Artificial Multi-Enzyme Networks for the Asymmetric Amination of sec-Alcohols

• Published in: Chemistry : a European journal Vol. 19; no. 12; pp. 4030 - 4035
• Main Authors: Tauber, Katharina, Fuchs, Michael, Sattler, Johann H., Pitzer, Julia, Pressnitz, Desiree, Koszelewski, Dominik, Faber, Kurt, Pfeffer, Jan, Haas, Thomas, Kroutil, Wolfgang
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 18.03.2013; WILEY‐VCH Verlag; Wiley Subscription Services, Inc
• Subjects: Alcohol; Alcohols; Alcohols - chemistry; Amination; Amines; Amines - chemical synthesis; Asymmetry; Biotechnology; Cascades; Chemistry; Conversion; Design engineering; domino reactions; enzymes; Ketones; Networks; oxidation; Oxidation-Reduction; Stereoisomerism
• ISSN: 0947-6539; 1521-3765
• DOI: 10.1002/chem.201202666

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 ed 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. Trickle‐down effect: The asymmetric amination of sec‐alcohols to the corresponding α‐chiral primary amines was performed with a biocatalytic cascade whereby the various steps were interconnected through the cofactors/cosubstrates. In a redox‐neutral cascade and under optimised conditions, up to 91 % conversion of an alcohol to the amine was achieved.