EC Number   |
Metals/Ions |
Reference |
|---|
   3.5.1.98 | Co2+ |
- |
696240 |
| 3.5.1.98 | Fe2+ |
- |
696240 |
| 3.5.1.98 | Zn2+ |
- |
696240, 696610, 696616, 697087, 697650, 698491, 698743, 699231, 699429, 699458, 700547 |
| 3.5.1.98 | Co2+ |
activates |
756047 |
| 3.5.1.98 | Zn2+ |
activates |
756047 |
| 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 | Zn2+ |
bound in the catalytic pocket |
756174 |
| 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 | 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 | 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 |
