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Extended Catalytic Scope of a Well‐Known Enzyme: Asymmetric Reduction of Iminium Substrates by Glucose Dehydrogenase
Authors:Sebastian Roth  Dr Andreas Präg  Dr Cindy Wechsler  Marija Marolt  Sascha Ferlaino  Dr Steffen Lüdeke  Dr Nicolas Sandon  Dr Dennis Wetzl  Dr Hans Iding  Dr Beat Wirz  Prof?Dr Michael Müller
Affiliation:1. Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universit?t Freiburg, Freiburg, Germany;2. Process Chemistry and Catalysis, F. Hoffmann–La Roche, Ltd., Basel, Switzerland
Abstract:NADP(H)‐dependent imine reductases (IREDs) are of interest in biocatalytic research due to their ability to generate chiral amines from imine/iminium substrates. In reaction protocols involving IREDs, glucose dehydrogenase (GDH) is generally used to regenerate the expensive cofactor NADPH by oxidation of d ‐glucose to gluconolactone. We have characterized different IREDs with regard to reduction of a set of bicyclic iminium compounds and have utilized 1H NMR and GC analyses to determine degree of substrate conversion and product enantiomeric excess (ee). All IREDs reduced the tested iminium compounds to the corresponding chiral amines. Blank experiments without IREDs also showed substrate conversion, however, thus suggesting an iminium reductase activity of GDH. This unexpected observation was confirmed by additional experiments with GDHs of different origin. The reduction of C=N bonds with good levels of conversion (>50 %) and excellent enantioselectivity (up to >99 % ee) by GDH represents a promiscuous catalytic activity of this enzyme.
Keywords:biotransformations  enantioselectivity  enzyme promiscuity  oxidoreductases  tertiary amines
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