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 three enoate reductases for their reduction potential in nitro-substituted compounds. High degrees of conversion, regio- and stereo-selectivity were observed for reduction of substrates such as 1-nitro-2-phenylpropene. 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.