3.5.1.98	Co2+	-	696240	
3.5.1.98	Co2+	activates	756047	
3.5.1.98	Co2+	ratio of kcat to KM value in presence of metal ion in decreasing order: Co(II), Fe(II), Zn(II), Ni(II)	678192	
3.5.1.98	Fe2+	-	696240	
3.5.1.98	Fe2+	activates, Fe(II)-HDAC8 is sensitive to oxidation and is not activated by Fe(III)	756047	
3.5.1.98	Fe2+	isozyme HDAC8 has higher activity with a bound Fe(II) than Zn(II), although Fe(II)-HDAC8 rapidly loses activity under aerobic conditions	735224	
3.5.1.98	Fe2+	ratio of kcat to KM value in presence of metal ion in decreasing order: Co(II), Fe(II), Zn(II), Ni(II). Fe(II) bound to enzyme is readily oxidized to Fe(III) upon exposure to oxygen	678192	
3.5.1.98	K+	K+ bound to monovalent cation site 2 enhances catalytic activity of HDAC8 45fold with maximal deacetylase activity observed at 10 mM KCl. K+ is the predominant monovalent cation bound to HDAC8 in vivo, K+ binding to site 1 enhances the affinity of HDAC8 for suberoylanilide hydroxamic acid	712485	
3.5.1.98	K+	presence of two potassium ions in the structure of isoform HDAC8, one of which interacts with the key catalytic residues. Direct role of potassium in fold stabilization	682501	
3.5.1.98	Mg2+	required	733817