3.5.1.98: histone deacetylase
This is an abbreviated version!
For detailed information about histone deacetylase, go to the full flat file.
Word Map on EC 3.5.1.98
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3.5.1.98
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hdacs
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chromatin
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deacetylases
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trichostatin
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deacetylation
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hydroxamic
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valproic
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saha
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acetyltransferase
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leukemia
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butyrate
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hyperacetylation
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methyltransferase
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vorinostat
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repressor
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lymphoma
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microtubule
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cyclin
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sirtuins
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nucleosome
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t-cells
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transactivation
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caspase
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bcl-2
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metastasis
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myeloid
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proteasome
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hypermethylation
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tumorigenesis
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cardiac
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sirt1
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neurodegenerative
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hematological
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prostate
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demethylation
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antiproliferative
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corepressors
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sirnas
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cpg
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non-histone
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5-aza-2'-deoxycytidine
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valproate
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medicine
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polycomb
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bortezomib
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dnmt3a
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heterochromatin
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creb-binding
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epigenome
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drug development
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coactivator
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relapsed
- 3.5.1.98
- hdacs
- chromatin
- deacetylases
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trichostatin
-
deacetylation
-
hydroxamic
-
valproic
- saha
- acetyltransferase
- leukemia
- butyrate
-
hyperacetylation
- methyltransferase
- vorinostat
- repressor
- lymphoma
- microtubule
- cyclin
- sirtuins
- nucleosome
- t-cells
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transactivation
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caspase
- bcl-2
- metastasis
- myeloid
- proteasome
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hypermethylation
- tumorigenesis
- cardiac
- sirt1
- neurodegenerative
- hematological
- prostate
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demethylation
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antiproliferative
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corepressors
- sirnas
- cpg
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non-histone
- 5-aza-2'-deoxycytidine
- valproate
- medicine
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polycomb
- bortezomib
- dnmt3a
- heterochromatin
-
creb-binding
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epigenome
- drug development
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coactivator
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relapsed
Reaction
hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone =
Synonyms
acetyl-lysine deacetylase, AhHDA1, AtHD1, class I acetyl-lysine deacetylase, class I HDAC, class I histone deacetylase, class II Hda1 HDAC, class II histone deacetylase, class IIa HDAC, class IIa histone deacetylase, Clr6, cytoplasmic deacetylase, deacetylase-like amidohydrolase, dRPD3, FB188 HDAH, Glyma.01 g245100, Glyma.04 g000200, Glyma.04 g187000, Glyma.04 g187100, Glyma.05 g012900, Glyma.05 g021400, Glyma.05 g040600, Glyma.05 g192600, Glyma.06 g000100, Glyma.06 g178700, Glyma.11 g000300, Glyma.11 g187800, Glyma.12 g086700, Glyma.12 g188200, Glyma.17 g078000, Glyma.17 g085700, Glyma.17 g120900, Glyma.17 g229600, GmHDA1, GmHDA10, GmHDA11, GmHDA12, GmHDA13, GmHDA14, GmHDA15, GmHDA16, GmHDA17, GmHDA18, GmHDA2, GmHDA3, GmHDA4, GmHDA5, GmHDA6, GmHDA7, GmHDA8, GmHDA9, GmHDAC, HD1B, HD2, HD8, HDA, HDA-1, HDA-2, HDA-3, HDA-4, hda1, HDA15, HDA19, HDA9, HdaA, HDAC, HDAC 11, HDAC 3, HDAC1, HDAC10, HDAC2, HDAC2-1, HDAC2-2, HDAC3, HDAC4, HDAC5, HDAC6, HDAC6p114, HDAC6p131, HDAC7, HDAC8, HDAC9, HDAH, HDLP, HDT1, HDT2, histone deacetylase, histone deacetylase 1, histone deacetylase 10, histone deacetylase 11, histone deacetylase 2, histone deacetylase 3, histone deacetylase 4, histone deacetylase 6, histone deacetylase 7, histone deacetylase 8, histone deacetylase-1, histone deacetylase-7, histone deacetylase-like amidohydrolase, histone deacetylase-like protein, histone deacetylase1, Hos2, HosB, PA3774, pfHDAC-1, RPD3, Set3 complex, Set3C, tubulin deacetylase, zinc-dependent histone deacetylase, Zn(II)-dependent deacetylase, Zn-HDAC
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3.5.1.98 histone deacetylaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.5.1.98 - histone deacetylase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
AC-Arg-Gly-Lys(AC)-4-amino-7-methylcoumarin + H2O
?
