This subfamily includes bacterial acetylpolyamine amidohydrolase (APAH) as well as other Class II histone deacetylase (HDAC) and related proteins. Deacetylases of class II are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. Mycoplana ramosa APAH exhibits broad substrate specificity and catalyzes the deacetylation of polyamines such as putrescine, spermidine, and spermine by cleavage of a non-peptide amide bond.
Comment:Active center contains inhibitor and a catalytic Zn ion that coordinates side chain atoms of two aspartates and one histidine, and a water molecule.
Comment:Inhibitor M344 is 4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide
Structure:3Q9B: Mycoplana ramosa acetylpolyamine amidohydrolase (APAH) binds hydroxamate inhibitor (M344) and Zn ion; contacts at 4.0A
Jiyao W et al.(2023). "The conserved domain database in 2023.",