Conversion of alcohols to enantiopure amines through dual-enzyme hydrogen-borrowing cascades

Author:

Mutti Francesco G.12,Knaus Tanja2,Scrutton Nigel S.2,Breuer Michael3,Turner Nicholas J.1

Affiliation:

1. School of Chemistry, University of Manchester, Manchester Institute of Biotechnology, Manchester M1 7DN, UK.

2. Manchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, Manchester M1 7DN, UK.

3. BASF SE, White Biotechnology Research, GBW/B-A030, 67056 Ludwigshafen, Germany.

Abstract

A clean and green approach to amines Enzymes evolved to operate in water and to modify their substrates using comparatively nontoxic reagents. Thus, a major advantage of applying enzymes to synthetic chemistry is their compatibility with environmentally benign conditions. Mutti et al. report that two enzymes—alcohol and amine dehydrogenases—can operate in tandem to convert alcohols to amines. The reaction proceeds with ammonium as the only input and water as the only byproduct. The mechanism relies on consecutive oxidation and reduction steps, with hydrogen shuttled by a nicotinamide coenzyme. Science , this issue p. 1525

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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