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The tetramer of alcohol dehydrogenase with a molecular weight of 141 kDa contains four identical subunits. The active site of each subunit contains a zinc atom. Each active site also contains 2 reactive sulfhydryl groups and a histidine residue. Isoelectric point: 5.4-5.8 Optimum pH: 8.6-9.0 Substrate: Yeast alcohol dehydrogenase reacts most easily with ethanol, and its reactivity decreases as the volume of alcohol increases or decreases. The reactivity with branched and secondary alcohols is also very low. KM (Chemicalbook Ethanol) = 2.1 x 10-3 MKM (methanol) = 1.3 x 10-1 MKM (isopropanol) = 1.4 x 10-1 M imines and iodoacetamides. Inhibitors of zinc chelators, including 1,10-phenanthroline, 8-hydroxyquinoline, 2,2'-bipyridine, and thiourea. Substrate analog inhibitors, including β-NAD analogs, purine and pyrimidine derivatives, chloroethanol, and fluoroethanol.