Pub. Date : 2006 May 16
PMID : 16681389
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion. | Metals | histone deacetylase 8 | Homo sapiens |
| 2 | Here we demonstrate that histone deacetylase 8 (HDAC8) is catalytically active with a number of divalent metal ions in a 1:1 stoichiometry with the following order of specific activity: Co(II) > Fe(II) > Zn(II) > Ni(II). | Metals | histone deacetylase 8 | Homo sapiens |
| 3 | Here we demonstrate that histone deacetylase 8 (HDAC8) is catalytically active with a number of divalent metal ions in a 1:1 stoichiometry with the following order of specific activity: Co(II) > Fe(II) > Zn(II) > Ni(II). | Metals | histone deacetylase 8 | Homo sapiens |
| 4 | The identity of the catalytic metal ion influences both the affinity of the HDAC inhibitor suberoylanilide hydroxamic acid (SAHA) and the Michaelis constant, with Fe(II)- and Co(II)-HDAC8 having K(M) values that are over 5-fold lower than that of Zn(II)-HDAC8. | Metals | histone deacetylase 8 | Homo sapiens |
| 5 | Identification of the in vivo metal ion of HDAC8 is essential for understanding the biological function and regulation of HDAC8 and for the development of improved inhibitors of this class of enzymes. | Metals | histone deacetylase 8 | Homo sapiens |
| 6 | Identification of the in vivo metal ion of HDAC8 is essential for understanding the biological function and regulation of HDAC8 and for the development of improved inhibitors of this class of enzymes. | Metals | histone deacetylase 8 | Homo sapiens |