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 | 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 | 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 | 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 |