HDAC10, EnkiLife, AMRe11939

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. 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).