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substrate activity assay
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-
?
Ac-Leu-Gly-Lys(Ac)-7-amido-4-methylcoumarin + H2O
Ac-Leu-Gly-Lys-7-amido-4-methylcoumarin + acetate
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-
-
?
acetyl-GAK(acetyl)-7-amido-4-methylcoumarin + H2O
acetyl-GAK-7-amino-4-methylcoumarin + acetate
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-
-
?
alpha-tubulin + H2O
?
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splicing variant HDAC6p114 is intact in its deacetylase activity against a-tubulin
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-
?
benzyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Lys-7-amido-4-methylcoumarin + acetate
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-
-
-
?
benzyloxycarbonyl-L-Lys(trifluoroacetyl)-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Lys-7-amido-4-methylcoumarin + trifluoroacetate
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-
-
-
?
Boc-trifluoroacetyl-Lys-7-amido-4-methylcoumarin + H2O
Boc-trifluoroacetyl-Lys + 7-amino-4-methylcoumarin
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-
-
?
LGK(ac)FRR + H2O
LGKFRR + acetate
i.e. La-related protein 1, LARP1, best peptide substrate
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-
?
N-acetyl-arginine-histidine-acetyl-lysine-acetyl-lysine-coumarin + H2O
?
substrate in crystallized enzyme-substrate complex
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-
?
N-acetyl-lysine-heat shock protein 90 + H2O
acetate + heat shock protein 90
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-
-
-
?
N-acetyl-lysine-histone H3 + H2O
histone H3 + acetate
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deacetylation occurs at Lys9 and Lys23
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-
?
N6-lysine acetylated histone H2A + H2O
histone H2A + acetate
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substrate of isoforms HDAC1, HDAC2, HDAC. Isoform HDAC3 preferentially cleeaves lysines 5 H2A
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-
?
N6-lysine acetylated histone H4 peptide + H2O
histone H4 peptide + acetate
peptide of N-terminal 20 amino acids
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-
?
N6-lysine-acetylated histone H4 peptide + H2O
acetate + histone H4 peptide
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-
-
?
RHK(ac)K(ac)-coumarin + H2O
RHKK-coumarin + 2 acetate
i.e. HDAC8 Fluor-de-Lys or HDAC8 p53 FdL, low activity
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-
?
RHKK(ac)-coumarin + H2O
RHKK-coumarin + acetate
i.e. SIRT1 Fluor-de-Lys
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-
?
tert-butyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Lys-7-amido-4-methylcoumarin + acetate
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-
-
?
Boc-acetyl-Lys-7-amido-4-methylcoumarin + H2O
Boc-acetyl-Lys + 7-amino-4-methylcoumarin
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-
-
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?
Boc-acetyl-Lys-7-amido-4-methylcoumarin + H2O
Boc-acetyl-Lys + 7-amino-4-methylcoumarin
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-
-
-
?
Boc-acetyl-Lys-7-amido-4-methylcoumarin + H2O
Boc-acetyl-Lys + 7-amino-4-methylcoumarin
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-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
i.e. Boc-K(ac)-Fluor-de-Lys
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-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
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-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
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-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
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-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
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-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
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-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
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-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
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-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
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-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
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-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
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-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
-
-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
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-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
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-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
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-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
-
-
-
?
N-acetyl-lysine-histone H3 + H2O
acetate + histone H3
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-
-
-
?
N-acetyl-lysine-histone H3 + H2O
acetate + histone H3
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individual lysine residues in the H3 tail are deacetylated at similar rates
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?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
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-
rate of deacetylation is not uniform. H4 K5 is deacetylated first, followed by K8, K12 and K16. The specificity of deacetylation and the histone-binding preference of transcriptional co-repressors N-CoR/SMRT match each other, rate of deacetylation by isoform HDAC3 is not uniform. H4 K5 is deacetylated first, followed by K8, K12 and K16. The specificity of deacetylation and the histone-binding preference of transcriptional co-repressors N-CoR/SMRT match each other
-
?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
-
-
-
?
N-acetyl-lysine-MyoD + H2O
acetate + MyoD
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transcription factor MyoD, its activity is co-dependent on isoform HDAC1 and transcriptional co-activator P/CAF
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-
?
