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Information on EC 3.5.1.98 - histone deacetylase
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3.5.1.98 histone deacetylaseIUBMB Comments
A class of enzymes that remove acetyl groups from N6-acetyl-lysine residues on a histone. The reaction of this enzyme is opposite to that of EC 2.3.1.48, histone acetyltransferase. Histone deacetylases (HDACs) can be organized into three classes, HDAC1, HDAC2 and HDAC3, depending on sequence similarity and domain organization. Histone acetylation plays an important role in regulation of gene expression. In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation . May be identical to EC 3.5.1.17, acyl-lysine deacylase.
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Word Map
- 3.5.1.98
- hdacs
- chromatin
- deacetylases
-
trichostatin
-
deacetylation
-
hydroxamic
-
valproic
- saha
- acetyltransferase
- leukemia
- butyrate
-
hyperacetylation
- methyltransferase
- vorinostat
- repressor
- lymphoma
- microtubule
- cyclin
- sirtuins
- nucleosome
- t-cells
-
transactivation
-
caspase
- bcl-2
- metastasis
- myeloid
- proteasome
-
hypermethylation
- tumorigenesis
- cardiac
- sirt1
- neurodegenerative
- hematological
- prostate
-
demethylation
-
antiproliferative
-
corepressors
- sirnas
- cpg
-
non-histone
- 5-aza-2'-deoxycytidine
- valproate
- medicine
-
polycomb
- bortezomib
- dnmt3a
- heterochromatin
-
creb-binding
-
epigenome
- drug development
-
coactivator
-
relapsed
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
Synonyms
histone deacetylase, hdac1, hdac6, hdac2, hdac3, hdac4, hdac5, hdac8, hdac9, hdac7, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
class I HDAC
class I histone deacetylase
class II Hda1 HDAC
class IIa histone deacetylase
deacetylase-like amidohydrolase
FB188 HDAH
GmHDAC
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
-
hda1
HDAC
HDAC1
HDAC10
HDAC2
HDAC3
HDAC4
HDAC6
HDAC6p114
-
splicing variant of histone deacetylase 6 lacking the first 152 amino acids from N-terminus in the major isoform HDAC6p131 protein
HDAC7
HDAC8
HDAH
histone deacetylase
histone deacetylase 1
histone deacetylase 2
histone deacetylase 3
histone deacetylase 6
histone deacetylase 7
histone deacetylase 8
histone deacetylase-like amidohydrolase
Hos2
PA3774
RPD3
tubulin deacetylase
HDAC
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
-
HDAC
-
-
histone deacetylase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
deacetylation
hydrolysis
deacetylation
-
-
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SYSTEMATIC NAME
IUBMB Comments
histone amidohydrolase
A class of enzymes that remove acetyl groups from N6-acetyl-lysine residues on a histone. The reaction of this enzyme is opposite to that of EC 2.3.1.48, histone acetyltransferase. Histone deacetylases (HDACs) can be organized into three classes, HDAC1, HDAC2 and HDAC3, depending on sequence similarity and domain organization. Histone acetylation plays an important role in regulation of gene expression. In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation [4]. May be identical to EC 3.5.1.17, acyl-lysine deacylase.
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CAS REGISTRY NUMBER
COMMENTARY
9076-57-7
-
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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
?
-
substrate activity assay
-
-
?
Ac-Leu-Gly-Lys(Ac)-7-amido-4-methylcoumarin + H2O
Ac-Leu-Gly-Lys-7-amido-4-methylcoumarin + acetate
-
-
-
?
acetyl-GAK(acetyl)-7-amido-4-methylcoumarin + H2O
acetyl-GAK-7-amino-4-methylcoumarin + acetate
-
-
-
?
alpha-tubulin + H2O
?
-
splicing variant HDAC6p114 is intact in its deacetylase activity against a-tubulin
-
-
?
benzyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Lys-7-amido-4-methylcoumarin + acetate
-
-
-
-
?
benzyloxycarbonyl-L-Lys(trifluoroacetyl)-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Lys-7-amido-4-methylcoumarin + trifluoroacetate
-
-
-
-
?
Boc-trifluoroacetyl-Lys-7-amido-4-methylcoumarin + H2O
Boc-trifluoroacetyl-Lys + 7-amino-4-methylcoumarin
-
-
-
?
LGK(ac)FRR + H2O
LGKFRR + acetate
i.e. La-related protein 1, LARP1, best peptide substrate
-
-
?
N-acetyl-arginine-histidine-acetyl-lysine-acetyl-lysine-coumarin + H2O
?
substrate in crystallized enzyme-substrate complex
-
-
?
N-acetyl-lysine-heat shock protein 90 + H2O
acetate + heat shock protein 90
-
-
-
-
?
N-acetyl-lysine-histone H3 + H2O
histone H3 + acetate
-
deacetylation occurs at Lys9 and Lys23
-
-
?
N6-lysine acetylated histone H2A + H2O
histone H2A + acetate
-
substrate of isoforms HDAC1, HDAC2, HDAC. Isoform HDAC3 preferentially cleeaves lysines 5 H2A
-
-
?
N6-lysine acetylated histone H4 peptide + H2O
histone H4 peptide + acetate
peptide of N-terminal 20 amino acids
-
-
?
N6-lysine-acetylated histone H4 peptide + H2O
acetate + histone H4 peptide
-
-
-
?
RHK(ac)K(ac)-coumarin + H2O
RHKK-coumarin + 2 acetate
i.e. HDAC8 Fluor-de-Lys or HDAC8 p53 FdL, low activity
-
-
?
RHKK(ac)-coumarin + H2O
RHKK-coumarin + acetate
i.e. SIRT1 Fluor-de-Lys
-
-
?
tert-butyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Lys-7-amido-4-methylcoumarin + acetate
-
-
-
?
Boc-acetyl-Lys-7-amido-4-methylcoumarin + H2O
Boc-acetyl-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-acetyl-Lys-7-amido-4-methylcoumarin + H2O
Boc-acetyl-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-acetyl-Lys-7-amido-4-methylcoumarin + H2O
Boc-acetyl-Lys + 7-amino-4-methylcoumarin
-
-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
i.e. Boc-K(ac)-Fluor-de-Lys
-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
-
-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
-
-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
-
-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
-
-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
-
-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
-
-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
-
-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
-
-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
-
-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
-
-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
-
-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
-
-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
-
-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
-
-
-
?
Boc-Lys(TFA)-coumarin + H2O
Boc-Lys-coumarin + trifluoroacetate
-
-
-
?
N-acetyl-lysine-histone H3 + H2O
acetate + histone H3
-
-
-
-
?
