Asymmetric Bioreduction of C=C Wih OPR1 and OPR3 From Arabidopsis Thaliana

The use of biocatalysts in enantiomerically pure compound synthesis garners increasing attention in fine chemistry and pharma. Bioreductions of activated alkenes by enoate reductases is one of the emerging biosynthetic tools for substrates such as enals, enones, and nitroalkenes. In this study, we have characterized enoate reductases OPR1 and OPR3 from Arabidopsis thaliana for their biocatalytically specificity and stability. In order to broaden the applicability of the enzymes, we investigated the substrate specificity using wide range of C=C activating groups including aldehyde-, ketone-, imide-, and carboxylic acid- moieties. The study explored the possibilities of reduction amination of nitro-substituted alkenes for efficient synthesis of asymmetric amines. Lastly, the enoate reductases also coupled with glucose dehydrogenase for development of efficient cofactor recycling system.