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Literature summary extracted from
- Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion (2006), Biochemistry, 45, 6170-6178.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.5.1.98 | expression in Escherichia coli | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.98 | suberoylanilide hydroxamic acid | - |
Homo sapiens |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.98 | 0.16 | - |
RHK(acetyl)K(acetyl)-fluorophore | presence of Co(II), 25°C. pH 8.0 | Homo sapiens | |
| 3.5.1.98 | 0.21 | - |
RHK(acetyl)K(acetyl)-fluorophore | presence of Fe(II), 25°C. pH 8.0 | Homo sapiens | |
| 3.5.1.98 | 1.1 | - |
RHK(acetyl)K(acetyl)-fluorophore | presence of Zn(II), 25°C. pH 8.0 | Homo sapiens | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 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) | Homo sapiens | |
| 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 | Homo sapiens | |
| 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 | Homo sapiens | |
| 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) | Homo sapiens | |
| 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) | Homo sapiens | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.98 | Homo sapiens | Q9BY41 | isoform HDAC8 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.5.1.98 | recombinant enzyme purified aerobically from Escherichia coli contains 8fold more iron than zinc before dialysis | Homo sapiens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.98 | acetyl-GAK(acetyl)-7-amido-4-methylcoumarin + H2O | - |
Homo sapiens | acetyl-GAK-7-amino-4-methylcoumarin + acetate | - |
? | |
| 3.5.1.98 | RHK(acetyl)K(acetyl)-fluorophore + H2O | i.e. Fluor de Lys, fluorogenic substrate | Homo sapiens | RHKK-fluorophore + acetate | - |
? | |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.98 | 0.48 | - |
RHK(acetyl)K(acetyl)-fluorophore | presence of Fe(II), 25°C. pH 8.0 | Homo sapiens | |
| 3.5.1.98 | 0.9 | - |
RHK(acetyl)K(acetyl)-fluorophore | presence of Zn(II), 25°C. pH 8.0 | Homo sapiens | |
| 3.5.1.98 | 1.2 | - |
RHK(acetyl)K(acetyl)-fluorophore | presence of Co(II), 25°C. pH 8.0 | Homo sapiens | |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.98 | 0.000044 | - |
suberoylanilide hydroxamic acid | presence of Co(II), 25°C. pH 8.0 | Homo sapiens | |
| 3.5.1.98 | 0.00013 | - |
suberoylanilide hydroxamic acid | presence of Fe(II), 25°C. pH 8.0 | Homo sapiens | |
| 3.5.1.98 | 0.00025 | - |
suberoylanilide hydroxamic acid | presence of Zn(II), 25°C. pH 8.0 | Homo sapiens | |
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