors: Katharina
authors: K
authors: Tauber
authors: Michael
authors: M
authors: Fuchs
authors: Johann H
authors: JH
authors: Sattler
authors: Julia
authors: J
authors: Pitzer
authors: Desiree
authors: D
authors: Pressnitz
authors: Dominik
authors: D
authors: Koszelewski
authors: Kurt
authors: K
authors: Faber
authors: Jan
authors: J
authors: Pfeffer
authors: Thomas
authors: T
authors: Haas
authors: Wolfgang
authors: W
authors: Kroutil
mesh_terms: D000438:Alcohols / Q000737:chemistry*; D000586:Amination; D000588:Amines / Q000138:chemical synthesis*; D010084:Oxidation-Reduction; D013237:Stereoisomerism
chemical_list: D000438:Alcohols; D000588:Amines