EC Number   |
Metals/Ions |
Reference |
|---|
   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 |
