Involved in polyamine metabolism. Catalyzes the deacetylation of various acetylated polyamines such as N-acetylputrescine, N-acetylcadaverine, N(1)-acetylspermine, N(1)-acetylspermidine and N(8)-acetylspermidine (PubMed:8824626, PubMed:3207420). In vitro, is also able to deacetylate L-Lys(epsilon-acetyl)coumarin, but has very low activity towards the larger tetrapeptide N-acetyl-L-Arg-L-His-L-Lys(epsilon-acetyl)-L-Lys(epsilon-acetyl)coumarin (PubMed:21268586). H2O + N-acetylputrescine = acetate + putrescine H2O + N-acetylcadaverine = acetate + cadaverine H2O + N(1)-acetylspermine = acetate + spermine H2O + N(1)-acetylspermidine = acetate + spermidine H2O + N(8)-acetylspermidine = acetate + spermidine Binds 1 zinc ion per subunit. Zinc ions inhibit enzyme activity in a dose-dependent manner (PubMed:8824626). Inhibited by KCl at concentrations above 10 mM (PubMed:21268586). Inhibited by o-oxyquinoline in vitro, suggesting that it is a metalloprotein (PubMed:3207420). Inhibited by various substrate N(8)-acetylspermidine analogs bearing different metal-binding groups such as trifluoromethylketone, thiol, or hydroxamate, and by hydroxamate analogs of short-chain acetyldiamines (PubMed:26200446). Optimum pH is 9 with acetylputrescine, N(1)-acetylspermidine, and N(8)-acetylspermidine as substrates, and is 8 with acetylcadaverine as substrate. Amine and polyamine metabolism. Homodimer. Belongs to the histone deacetylase family.