N-acetyl-lysine-histone H3 + H2O
acetate + histone H3
-
-
individual lysine residues in the H3 tail are deacetylated at similar rates
-
?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
-
-
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
-
transcription factor MyoD, its activity is co-dependent on isoform HDAC1 and transcriptional co-activator P/CAF
-
-
?
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
-
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
-
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
-
-
?
RHK(acetyl)K(acetyl)-fluorophore + H2O
RHKK-fluorophore + acetate
-
i.e. Fluor de Lys, fluorogenic substrate
-
-
?
additional information
?
-
activity assay using human histones from HeLa cells as substrate
-
-
-
additional information
?
-
-
activity assay using human histones from HeLa cells as substrate
-
-
-
additional information
?
-
-
conserved mechanism of histone deacetylase repression of some secondary metabolite gene clusters
-
-
?
additional information
?
-
-
deacetylation of histone H4 by Set3C is independent of H3K4 methylation at the PFK1 locus. Set3 interacts with Hos2
-
-
?
additional information
?
-
-
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
?
-
-
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
-
-
?
additional information
?
-
-
isoform HDAC4 is an essential regulator of myofibroblastic differentiation
-
-
?
additional information
?
-
-
isoforms HDAC1 and HDAC2 are associated in vivo, complex is able to deacetylate all four core histones in vitro
-
-
?
additional information
?
-
isoform HDAC10 represses transcription independent of its deacetylase activity
-
-
?
additional information
?
-
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
?
-
-
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
?
-
-
HDAC6 deacetylases tubulins, best noted substrate is beta-tubulin
-
-
?
additional information
?
-
-
HDACs catalyse the removal of acetyl groups from e-N-acetylated lysine residues of various protein substrates
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
histone deacetylase proteins catalyze the removal of acetyl groups from acetylated lysines on histone substrates
-
-
?
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
-
-
?
additional information
?
-
histone deacetylases catalyze the removal of acetyl groups from histones, leading to chromatin condensation and transcriptional repression
-
-
?
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
-
-
?
additional information
?
-
Fluor de Lys HDAC substrate, commercially available kit
-
-
?
additional information
?
-
-
HDAC7 binds directly to beta-catenin in the cytoplasm of endothelial cells
-
-
?
additional information
?
-
HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
-
-
-
additional information
?
-
-
HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
substrate are acetate-labeled histones from HT-29 cells
-
-
-
additional information
?
-
-
substrate are acetate-labeled histones from HT-29 cells
-
-
-
additional information
?
-
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
-
-
-
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
-
-
?
additional information
?
-
HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
-
-
-
additional information
?
-
HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
acetylation of histone core proteins is regulated by HDAC, H3K9-K14 deacetylation is mediated, at least in part, by HDAC 11
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
alpha-tubulin + H2O
?
-
splicing variant HDAC6p114 is intact in its deacetylase activity against a-tubulin
-
-
?
N-acetyl-lysine-heat shock protein 90 + H2O
acetate + heat shock protein 90
-
-
-
-
?
N-acetyl-lysine-MyoD + H2O
acetate + MyoD
-
transcription factor MyoD, its activity is co-dependent on isoform HDAC1 and transcriptional co-activator P/CAF
-
-
?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
-
-
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
-
?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
-
-
-
?
additional information
?
-
-
conserved mechanism of histone deacetylase repression of some secondary metabolite gene clusters
-
-
?
additional information
?
-
-
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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isoform HDAC4 is an essential regulator of myofibroblastic differentiation
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additional information
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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
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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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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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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
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required for deacetylation of histone H4 in purified nucleosomes by isoforms HDAC1 and HDAC3. ATP also enhances cleavage of free, non-nucleosomal histones by HDAC1 and HDAC3
additional information
-
deacetylation by isoform dHDAC1 does not require any additional cofactors
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
K+
Mg2+
Na+
-
Na+ binds more weakly to both monovalent cation sites and activates HDAC8 to a lesser extent than K+
Ni2+
ratio of kcat to KM value in presence of metal ion in decreasing order: Co(II), Fe(II), Zn(II), Ni(II)
Zinc
-
enzyme active site consists of a tubular pocket, a zinc-binding site and two D-H charge-relay systems
Zn2+
additional information
Co2+
ratio of kcat to KM value in presence of metal ion in decreasing order: Co(II), Fe(II), Zn(II), Ni(II)
Fe2+
ratio of kcat to KM value in presence of metal ion in decreasing order: Co(II), Fe(II), Zn(II), Ni(II). Fe(II) bound to enzyme is readily oxidized to Fe(III) upon exposure to oxygen
Fe2+
isozyme HDAC8 has higher activity with a bound Fe(II) than Zn(II), although Fe(II)-HDAC8 rapidly loses activity under aerobic conditions
Fe2+
activates, Fe(II)-HDAC8 is sensitive to oxidation and is not activated by Fe(III)
K+
presence of two potassium ions in the structure of isoform HDAC8, one of which interacts with the key catalytic residues. Direct role of potassium in fold stabilization
K+
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K+ bound to monovalent cation site 2 enhances catalytic activity of HDAC8 45fold with maximal deacetylase activity observed at 10 mM KCl. K+ is the predominant monovalent cation bound to HDAC8 in vivo, K+ binding to site 1 enhances the affinity of HDAC8 for suberoylanilide hydroxamic acid
Zn2+
ratio of kcat to KM value in presence of metal ion in decreasing order: Co(II), Fe(II), Zn(II), Ni(II)
Zn2+
Zn(II)-dependent deacetylase, but isozyme HDAC8 has higher activity with a bound Fe(II) than Zn(II), although Fe(II)-HDAC8 rapidly loses activity under aerobic conditions
additional information
the identity of the catalytic metal ion influences both the Michaelis-Menten constant and the affinity of inhibitor suberoylanilide hydroxamic acid, with Fe(II) and Co(II) giving KM values 5fold lower than that of Zn(II). Apo-enzyme has a low residual level of activity
additional information
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the identity of the catalytic metal ion influences both the Michaelis-Menten constant and the affinity of inhibitor suberoylanilide hydroxamic acid, with Fe(II) and Co(II) giving KM values 5fold lower than that of Zn(II). Apo-enzyme has a low residual level of activity
