Abstract Four NAD (P) H-dependent non-flavin ene reductases have been investigated for their ability to reduce activated C= C bonds in an asymmetric fashion by using 20 structurally diverse substrates. In comparison with flavin-dependent Old Yellow Enzyme homologues, a higher degree of electronic activation was required, because the best activities were obtained with enals and nitroalkenes rather than enones and carboxylic esters. Although ...
