Generation of new imine reducing enzymes - expansion of the imine reductase sequence space
September 24-28, 2017
The synthesis of chiral molecules by asymmetric hydrogenation applying rhodium and ruthenium-based metal catalysts and molecular H2 as hydride donor is an important and established technology in the pharmaceutical and fine-chemical industries.1 The tremendous progress in enzyme discovery, enzyme engineering and process development made in recent years enable to extend these technologies by biocatalytic alternatives. Many reductase enzymes catalyzing the stereocontrolled addition of hydrogen from NAD(P)H to α,ß-unsaturated carbonyl compounds, cyclic/acyclic imines and aldehydes/ketones are described.2 The latest discovered enzymes in this field are imine reductases (IREDs), catalyzing the reduction of various C=N bonds.3 Recently the structural similarity of IREDs to ß-hydroxyacid dehydrogenases (ßHADs) was investigated4, suggesting a common ancestry to C=O reducing enzymes.
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Maike Lenz, Silvia Fademrecht, Bernhard Hauer, Bettina Nestl, and Jürgen Pleiss, "Generation of new imine reducing enzymes - expansion of the imine reductase sequence space" in "Enzyme Engineering XXIV", Pierre Monsan, Toulouse White Biotechnology, France Magali Remaud-Simeon, LISBP-INSA, University of Toulouse, France Eds, ECI Symposium Series, (2017). http://dc.engconfintl.org/enzyme_xxiv/68