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Updated: Jun 10, 2026

Light-driven Enzymatic Decarboxylation
Published on: May 22, 2016
Asymmetric reduction of activated alkenes using an enoate reductase from Gluconobacter oxydans
Nina Richter1, Harald Gröger, Werner Hummel
1evocatal GmbH, Merowingerplatz 1a, 40225 Düsseldorf, Germany.
Abstract:
A recombinant enoate reductase from Gluconobacter oxydans was heterologously expressed, purified, characterised and applied in the asymmetric reduction of activated alkenes. In addition to the determination of the kinetic properties, the major focus of this work was to utilise the enzyme in the biotransformation of different interesting compounds such as 3,5,5-trimethyl-2-cyclohexen-1,4-dione (ketoisophorone) and (E/Z)-3,7-dimethyl-2,6-octadienal (citral). The reaction proceeded with excellent stereoselectivities (>99% ee) as well as absolute chemo- and regioselectivity, only the activated C=C bond of citral was reduced by the enoate reductase, while non-activated C=C bond and carbonyl moiety remained untouched. The described strategy can be used for the production of enantiomerically pure building blocks, which are difficult to prepare by chemical means. In general, the results show that the investigated enoate reductase is a promising catalyst for the use in asymmetric C=C bond reductions.
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