additional information
the active site metal identity alters histone deacetylase 8 substrate selectivity. HDAC8 is activated by several divalent metal ions suggesting metal-dependent regulation of this enzyme in vivo. Fe(II)-HDAC8 catalyzes deacetylation of peptides comparable to or faster than Zn(II)-HDAC8. The residues that coordinate the active site metal ion (His180, Asp267, and Asp178) are positioned by the flexible loops. Intrinsic properties of the metal ion, including Lewis acidity and size, can influence the structure and dynamics of the loop regions and alter the binding interface presented to substrates. Altering the active site metal ion coordination is expected to propagate structural changes to the peptide binding site via the residues in the hydrophobic shell around the metal ligands
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,5S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-6-oxabicyclo[3.1.1]heptane-3-carboxamide
i.e. BRD7232, inhibition kinetics; i.e. BRD7232, possesses kinetic selectivity for isozyme HDAC1 versus HDAC2, inhibition kinetics; inhibition kinetics
(2E)-3-[1,2-bis(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[1-benzyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[1-benzyl-2-(2-phenylethyl)-1H-benzimidazol-6-yl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[1-ethyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[1-[2-(diethylamino)ethyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[1-[3-(dimethylamino)-2,2-dimethylpropyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[1-[3-(dimethylamino)propyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[1-[4-(dimethylamino)butyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[2-cyclohexyl-1-(3-hydroxypropyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[2-[(benzyloxy)methyl]-1-(3-hydroxypropyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[4-([[2-(3a,7a-dihydro-1H-indol-3-yl)ethyl](2-hydroxyethyl)amino]methyl)phenyl]-N-hydroxyprop-2-enamide
-
(2E)-N-(2-aminophenyl)-3-(4-{1-[(2-hydroxyethyl)amino]-2-oxo-2-[4-(trifluoromethyl)anilino]ethyl}phenyl)prop-2-enamide
(2E)-N-(2-aminophenyl)-3-(4-{1-[(3S)-3-(dimethylamino)pyrrolidin-1-yl]-2-oxo-2-[4-(trifluoromethyl)anilino]ethyl}phenyl)prop-2-enamide
(2E)-N-(2-aminophenyl)-3-[2-(2-phenylethyl)-1-(pyridin-2-ylmethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-(2-aminophenyl)-3-[4-(1-{[2-(morpholin-4-yl)ethyl]amino}-2-oxo-2-[4-(trifluoromethyl)anilino]ethyl)phenyl]prop-2-enamide
(2E)-N-(2-aminophenyl)-3-{4-[2-(4-bromoanilino)-1-(3-hydroxypyrrolidin-1-yl)-2-oxoethyl]phenyl}prop-2-enamide
(2E)-N-hydroxy-3-[1-(2-morpholin-4-ylethyl)-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(1-methylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-methylpropyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-phenylpropyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-octyl-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-thiophen-3-yl-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[1-(3-methoxypropyl)-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[1-(3-morpholin-4-ylpropyl)-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[1-methyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[1-[3-(1H-imidazol-1-yl)propyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[1-[3-(2-oxopyrrolidin-1-yl)propyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(2-piperidin-1-ylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(2-pyrrolidin-1-ylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(3,4,5-trimethoxybenzyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(3-pyrrolidin-1-ylpropyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(pyridin-2-ylmethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-propyl-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-[2-[(4-methoxyphenyl)sulfonyl]-2,3-dihydro-1H-isoindol-5-yl]prop-2-enamide
-
anti-proliferative activity in human HCT116 cell line, IC50 0.93 microM
(2E)-N-hydroxy-3-[2-[2-(1H-indol-3-yl)ethyl]-2,3-dihydro-1H-isoindol-5-yl]prop-2-enamide
-
anti-proliferative activity in human HCT116 cell line, IC50 0.22 microM
(2E)-N-hydroxy-3-[2-[2-(2-methyl-1H-indol-3-yl)ethyl]-2,3-dihydro-1H-isoindol-5-yl]prop-2-enamide
-
anti-proliferative activity in human HCT116 cell line, IC50 0.1042microM. Compound has a reasonable combination of potency, solubility and human microsomal stability to justify further investigation
(2E)-N-hydroxy-3-[2-[2-(pyrazolo[1,5-a]pyridin-3-yl)ethyl]-2,3-dihydro-1H-isoindol-5-yl]prop-2-enamide
-
anti-proliferative activity in human HCT116 cell line, IC50 0.53 microM. Compound has a reasonable combination of potency, solubility and human microsomal stability to justify further investigation
(2R)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
-
(2S)-2-(acetylamino)-3-[3-[(2S)-2-[[(2S)-2-ammonio-7-(hydroxyamino)-7-oxoheptanoyl]amino]-3-methoxy-3-oxopropyl]phenyl]propanoate
-
-
(2S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]-2-fluorophenyl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-benzyl-N-(4-chlorophenyl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(3-methylphenyl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(4-methylphenyl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(6-methylpyridin-3-yl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(piperidin-1-yl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(propan-2-yl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(pyridin-2-yl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(pyridin-3-yl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(pyridin-4-yl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-phenylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-[4-(propan-2-yl)phenyl]pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-[4-(trifluoromethyl)phenyl]pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(2,4-difluorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(2-chloro-4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(2-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3,4-dichlorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3,4-difluorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-bromo-4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-chloro-4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-methoxyphenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-bromophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chloro-3-methylphenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2,2,2-trifluoroethyl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2,2-difluoroethyl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2,2-dimethylpropyl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2-fluoroethyl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2-hydroxy-2-methylpropyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2-hydroxyethyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2-methoxyethyl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(3-hydroxy-2,2-dimethylpropyl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(cyanomethyl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(oxan-4-yl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(propan-2-yl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(pyrimidin-2-yl)pyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-cyclobutylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-ethylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-cyanophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-cyclopropylphenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-fluoro-3-methylphenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-methoxyphenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(5-chloropyridin-2-yl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-cyclopentyl-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-cyclopropyl-1-methylpyrrolidine-3-carboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N~3~-(4-chlorophenyl)-N~1~,N~1~-diethylpyrrolidine-1,3-dicarboxamide
