EC Number   |
Metals/Ions |
Reference |
|---|
   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 | more |
the active site metal identity alters histone deacetylase 8 substrate selectivity. HDAC8 is activated by several divalent metal ions suggesting metal-dependent regulation of this enzyme in vivo. Fe(II)-HDAC8 catalyzes deacetylation of peptides comparable to or faster than Zn(II)-HDAC8. The residues that coordinate the active site metal ion (His180, Asp267, and Asp178) are positioned by the flexible loops. Intrinsic properties of the metal ion, including Lewis acidity and size, can influence the structure and dynamics of the loop regions and alter the binding interface presented to substrates. Altering the active site metal ion coordination is expected to propagate structural changes to the peptide binding site via the residues in the hydrophobic shell around the metal ligands |
756047 |
| 3.5.1.98 | more |
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 | Na+ |
Na+ binds more weakly to both monovalent cation sites and activates HDAC8 to a lesser extent than K+ |
712485 |
| 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 | 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 | Zn2+ |
- |
696240, 696610, 696616, 697087, 697650, 698491, 698743, 699231, 699429, 699458, 700547 |
| 3.5.1.98 | Zn2+ |
activates |
756047 |
| 3.5.1.98 | Zn2+ |
bound in the catalytic pocket |
756174 |
