3.5.1.98	alpha-tubulin + H2O	splicing variant HDAC6p114 is intact in its deacetylase activity against a-tubulin	
3.5.1.98	alpha-tubulin + H2O	-	
3.5.1.98	additional information	conserved mechanism of histone deacetylase repression of some secondary metabolite gene clusters	
3.5.1.98	additional information	histone deacetylases regulate the expression of HoxA9, which acts as a master switch to regulate the expression of prototypical endothelial-committed genes such as endothelial nitric oxide synthase, VE-cadherin, VEGF-R2, and mediates the shear stress-induced maturation of endothelial cells	
3.5.1.98	additional information	isoform HDAC4 is an essential regulator of myofibroblastic differentiation	
3.5.1.98	additional information	isoforms HDAC1 and HDAC2 are associated in vivo, complex is able to deacetylate all four core histones in vitro	
3.5.1.98	additional information	acetylation of histone core proteins is regulated by HDAC, H3K9-K14 deacetylation is mediated, at least in part, by HDAC 11	
3.5.1.98	additional information	deacetylation of tubulin	
3.5.1.98	additional information	HDAC6 deacetylases tubulins, best noted substrate is beta-tubulin	
3.5.1.98	additional information	HDACs catalyse the removal of acetyl groups from e-N-acetylated lysine residues of various protein substrates	
3.5.1.98	additional information	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	additional information	histone deacetylase proteins catalyze the removal of acetyl groups from acetylated lysines on histone substrates	
3.5.1.98	additional information	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	additional information	histone deacetylases catalyze the removal of acetyl groups from histones, leading to chromatin condensation and transcriptional repression	
3.5.1.98	additional information	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	additional information	deacetylation of histone H4 by Set3C is independent of H3K4 methylation at the PFK1 locus. Set3 interacts with Hos2	
3.5.1.98	additional information	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	additional information	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	-	
3.5.1.98	N-acetyl-lysine-heat shock protein 90 + H2O	-	
3.5.1.98	N-acetyl-lysine-histone + H2O	-	
3.5.1.98	N-acetyl-lysine-histone H1 + H2O	-	
3.5.1.98	N-acetyl-lysine-histone H3 + H2O	-	
3.5.1.98	N-acetyl-lysine-histone H4 + H2O	-	
3.5.1.98	N-acetyl-lysine-MyoD + H2O	transcription factor MyoD, its activity is co-dependent on isoform HDAC1 and transcriptional co-activator P/CAF	
3.5.1.98	N-acetyl-lysine4-histone H3 + H2O	-