Pub. Date : 2017 Oct 24
PMID : 28937750
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Active Site Metal Identity Alters Histone Deacetylase 8 Substrate Selectivity: A Potential Novel Regulatory Mechanism. | Metals | histone deacetylase 8 | Homo sapiens |
| 2 | Previous work has shown that the efficiency of HDAC8-catalyzed deacetylation of a methylcoumarin peptide varies depending on the identity of the divalent metal ion in the HDAC8 active site. | Metals | histone deacetylase 8 | Homo sapiens |
| 3 | Previous work has shown that the efficiency of HDAC8-catalyzed deacetylation of a methylcoumarin peptide varies depending on the identity of the divalent metal ion in the HDAC8 active site. | Metals | histone deacetylase 8 | Homo sapiens |
| 4 | Here we demonstrate that both HDAC8 activity and substrate selectivity for a diverse range of peptide substrates depend on the identity of the active site metal ion. | Metals | histone deacetylase 8 | Homo sapiens |
| 5 | These data provide support for the hypothesis that HDAC8 may undergo metal switching in vivo that, in turn, may regulate its activity. | Metals | histone deacetylase 8 | Homo sapiens |
| 6 | However, future studies are needed to explore the identity of the metal ion bound to HDAC8 in cells under varied conditions. | Metals | histone deacetylase 8 | Homo sapiens |