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N~3~-(4-chlorophenyl)-N~1~-ethylpyrrolidine-1,3-dicarboxamide
(3R)-4-{5-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyrazin-2-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{5-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyridin-2-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{6-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyridazin-3-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R)-4-{6-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyridin-3-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
(3R,4S)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
(3S)-3-{[(3S)-3-{[(benzyloxy)carbonyl]amino}-3-cyclopropylpropanoyl]amino}-2-oxo-5-phenylpentyl acetate
-
-
(3S,15R,20aS)-15-methyl-3-[(1E)-4-sulfanylbut-1-en-1-yl]-3,4,6,7,14,15,18,19,20,20a-decahydro-1H,5H,16H-11,8:15,12-di(azeno)pyrrolo[2,1-c][1,8,12,4,15]oxadithiadiazacyclooctadecine-1,5,16-trione
-
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
-
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
-
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
-
-
(4E)-N-(2-aminophenyl)-5-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]pent-4-enamide
-
(4Z)-6-[(5R,8S,11R)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]hex-4-enoic acid
-
(5E)-N-(2-aminophenyl)-6-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]hex-5-enamide
-
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
-
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3-thia-7,14,20,21-tetraazatricyclo[14.3.1.1-2,5]henicosa-1(20),2(21),16,18-tetraene-6,9,13-trione
-
(5R,8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
-
(5S,8R,11R)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
-
(5S,8S,11S,5'S,8'S,11'S)-11,11'-[disulfanediyldi(1E)but-1-ene-4,1-diyl]bis[5-methyl-8-(1-methylethyl)-3,10,17-trioxa-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione]
-
(8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),4,16(19)-tetraene-6,9,13-trione
-
(E)-3-(2-(((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)pyrimidin-5-yl)-N-hydroxyacrylamide
55% inhibition at 100 nM; 65% inhibition at 100 nM
(E)-3-[3-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]phenyl]-N-hydroxyacrylamide
-
inhibitor for both EGFR/HER2 kinase and HDAC with potent cellular activity, i.e. target inhibition and cytotoxicity
(E)-N-hydroxy-3-(2-(methyl((3-(1-(4-methylbenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)amino)pyrimidin-5-yl)acrylamide
60% inhibition at 100 nM; 61% inhibition at 100 nM
(E)-N1-hydroxy-N5-(5-styryl-1,3,4-thiadiazol-2-yl)glutaramide
-
antiproliferative activities against MDA-MB-231 and K562 cell lines, IC50 0.0059 and 0.00675 microM, respectively
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-(4-methoxyphenyl)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-(naphthalen-1-yl)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-m-tolyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-o-tolyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-p-tolyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-pentyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-phenethyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-phenyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide hydrochloride
-
(S)-benzyl 3-(biphenyl-4-ylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-benzyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenethylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-benzyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-N-(2,4-dimethylphenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-N-(3-chloro-4-fluorophenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-N-(3-chlorophenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-N-(4-fluorophenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-N-(biphenyl-4-yl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-N-benzyl-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide hydrochloride
-
(S)-N-hexyl-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-N-tert -butyl-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
(S)-tert-butyl 3-(2,4-dimethylphenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 3-(3-chloro-4-fluorophenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 3-(3-chlorophenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 3-(4-fluorophenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 3-(benzylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 3-(biphenyl-4-ylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 3-(hexylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 3-(tert-butylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(4-methoxyphenylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(mtolylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(naphthalen-1-ylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(o-tolylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(p-tolylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(pentylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenethylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
1-methyl-N-[(1S)-7-oxo-1-[(4-phenyl-1,3-thiazol-2-yl)carbamoyl]octyl]piperidine-2-carboxamide
-
-
1-[5-(2,3-dihydro-1,4-benzodioxin-6-yl)thiophen-2-yl]-2,2,2-trifluoroethanone
-
-
15-deoxy-DELTA12,14-prostaglandin J2-biotin
-
maximal inhibition of recombinant HDAC3 in complex with CoR1 is 50%
2,2,2-trifluoro-1-(5-[3-[(methylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
potent inhibitor of HDAC4 and shows more than 100fold selectivity overHDAC1
2,2,2-trifluoro-1-(5-[3-[(propylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
-
2,2,2-trifluoro-1-(5-[3-[(thiophen-2-ylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
-
2,2,2-trifluoro-1-[5-(3-methyl-1,2,4-oxadiazol-5-yl)thiophen-2-yl]ethanone
-
HDAC4-selective inhibitor
2,2,2-trifluoro-1-[5-(3-[[(4-fluorobenzyl)sulfonyl]methyl]-1,2,4-oxadiazol-5-yl)thiophen-2-yl]ethanone
-
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid (3,4-dimethylphenyl)-amide hydroxyamide
-
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid biphenyl-2-ylamide hydroxyamide
-
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide (4-phenylthiazol-2-yl)amide
-
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenyl-amide
-
competitive. Significant but rather unselective inhibition of cellular HDACs
2-(((3-(1-(2,4-difluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
66% inhibition at 100 nM; 88% inhibition at 100 nM
2-(((3-(1-(2-chloro-4-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
49% inhibition at 100 nM; 73% inhibition at 100 nM
2-(((3-(1-(2-chlorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
55% inhibition at 100 nM; 93% inhibition at 100 nM
