Oxaloacetate decarboxylase of Klebsiella pneumoniae was shown to contain between 0.6 and 1.0 mol zinc per mol enzyme in different preparations. The decarboxylase activity was completely abolished after 15 min incubation with 1 mM Hg(NO3)2 in phosphate buffer, while the activity decreased only 20% if the incubation was performed in MES/Tris buffer. Treatment of the isolated subunits with Hg(NO3)2 indicated that the binding site for Hg2+ ions is on the alpha subunit. Other inhibitors of the decarboxylase are KSCN and diethylstilbestrol. Inactivation of the enzyme with 2% 1-butanol was significantly reduced by 100 mM NaCl. Sodium ions also protected the isolated beta + gamma subunits from a digestion with trypsin.