Catalytically different from common alcohol dehydrogenases. Effective in oxidizing ethanol, other primary alcohols and benzylalcohol only in the presence of p-nitroso-N,N-dimethylaniline (NDMA) as an electron acceptor. NADH acts as a cofactor here instead as a coenzyme. a primary alcohol + N,N-dimethyl-4-nitrosoaniline = 4-(hydroxylamino)-N,N-dimethylaniline + an aldehyde A + ethanol = acetaldehyde + AH2 Inhibited by trans-4-(N,N-dimethylamino)-cinnamaldehyde through direct binding to the catalytic zinc ion in a substrate-like geometry. Isobutyramide acts as competitive inhibitor with respect to the electron acceptor NDMA. Acetaldehyde, AMP, ADP, ATP, as well as CuSO(4), FeSO(4), HgCl(2), NiCl(2), ZnSO(4), KCN, and NaN(3) are additional inhibitors of the catalytic activity. KM for benzylalcohol is lower than 0.005 mM. Optimum pH is 7. Optimum temperature is 45 degrees Celsius. Homotrimer. Belongs to the zinc-containing alcohol dehydrogenase family.