2-(((3-(1-(2-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
44% inhibition at 100 nM; 84% inhibition at 100 nM
2-(((3-(1-(4-cyanobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
38% inhibition at 100 nM; 68% inhibition at 100 nM
2-(((3-(1-(4-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
65% inhibition at 100 nM; 92% inhibition at 100 nM
2-(((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
63% inhibition at 100 nM; 96% inhibition at 100 nM
2-(3,6-dihydroxy-9H-xanthen-9-yl)-5-(8-(hydroxyamino)-8-oxooctanamido)benzoic acid
synthesis, overview
2-(3,6-dihydroxy-9H-xanthen-9-yl)-5-(8-methoxy-8-oxooctanamido)benzoic acid
synthesis, overview
2-(4-((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacetamide
18% inhibition at 100 nM; 35% inhibition at 100 nM
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide
-
-
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
-
-
3-(4-((3-(1-(2,4-difluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
35% inhibition at 100 nM; 74% inhibition at 100 nM
3-(4-((3-(1-(2-chlorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
59% inhibition at 100 nM; 8% inhibition at 100 nM
3-(4-((3-(1-(2-cyanobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
36% inhibition at 100 nM; 65% inhibition at 100 nM
3-(4-((3-(1-(2-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
31% inhibition at 100 nM; 68% inhibition at 100 nM
3-(4-((3-(1-(3,4-difluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
17% inhibition at 100 nM; 60% inhibition at 100 nM
3-(4-((3-(1-(3-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
35% inhibition at 100 nM; 73% inhibition at 100 nM
3-(4-((3-(1-(4-bromobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
58% inhibition at 100 nM; 6% inhibition at 100 nM
3-(4-((3-(1-(4-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
38% inhibition at 100 nM; 75% inhibition at 100 nM
3-(4-((3-(1-allylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
34% inhibition at 100 nM; 66% inhibition at 100 nM
3-(4-((3-(1-allylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxypropanamide
15% inhibition at 100 nM; 4% inhibition at 100 nM
3-(4-((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N- hydroxypropanamide
11% inhibition at 100 nM; 22% inhibition at 100 nM
3-(4-((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
35% inhibition at 100 nM; 71% inhibition at 100 nM
3-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
-
the inhibitor shows 40fold selectivity for HDAC4 and 180fold for HDAC6 against HDAC1
3-[5-[(1E)-3-(hydroxyamino)-3-oxoprop-1-en-1-yl]-2-(2-phenylethyl)-1H-benzimidazol-1-yl]propanoic acid
-
-
3-[5-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]furan-2-yl]-N-hydroxy-acrylamide
-
inhibitor for both EGFR/HER2 kinase and HDAC with potent cellular activity, i.e. target inhibition and cytotoxicity
4-((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)-N-hydroxybenzamide
29% inhibition at 100 nM; 66% inhibition at 100 nM
4-hydroxy-2-nonenal
-
maximal inhibition of recombinant HDAC3 in complex with CoR1 is 70%
4-[[(2E)-2-(2-chlorobenzylidene)hydrazinyl]carbonothioyl]-N-hydroxypiperazine-1-carboxamide
-
4-[[(2E)-2-(4-chlorobenzylidene)hydrazinyl]carbonothioyl]-N-hydroxypiperazine-1-carboxamide
inactivates HDAC8 preferentially over HDAC1
4-[[(2E)-2-(anthracen-9-ylmethylidene)hydrazinyl]carbonothioyl]-N-hydroxypiperazine-1-carboxamide
-
6-[(2E)-2-[(2-bromo-4-hydroxy-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
-
6-[(2E)-2-[(2-bromo-4-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
-
6-[(2E)-2-[(2-bromo-5-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
-
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
-
-
6-[(biphenyl-4-ylmethyl)[4-[(4-bromobenzyl)oxy]benzyl]amino]-N-hydroxyhexanamide
-
-
6-[[4-[(4-bromobenzyl)oxy]benzyl](9H-fluoren-3-ylmethyl)amino]-N-hydroxyhexanamide
-
-
7-mercapto-N-phenylheptanamide
thiol formed by enzymatic hydrolysis in the cell reacts with the zinc ion in the active site of histone deacetylase. Molecular modeling of complex with histone HDAC8
7-[(2E)-2-[(2-bromo-4-hydroxy-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
-
7-[(2E)-2-[(2-bromo-5-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
-
7-[(2E)-2-[(2-bromo-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
-
7-[(2E)-2-[(2-bromophenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
-
7-[(2E)-2-[(2-bromopyridin-3-yl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
-
7-[(2E)-2-[(2-chlorophenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
-
7-[(2E)-2-[(6-bromo-1,3-benzodioxol-5-yl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
-
7-[(2E)-2-[[4-(dimethylamino)-2-hydroxyphenyl]methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
-
8-[(2E)-2-[(2,5-dihydroxyphenyl)methylidene]hydrazino]-N-hydroxy-8-oxooctanamide
-
acetylated histone deacetylase 1
-
the activity of HDAC2 is inhibited by acetylated HDAC1
-
allyl mercaptan
garlic organosulfur compounds can be metabolized to allyl mercaptan
alpha-keto-gamma-methylselenobutyrate
causes dose-dependent inhibition of HDAC activity, HDAC1 shows about 80% residual activity at 2 mM, HDAC8 shows less than 60% residual activity at 2 mM
beta-methylselenopyruvate
causes dose-dependent inhibition of HDAC activity, competitive inhibitor of HDAC8, HDAC1 shows about 30% residual activity at 2 mM, HDAC8 shows less than 30% residual activity at 2 mM
chlorogenic acid
highly potent HDAC inhibitor, 40% residual activity at 0.5 mM
cyclo (N-O-methyl-L-tryptophanyl-L-isoleucinyl-D-pipecolinyl-L-2-amino-8-oxodecanoyl)
-
i.e. apicidin, a cyclic tetrapeptide having broad-spectrum antiparasitic activity, inhibits the enzyme activity as well as the in vitro growth of Babesia parasites with an IC50 of 3.8 ng/ml
EDTA
-
1 mM, 30 min, complete loss of activity. Zn2+, Mg2+, Mn2+ may restore activity
FOXP
-
FOXP3 specifically inhibits binding of histone deacetylase 2 and 4 to the site and increases local histone H3 acetylation
-
FR901228
-
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
K+
-
K+ bound to monovalent cation site 1 inhibits catalytic activity of HDAC8 (11fold less active with two K+ ions bound compared to one K+ ion bound), partial inhibition at high KCl
MC1568
specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs
MC1575
specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs
MCP30
30 kDa protein isolated from bitter melon seeds, Momordica charantia, contains two highly related type I ribosome-inactivating proteins, alpha- and beta-momorcharin
-
methyl (3R,6R,9R)-9-(acetylamino)-6-[6-(hydroxyamino)-6-oxohexyl]-5,8-dioxo-4,7-diazabicyclo[9.3.1]pentadeca-1(15),11,13-triene-3-carboxylate
-
tight binding competitive inhibition
methyl N-[(2S)-2-[(N-acetyl-L-alanyl)amino]-7-(hydroxyamino)-7-oxoheptanoyl]-L-phenylalaninate
-
-
MGCD 290
-
an enzyme Hos2 inhibitor, for use in combination with azoles, such as fluconazole, for fungal infections
-
N-(2-aminophenyl)-4-[[(4-biphenyl-4-yl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]methyl]benzamide
-
-
N-(2-aminophenyl)-4-[[(6-oxo-4-phenyl-1,6-dihydropyrimidin-2-yl)sulfanyl]methyl]benzamide
-
-
N-(2-aminophenyl)-5-[(4-biphenyl-4-yl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]pentanamide
-
-
N-(2-aminophenyl)-5-[(6-oxo-4-phenyl-1,6-dihydropyrimidin-2-yl)sulfanyl]pentanamide
-
-
N-(2-aminophenyl)-6-(4-biphenyl-4-yl-6-oxo-1,6-dihydropyrimidin-2-yl)hexanamide
-
-
N-(2-aminopyridin-3-yl)-5-[(6-oxo-4-phenyl-1,6-dihydropyrimidin-2-yl)sulfanyl]pentanamide
