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Artificial Multi‐Enzyme Networks for the Asymmetric Amination of sec ‐Alcohols
Author(s) -
Tauber Katharina,
Fuchs Michael,
Sattler Johann H.,
Pitzer Julia,
Pressnitz Desiree,
Koszelewski Dominik,
Faber Kurt,
Pfeffer Jan,
Haas Thomas,
Kroutil Wolfgang
Publication year - 2013
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201202666
Subject(s) - amination , reductive amination , amine gas treating , alcohol dehydrogenase , chemistry , alcohol , ketone , hydride , redox , alcohol oxidation , biocatalysis , transaminase , primary (astronomy) , organic chemistry , combinatorial chemistry , enzyme , catalysis , reaction mechanism , hydrogen , physics , astronomy
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.