Design of cosubstrate binding behavior of ene reductases for asymmetric syntheses

Christoph Mähler, doctoral thesis Technical University of Munich, 2019

The economically and ecologically unfavorable but pronounced NADPH preference of the cyanobacterial ene reductase NostocER1 was deliberately changed by the exchange of surface loops. As a result, an increase in catalytic efficiency with the industrially preferred cosubstrate NADH was achieved by almost one order of magnitude. Optimized ene reductases overexpressed in NADH regenerating E. coli enabled a particularly efficient reduction of the terpene (R)-carvone in a stirred-tank reactor.



  • Mähler C, Burger C, Kratzl F, Weuster-Botz D, Castiglione K (2019): Asymmetric whole-cell bioreductions of (R)-carvone using optimized ene reductases. Molecules 24: 2550.
  • Mähler C, Kratzl F, Vogel M, Vinnenberg S, Weuster-Botz D, Castiglione K (2019): Loop swapping as a potent approach to increase ene reductase activity with NADH. Adv Syn Cat 361: 2505-2513.