-
-
N-(2-hydroxyphenyl)-5-[(6-oxo-4-phenyl-1,6-dihydropyrimidin-2-yl)sulfanyl]pentanamide
-
-
N-(4-amino-3'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
-
N-(4-amino-4'-chloro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
-
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-1H-2-benzopyran-3-carboxamide
-
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-2H-1-benzopyran-3-carboxamide
-
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3-oxabicyclo[3.1.0]hexane-6-carboxamide
-
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-3-carboxamide
-
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
i.e. BRD4884, coordinates to the Zn2+ ion via the free aniline -NH2, completing its tetrahedral coordination sphere in addition to the side chains of Asp181, His183, and Asp269 with the anilide carbonyl oxygen situated at a distance of 2.8 A to the Zn2+ ion. The anilide-NH of BRD4884 forms an H-bond to the backbone carbonyl oxygen of Gly154. The 11 A lipophilic channel harbors the tetrahydropyran moiety of BRD4884 making Van Der Waals contacts with the channel wall. The tetrahydropyran ring adopts a preferential chair conformation allowing the pyran oxygen atom to form a hydrogen bond (3.5 A) with a conserved water at the surface of HDAC2, inhibition kinetics; i.e. BRD4884, possesses kinetic selectivity for isozyme HDAC1 versus HDAC2, inhibition kinetics; inhibition kinetics
N-(4-aminopyrimidin-5-yl)-5-[(6-oxo-4-phenyl-1,6-dihydropyrimidin-2-yl)sulfanyl]pentanamide
-
-
N-(8-aminonaphthalen-1-yl)-5-[(4-biphenyl-4-yl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]pentanamide
-
-
N-(8-aminonaphthalen-1-yl)-5-[(6-oxo-4-phenyl-1,6-dihydropyrimidin-2-yl)sulfanyl]pentanamide
-
-
N-(8-aminonaphthalen-1-yl)-6-(4-biphenyl-4-yl-6-oxo-1,6-dihydropyrimidin-2-yl)hexanamide
-
-
N-(8-aminonaphthalen-1-yl)-6-(6-oxo-4-phenyl-1,6-dihydropyrimidin-2-yl)hexanamide
-
-
N-hydroxy-1-(3-hydroxypropyl)-2-(2-phenylethyl)-1H-benzimidazole-5-carboxamide
-
-
N-hydroxy-2-(methyl((3-(1-(3-methylbenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)amino)pyrimidine-5-carboxamide
54% inhibition at 100 nM; 93% inhibition at 100 nM
N-hydroxy-2-(methyl((3-(1-(4-(trifluoromethyl)benzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)amino)pyrimidine-5-carboxamide
30% inhibition at 100 nM; 62% inhibition at 100 nM
N-hydroxy-2-(methyl((3-(1-(4-methylbenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)amino)pyrimidine-5-carboxamide
71% inhibition at 100 nM; 96% inhibition at 100 nM
N-hydroxy-2-[1-methyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]cyclopropanecarboxamide
-
-
N-hydroxy-3-(4-((3-(1-(2-methylbenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)acrylamide
14% inhibition at 100 nM; 68% inhibition at 100 nM
N-hydroxy-3-(4-((3-(1-(2-nitrobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)acrylamide
19% inhibition at 100 nM; 63% inhibition at 100 nM
N-hydroxy-3-(4-((3-(1-(3-methylbenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)acrylamide
25% inhibition at 100 nM; 73% inhibition at 100 nM
N-hydroxy-3-(4-((3-(1-(4-methoxybenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)acrylamide
36% inhibition at 100 nM; 75% inhibition at 100 nM
N-hydroxy-3-(4-((3-(1-(4-methylbenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)acrylamide
32% inhibition at 100 nM; 76% inhibition at 100 nM
N-hydroxy-3-(4-((3-(1-(4-methylbenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)propanamide
12% inhibition at 100 nM; 28% inhibition at 100 nM
N-hydroxy-3-(4-((3-(1-propylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)acrylamide
40% inhibition at 100 nM; 69% inhibition at 100 nM
N-hydroxy-3-(4-((3-(1-propylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)propanamide
13% inhibition at 100 nM; 5% inhibition at 100 nM
N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-methylpropyl)-1H-benzimidazol-5-yl]propanamide
-
-
N-hydroxy-3-[2-(2-phenylethyl)-1-(3,4,5-trimethoxybenzyl)-1H-benzimidazol-5-yl]propanamide
-
-
N-hydroxy-3-[2-[(2-methyl-1H-indol-3-yl)acetyl]-2,3-dihydro-1H-isoindol-5-yl]propanamide
-
anti-proliferative activity in human HCT116 cell line, IC50 0.19 microM
N-hydroxy-4-[[(2E)-2-(2-hydroxybenzylidene)hydrazinyl]carbonothioyl]piperazine-1-carboxamide
inactivates HDAC8 preferentially over HDAC1
N-hydroxy-4-[[(2E)-2-(4-methylbenzylidene)hydrazinyl]carbonothioyl]piperazine-1-carboxamide
-
N-hydroxy-4-[[(2Z)-2-(2-oxo-1,2-dihydro-3H-indol-3-ylidene)hydrazinyl]carbonothioyl]piperazine-1-carboxamide
-
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
-
-
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
-
-
N-hydroxy-7-[(2E)-2-[(2-hydroxynaphthalen-1-yl)methylidene]hydrazino]-7-oxoheptanamide
-
N-hydroxy-7-[(2E)-2-[(3-hydroxyphenyl)methylidene]hydrazino]-7-oxoheptanamide
-
N-hydroxy-7-[(2E)-2-[[4-(1H-imidazol-1-yl)phenyl]methylidene]hydrazino]-7-oxoheptanamide
-
N-hydroxy-8-oxo-8-[(2E)-2-[(2,4,6-trihydroxyphenyl)methylidene]hydrazino]octanamide
-
N-methyl-N-(quinoxalin-6-ylmethyl)-5-(trifluoroacetyl)thiophene-2-carboxamide
-
-
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
-
-
N-[(2E)-3-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]prop-2-en-1-yl]-2-sulfanylacetamide
-
N-[(3E)-4-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]but-3-en-1-yl]-2-sulfanylacetamide
-
N-[1,1,2,2,3,3,4,4,5,5,6,6-dodecafluoro-7-(hydroxyamino)-7-oxoheptyl]benzamide
a highly selective hydroxamate inhibitor
N-[4-amino-4'-(trifluoromethyl)[1,1'-biphenyl]-3-yl]oxane-4-carboxamide
-
N1-(5-benzyl-1,3,4-thiadiazol-2-yl)-N7-hydroxyheptanediamide
-
antiproliferative activities against MDA-MB-231 and K562 cell lines, IC50 0.0061 and 0.0122 microM, respectively
N1-(5-benzyl-1,3,4-thiadiazol-2-yl)-N8-hydroxyoctanediamide
-
antiproliferative activities against MDA-MB-231 and K562 cell lines, IC50 0.00298 and 0.0091 microM, respectively
N1-hydroxy-N7-(5-phenyl-1,3,4-thiadiazol-2-yl)heptanediamide
-
antiproliferative activities against MDA-MB-231 and K562 cell lines, IC50 0.0055 and 0.0129 microM, respectively
NaCl
inhibitory in sodium phosphate/citric acid buffer, 50% inhibition at 100 mM
peroxynitrite
activity of wild-type enzyme is reduced to 38% in presence of peroxynitrite. Activities of mutants Y153A and Y253A are 233 completely abolished in the presence of peroxynitrite. Mutant Y146A shows 32% reduction in activity
pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
i.e. MS27-275
S-nitrosocysteine
the activity of HDAC8 is significantly inhibited when incubated with S-nitrosoglutathione and S-nitrosocysteine in a time- and dosage-dependent manner. Sodium nitroprusside and dithiothreitol cannot reverse this inhibition
S-nitrosoglutathione
HDAC8 can be S-nitrosylated by S-nitrosoglutathione in vitro, and the activity of HDAC8 is significantly inhibited when incubated with S-nitrosoglutathione and S-nitrosocysteine in a time- and dosage-dependent manner. Sodium nitroprusside and dithiothreitol cannot reverse this inhibition
S-[7-oxo-7-(2-phenyl1,3-thiazol-5-ylamino)heptyl] 2-methylpropanethioate
analysis of growth inhibition of various cancer cells and comparison with suberoylanilide hydroxamic acid
suberoylanilide hydroxyamic acid
-
a specific inhibitor of zinc-dependent histone deacetylase activity. The compound directly induces p19INK4d expression in regenerating liver by increasing p19INK4d promoter-associated histone acetylation, molecular mechanisms by which the inhibitor delays liver regeneration exerting promoter-specific effects on histone acetylation during liver regeneration, overview
