3.5.1.98	Mg2+	Zn2+, Mg2+, or Mn2+ is required. Zn2+ is the most efficient	677978	
3.5.1.98	Mn2+	Zn2+, Mg2+, or Mn2+ is required. Zn2+ is the most efficient	677978	
3.5.1.98	Zn2+	Zn2+, Mg2+, or Mn2+ is required. Zn2+ is the most efficient	677978	
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+	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	additional information	the identity of the catalytic metal ion influences both the Michaelis-Menten constant and the affinity of inhibitor suberoylanilide hydroxamic acid, with Fe(II) and Co(II) giving KM values 5fold lower than that of Zn(II). Apo-enzyme has a low residual level of activity	678192	
3.5.1.98	Ni2+	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	Zn2+	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	Zinc	enzyme active site consists of a tubular pocket, a zinc-binding site and two D-H charge-relay systems	682087	
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