Enoate reductases (ER) selectively reduce carbon-carbon double bonds in α/β-unsaturated carbonyl compounds and thus can be employed advantageously to prepare enantiomerically pure aldehydes, ketones, and esters. However, current enoate reductases are either biochemically very well characterized, most notably Old Yellow Enzyme (OYE), or they only have been used in whole-cell systems, with endogenous ketoreductases often interfering with the ER activity. Here, we clone the genes and express three different non-related enoate reductases and observe that all three proteins showed broad enoate reductase specificity and broad temperature and pH optima but different patterns. By coupling one of these novel enoate reductases with glucose dehydrogenase (GDH) to recycle NADP(H), conversion of >99% within one hour was obtained for the reduction of 2-cyclohexenone.. In summary, we successfully demonstrate the wide specificity of enoate reductases for a range of α/β-unsaturated carbonyl compounds as well as coupling to glucose dehydrogenase for recycling of NAD(P)(H).