trichostatinA
TSA, treatment with the specific HDAC inhibitor induces the enzyme HDA1, effectively inhibits AhHDA1 activity
[4-[(E)-[[6-(hydroxyamino)-6-oxohexanoyl]hydrazono]methyl]phenyl]boronic acid
-
(2E)-N-(2-aminophenyl)-3-(4-{1-[(2-hydroxyethyl)amino]-2-oxo-2-[4-(trifluoromethyl)anilino]ethyl}phenyl)prop-2-enamide
-
(2E)-N-(2-aminophenyl)-3-(4-{1-[(2-hydroxyethyl)amino]-2-oxo-2-[4-(trifluoromethyl)anilino]ethyl}phenyl)prop-2-enamide
-
(2E)-N-(2-aminophenyl)-3-(4-{1-[(3S)-3-(dimethylamino)pyrrolidin-1-yl]-2-oxo-2-[4-(trifluoromethyl)anilino]ethyl}phenyl)prop-2-enamide
-
(2E)-N-(2-aminophenyl)-3-(4-{1-[(3S)-3-(dimethylamino)pyrrolidin-1-yl]-2-oxo-2-[4-(trifluoromethyl)anilino]ethyl}phenyl)prop-2-enamide
-
(2E)-N-(2-aminophenyl)-3-[4-(1-{[2-(morpholin-4-yl)ethyl]amino}-2-oxo-2-[4-(trifluoromethyl)anilino]ethyl)phenyl]prop-2-enamide
-
(2E)-N-(2-aminophenyl)-3-[4-(1-{[2-(morpholin-4-yl)ethyl]amino}-2-oxo-2-[4-(trifluoromethyl)anilino]ethyl)phenyl]prop-2-enamide
-
(2E)-N-(2-aminophenyl)-3-{4-[2-(4-bromoanilino)-1-(3-hydroxypyrrolidin-1-yl)-2-oxoethyl]phenyl}prop-2-enamide
-
(2E)-N-(2-aminophenyl)-3-{4-[2-(4-bromoanilino)-1-(3-hydroxypyrrolidin-1-yl)-2-oxoethyl]phenyl}prop-2-enamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]-2-fluorophenyl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]-2-fluorophenyl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-benzyl-N-(4-chlorophenyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-benzyl-N-(4-chlorophenyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(3-methylphenyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(3-methylphenyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(4-methylphenyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(4-methylphenyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(6-methylpyridin-3-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(6-methylpyridin-3-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(piperidin-1-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(piperidin-1-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(propan-2-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(propan-2-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(pyridin-2-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(pyridin-2-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(pyridin-3-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(pyridin-3-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(pyridin-4-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-(pyridin-4-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-phenylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-phenylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-[4-(propan-2-yl)phenyl]pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-[4-(propan-2-yl)phenyl]pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-[4-(trifluoromethyl)phenyl]pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-1-methyl-N-[4-(trifluoromethyl)phenyl]pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(2,4-difluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(2,4-difluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(2-chloro-4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(2-chloro-4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(2-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(2-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3,4-dichlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3,4-dichlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3,4-difluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3,4-difluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-bromo-4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-bromo-4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-chloro-4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-chloro-4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-methoxyphenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(3-methoxyphenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-bromophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-bromophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chloro-3-methylphenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chloro-3-methylphenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2,2,2-trifluoroethyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2,2,2-trifluoroethyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2,2-difluoroethyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2,2-difluoroethyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2,2-dimethylpropyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2,2-dimethylpropyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2-fluoroethyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2-fluoroethyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2-methoxyethyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2-methoxyethyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(3-hydroxy-2,2-dimethylpropyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(3-hydroxy-2,2-dimethylpropyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(cyanomethyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(cyanomethyl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(oxan-4-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(oxan-4-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(propan-2-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(propan-2-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(pyrimidin-2-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(pyrimidin-2-yl)pyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-cyclobutylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-cyclobutylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-ethylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-ethylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-cyanophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-cyanophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-cyclopropylphenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-cyclopropylphenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-fluoro-3-methylphenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-fluoro-3-methylphenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-fluorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-methoxyphenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-methoxyphenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(5-chloropyridin-2-yl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(5-chloropyridin-2-yl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-cyclopentyl-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-cyclopentyl-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-cyclopropyl-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-cyclopropyl-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N~3~-(4-chlorophenyl)-N~1~,N~1~-diethylpyrrolidine-1,3-dicarboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N~3~-(4-chlorophenyl)-N~1~,N~1~-diethylpyrrolidine-1,3-dicarboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N~3~-(4-chlorophenyl)-N~1~-ethylpyrrolidine-1,3-dicarboxamide
-
(3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N~3~-(4-chlorophenyl)-N~1~-ethylpyrrolidine-1,3-dicarboxamide
-
