Enoate reductases (ER) selectively reduce carbon-carbon double bonds in a/b-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. However, not many ERs are biocatalytically characterized as to specificity and stability. 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. All three proteins prefer NADPH as cofactor over NADH and are stable up to 40°C. 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. Upon lowering the enzyme loadings, we discovered rapid deactivation of either enzyme, especially of the thermostable GDH. We found that the presence of enone substrate is responsible for the deactivation but not the presence of oxygen or elevated temperature. In summary, we successfully demonstrate the wide specificity of enoate reductases for a range of a/b-unsaturated carbonyl compounds as well as coupling to glucose dehydrogenase for recycling of NAD(P)(H); however, the stability limitations we found need to be overcome to envision large-scale use of enoate reductases in synthesis.