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). Histone deacetylase activity has been observed in vitro (PubMed:
11861901, PubMed:
11726666, PubMed:
11677242, PubMed:
11739383). Has also been shown to be involved in MSH2 deacetylation (PubMed:
26221039). The physiological relevance of protein/histone deacetylase activity is unclear and could be very weak (PubMed:
28516954). May play a role in the promotion of late stages of autophagy, possibly autophagosome- lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells (PubMed:
23801752, PubMed:
29968769). May play a role in homologous recombination (PubMed:
21247901). May promote DNA mismatch repair (PubMed:
26221039).