N6-lysine acetylated histone H2A-H2B dimer + H2O
histone H3-H4 dimer + acetate
-
-
-
?
N6-lysine acetylated histone H2A-H2B dimer + H2O
histone H3-H4 dimer + acetate
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isoform HD2, slightly preferred substrate
-
-
?
N6-lysine acetylated histone H3-H4 tetramer + H2O
histone H3-H4 tetramer + acetate
preferred substrate
-
-
?
N6-lysine acetylated histone H3-H4 tetramer + H2O
histone H3-H4 tetramer + acetate
-
isoform HD1, preferred substrate
-
-
?
N6-lysine acetylated histone H4 + H2O
histone H4 + acetate
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substrate of isoforms HDAC1, HDAC2, HDAC. HDAC3 preferentially cleeaves lysines 5 and 12 of H4. H4 tails in purified mononucleosomes are deacetylated by isoforms HDAC1 and HDAC3 only in presence of ATP
-
-
?
RHK(acetyl)K(acetyl)-fluorophore + H2O
RHKK-fluorophore + acetate
i.e. Fluor de Lys, fluorogenic substrate
-
-
?
RHK(acetyl)K(acetyl)-fluorophore + H2O
RHKK-fluorophore + acetate
i.e. Fluor de Lys, fluorogenic substrate
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-
?
RHK(acetyl)K(acetyl)-fluorophore + H2O
RHKK-fluorophore + acetate
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i.e. Fluor de Lys, fluorogenic substrate
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-
?
additional information
?
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activity assay using human histones from HeLa cells as substrate
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-
-
additional information
?
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activity assay using human histones from HeLa cells as substrate
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-
-
additional information
?
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conserved mechanism of histone deacetylase repression of some secondary metabolite gene clusters
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-
?
additional information
?
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-
deacetylation of histone H4 by Set3C is independent of H3K4 methylation at the PFK1 locus. Set3 interacts with Hos2
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-
?
additional information
?
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-
purified fungal Hos2 protein consistently deacetylates tubulins, rather than histones from trichostatin A-treated cells. Hos2 does not show any sirtuin activity, the enzyme deacetylates human nuclear histones from HeLa cells and human acetylated tubulin from Jurkat cells, overview
-
-
?
additional information
?
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-
purified fungal Hos2 protein consistently deacetylates tubulins, rather than histones from trichostatin A-treated cells. Hos2 does not show any sirtuin activity, the enzyme deacetylates human nuclear histones from HeLa cells and human acetylated tubulin from Jurkat cells, overview
-
-
?
additional information
?
-
-
Gal4-dHDAC1, consisting of the N-terminal 147 amino acid residues of the yeast Gal4 protein fused to the N terminus of full-length dHDAC1 protein, but not dHDAC1, is able to repress transcription in vitro. Transcriptional repression is blocked by the enzyme inhibitor FR901228
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-
?
additional information
?
-
-
isoform HDAC4 is an essential regulator of myofibroblastic differentiation
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-
?
additional information
?
-
-
isoforms HDAC1 and HDAC2 are associated in vivo, complex is able to deacetylate all four core histones in vitro
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-
?
additional information
?
-
isoform HDAC10 represses transcription independent of its deacetylase activity
-
-
?
additional information
?
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isoforms HDAC9 and HDAC9a both contain the histone deacetylase catalytic domain, possess histone deacetylase activity, and also repress myocyte enhancer-binding factor-2 mediated transcription
-
-
?
additional information
?
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-
isoforms HDAC9 and HDAC9a both contain the histone deacetylase catalytic domain, possess histone deacetylase activity, and also repress myocyte enhancer-binding factor-2 mediated transcription
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-
?
additional information
?
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-
HDAC6 deacetylases tubulins, best noted substrate is beta-tubulin
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-
?
additional information
?
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-
HDACs catalyse the removal of acetyl groups from e-N-acetylated lysine residues of various protein substrates
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-
?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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histone deacetylase proteins catalyze the removal of acetyl groups from acetylated lysines on histone substrates
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-
?
additional information
?
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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
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?
additional information
?
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histone deacetylases catalyze the removal of acetyl groups from histones, leading to chromatin condensation and transcriptional repression
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?
additional information
?
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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
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-
?
additional information
?
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Fluor de Lys HDAC substrate, commercially available kit
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-
?
additional information
?
