Investigation of the stereochemical course of ene reductase-catalysed reactions by deuterium labelling

The stereoselective redn. of suitably substituted C=C bonds mediated by enzymes, called ene reductases, has received great attention in the last decade. Some successful applications of this biocatalyzed procedure to the synthesis of chiral active pharmaceutical ingredients have been reported in the literature. The generation of suitable models to be used for predicting the stereochem. outcome of this kind of redns. is a challenging task. In the last years we have exploited deuterium labeling to investigate the stereochem. course of the enzyme-mediated redns. of a wide collection of substrates belonging to well-defined chem. classes. The results of this research have allowed us to draw conclusions on the relationship between the structural characteristics of the substrate and the binding mode it adopts in the enzyme active site. The collected data can be exploited to create an empirical model to rationalise and predict the stereoselectivity of old yellow enzyme (OYE)-catalyzed redns.