EC Number   |
Natural Substrates |
|---|
   3.5.1.98 | more |
HDACs catalyze the deacetylation of lysine residues in the N-terminal tails of core histones, in addition non-histone proteins may also serve as substrates |
| 3.5.1.98 | more |
histone deacetylase proteins catalyze the removal of acetyl groups from acetylated lysines on histone substrates |
| 3.5.1.98 | more |
histone deacetylases catalyse the removal of the N-acetyl lysine residues from the histone tails, they also deacetylate a growing number of non-histone proteins |
| 3.5.1.98 | more |
histone deacetylases catalyze the removal of acetyl groups from histones, leading to chromatin condensation and transcriptional repression |
| 3.5.1.98 | more |
the acetylation status of lysine residues in nucleosomal proteins is tightly controlled by two counteracting enzyme families, the histone acetyl transferases and the histone deacetylases, HDACs |
| 3.5.1.98 | more |
deacetylation of histone H4 by Set3C is independent of H3K4 methylation at the PFK1 locus. Set3 interacts with Hos2 |
| 3.5.1.98 | more |
catalytic reactive mechanism with catalytic Zn2+, detailed overview. Structure comparison of PA3774 with several HDACs and HDLP. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity |
| 3.5.1.98 | more |
HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors |
| 3.5.1.98 | N-acetyl-Lys16-histone H4 + H2O |
- |
| 3.5.1.98 | N-acetyl-lysine-alpha-tubulin + H2O |
- |