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HDAC7 binds directly to beta-catenin in the cytoplasm of endothelial cells
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-
?
additional information
?
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HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
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-
additional information
?
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HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
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-
-
additional information
?
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enzyme assay using carboxyfluorescein (FAM)-labeled acetylated or trifluoroacetylated peptide substrates in vitro, and in a cell-based assay by measuring H3K9 and H4K12 acetylation changes in primary mouse neuronal culture
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-
-
additional information
?
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enzyme assay using carboxyfluorescein (FAM)-labeled acetylated or trifluoroacetylated peptide substrates in vitro, and in a cell-based assay by measuring H3K9 and H4K12 acetylation changes in primary mouse neuronal culture
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additional information
?
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enzyme assay using carboxyfluorescein (FAM)-labeled acetylated or trifluoroacetylated peptide substrates in vitro, and in a cell-based assay by measuring H3K9 and H4K12 acetylation changes in primary mouse neuronal culture
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-
-
additional information
?
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histone deacetylase 6 (HDAC6) is a multidomain cytosolic hydrolase acting mostly on non-histone protein substrates. The substrate specificity of HDAC6 is influenced by the presence of two catalytically active deacetylase domains, DD1 and DD2. Substrate specificity analysis of HDAC6 domains using acetylome peptide microarrays and peptide libraries using a peptide microarray displaying over 6800 peptides derived from known human acetylation sites, profiling of HDAC6 deacylation specificity, overview. No activity with SQSEEEK(Ac)KSEESE and SQSEVKK(Ac)PSEESE. The acetylation sites are collected from previously published data, synthesized as 13 mer derivatives with an N-terminal reactivity tag, and immobilized onto modified glass slides via a covalent bond. Residues N- and C-terminal to the central Lys(Ac) are required for efficient substrate recognition by HDAC6. The DD1 domain is unable to remove the acetyl group from the central lysine residue in the context of 13 mer peptides attached to the glass surface
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additional information
?
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histone deacetylase 6 (HDAC6) is a multidomain cytosolic hydrolase acting mostly on non-histone protein substrates. The substrate specificity of HDAC6 is influenced by the presence of two catalytically active deacetylase domains, DD1 and DD2. Substrate specificity analysis of HDAC6 domains using acetylome peptide microarrays and peptide libraries using a peptide microarray displaying over 6800 peptides derived from known human acetylation sites, profiling of HDAC6 deacylation specificity, overview. No activity with SQSEEEK(Ac)KSEESE and SQSEVKK(Ac)PSEESE. The acetylation sites are collected from previously published data, synthesized as 13 mer derivatives with an N-terminal reactivity tag, and immobilized onto modified glass slides via a covalent bond. Residues N- and C-terminal to the central Lys(Ac) are required for efficient substrate recognition by HDAC6. The DD1 domain is unable to remove the acetyl group from the central lysine residue in the context of 13 mer peptides attached to the glass surface
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additional information
?
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substrate are acetate-labeled histones from HT-29 cells
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additional information
?
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substrate are acetate-labeled histones from HT-29 cells
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additional information
?
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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, overview. Both protein structure and long-range HDAC8-substrate interactions contribute to substrate selectivity, peptide substrate evaluation
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additional information
?
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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
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-
?
additional information
?
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HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
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-
-
additional information
?
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HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
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-
-
additional information
?
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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
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-
additional information
?
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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
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-
-
additional information
?
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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
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-
-
additional information
?
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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
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-
-
additional information
?
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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
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-
-
additional information
?
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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
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-
-
additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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acetylation of histone core proteins is regulated by HDAC, H3K9-K14 deacetylation is mediated, at least in part, by HDAC 11
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?
additional information
?
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the enzyme HDA1 recognizes both the H2A-H2B dimer and H3-H4 tetramer as substrates. The ARB2 domain binds to the reconstituted yeast histone H2A-H2B dimer and H3-H4 tetramer in vitro
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additional information
?
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the enzyme HDA1 recognizes both the H2A-H2B dimer and H3-H4 tetramer as substrates. The ARB2 domain binds to the reconstituted yeast histone H2A-H2B dimer and H3-H4 tetramer in vitro
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additional information
?
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the enzyme HDA1 recognizes both the H2A-H2B dimer and H3-H4 tetramer as substrates. The ARB2 domain binds to the reconstituted yeast histone H2A-H2B dimer and H3-H4 tetramer in vitro
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