Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine (PubMed:28516954). Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine (PubMed:28516954). Has a very weak lysine deacetylase, if any (PubMed:28516954). H2O + N(8)-acetylspermidine = acetate + spermidine H2O + N-acetylputrescine = acetate + putrescine H2O + N-acetylcadaverine = acetate + cadaverine Excluded from the nucleoli. Belongs to the histone deacetylase family. HD type 2 subfamily. Originally thought to be a histone deacetylase and shown in vitro to have this activity (By similarity). Has also been shown to be involved in MSH2 deacetylation (By similarity). However, protein deacetylase activity is a matter of debate, as 3D structure analysis shows that a glutamate gatekeeper and a sterically constricted active site confer specificity for N(8)-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. Supporting this observation, has been shown to exhibit only very low activity, if any, towards acetyl-lysine peptide substrates (By similarity).