Cloned (Comment) | Organism |
---|---|
- |
Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
D176A | the mutation increases the K1/2 for potassium inhibition by more than 40fold | Homo sapiens |
H142A | the mutation increases the K1/2 for potassium inhibition by more than 40fold | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
K+ | K+ bound to monovalent cation site 1 inhibits catalytic activity of HDAC8 (11fold less active with two K+ ions bound compared to one K+ ion bound), partial inhibition at high KCl | Homo sapiens | |
suberoylanilide hydroxamic acid | - |
Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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 | Homo sapiens | |
Na+ | Na+ binds more weakly to both monovalent cation sites and activates HDAC8 to a lesser extent than K+ | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Oxidation Stability | Organism |
---|---|
Co(2+)-HDAC8 is stable in the presence of oxygen | Homo sapiens |
Purification (Comment) | Organism |
---|---|
- |
Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Fluor de Lys H4-AcK16 + H2O | - |
Homo sapiens | ? | - |
? | |
Fluor de Lys HDAC8 substrate + H2O | - |
Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
HDAC8 | - |
Homo sapiens |
histone deacetylase 8 | - |
Homo sapiens |