(3R)-4-{5-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyrazin-2-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{5-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyrazin-2-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{5-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyridin-2-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{5-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyridin-2-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{6-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyridazin-3-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{6-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyridazin-3-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{6-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyridin-3-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R)-4-{6-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]pyridin-3-yl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R,4S)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
(3R,4S)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-methylpyrrolidine-3-carboxamide
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenylamide
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenylamide
-
6-[(9H-fluoren-3-ylmethyl)(3-phenoxybenzyl)amino]-N-hydroxyhexanamide
simultaneous and efficient interactions of compound with both the enzyme surface and the tubular binding pocket, through proper selection of its arm groups, are critical for potential antagonist activity
Butyrate
-
inhibition of histone deacetylase activity, resulting in prevention of interferon gamma-induced Janus kinase 1 activation, STAT1 phosphorylation, its nuclear translocation, and STAT1-dependent gene activation
Butyrate
-
inhibition of histone deacetylases, results in down-regulation of HoxA9 expression
HC-toxin
-
cyclic peptide inhibitor from Cochliobolus carbonum. Histone deacetylase in crude extracts of Alternaria brassicola is relatively insensitive to inhibition, such as enzyme from Cochliobolus carbonum. Comparison of sensitivity in various Cochliobolus carbonum strains and in several other fungi
HC-toxin
cyclic peptide inhibitor from Cochliobolus carbonum. Histone deacetylase in crude extracts of Cochliobolus carbonum is relatively insensitive to inhibition. Comparison of sensitivity in various Cochliobolus carbonum strains and in several other fungi. Resistance genetically cosegregates with toxin production
HC-toxin
-
cyclic peptide inhibitor from Cochliobolus carbonum. Histone deacetylase in crude extracts of Diheterospora chlamydosporia is relatively insensitive to inhibition, such as enzyme from Cochliobolus carbonum. Comparison of sensitivity in various Cochliobolus carbonum strains and in several other fungi
LAQ824
-
enzyme inhibition results in altered Toll-like receptor 4-dependent activation and function of macrophages and dendritic cells. Pan-HDAC inhibition modulates only a limited set of genes involved in distinct arms of immune responses, specifically dendritic cell-controlled T helper 1 effector, but not T helper 2 effector cell activation and migration. It also inhibits dendritic cell-mediated monocyte, but not neutrophil chemotaxis
MS-275
-
inhibition of HDAC1 leads to a significant increase of global acetylation of residues K9 and K14 on histone H3, which is a feature of active transcription, and a significant induction of proinflammatory cytokine expression. Genomic DNA corresponding to the IL1beta and IL6 promoter is significantly enriched upon HDAC 1 inhibition
MS-275
-
inhibition of histone deacetylases, results in down-regulation of HoxA9 expression
N-hydroxy-4-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}butanamide
-
N-hydroxy-4-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}butanamide
-
N-hydroxy-5-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}pentanamide
-
N-hydroxy-5-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}pentanamide
-
N-hydroxy-6-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}hexanamide
-
N-hydroxy-6-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}hexanamide
-
N-hydroxy-7-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}heptanamide
-
N-hydroxy-7-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}heptanamide
-
N-hydroxy-8-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}octanamide
-
N-hydroxy-8-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}octanamide
-
N-hydroxy-N~3~-[5-(propan-2-yl)naphthalene-1-sulfonyl]-beta-alaninamide
-
N-hydroxy-N~3~-[5-(propan-2-yl)naphthalene-1-sulfonyl]-beta-alaninamide
-
suberoylanilide hydroxamic acid
-
inhibition of histone deacetylase activity, resulting in prevention of interferon gamma-induced Janus kinase 1 activation, STAT1 phosphorylation, its nuclear translocation, and STAT1-dependent gene activation
suberoylanilide hydroxamic acid
-
SAHA, vorinostat, zolinza, broad-spectrum or pan-HDAC inhibitor
suberoylanilide hydroxamic acid
SAHA; SAHA; SAHA; SAHA; SAHA
suberoylanilide hydroxamic acid
-
i.e. SAHA, antiproliferative activities against MDA-MB-231 and K562 cell lines, IC50 0.00132 and 0.00169 microM, respectively
suberoylanilide hydroxamic acid
complete inhibition; complete inhibition
suberoylanilide hydroxamic acid
SAHA, Ki, for the T-cell lymphoma drug suberoylanilide hydroxamic acid (SAHA) is different for each metal-substituted HDAC8
sulforaphane
-
at 0.015 mM, 40, 30 and 40% inhibition of histone deacetylase activities in BPH-1, LnCaP and PC-3 prostate epithelial cells, resp. Inhibition is accompanied by a 50-100% increase in acetylated histones. BPH-1 cells treated with inhibitor show enhanced interaction of acetylated histone H4 with the promoter region of the P21 gene and the bax gene
trichostatin A
TSA, a HDAC inhibitor; TSA, a HDAC inhibitor
trichostatin A
-
inhibition of histone deacetylase activity, resulting in prevention of interferon gamma-induced Janus kinase 1 activation, STAT1 phosphorylation, its nuclear translocation, and STAT1-dependent gene activation
trichostatin A
-
-
trichostatin A
-
inhibition of histone deacetylases, results in down-regulation of HoxA9 expression
trichostatin-A
specific HDAC inhibitor; specific HDAC inhibitor; specific HDAC inhibitor
Valproic acid
-
treatment causes hyperacetylation of histones in cultured cells and activates transcription from diverse exogenous and endogenous promoters
additional information
enzyme is part of a high molecular weight complex insensitive to trichostatin A
-
additional information
enzyme is part of a high molecular weight complex insensitive to trichostatin A
-
additional information
-
in phosphate buffer, the presence of NaCl is inhibitory
-
additional information
isoform HDAC10 is resistant to inhibitors trapoxin B and sodium butyrate
-
additional information
-
when A-549 cells are stretched for 24 h cytoplasmic HDAC activity is decreased
-
additional information
-
nitration of distinct tyrosine residues; nitrative/oxidative stress reduce HDAC2 expression via nitration of distinct tyrosine residues. Peroxynitrite, hydrogen peroxide and cigarette smoke-conditioned medium reduce HDAC2 expression in A549 epithelial cells in vitro. This reduction is due to increased proteasomal degradation following ubiquitination rather than reduction of mRNA expression or stability
-
additional information
nitration of distinct tyrosine residues; nitrative/oxidative stress reduce HDAC2 expression via nitration of distinct tyrosine residues. Peroxynitrite, hydrogen peroxide and cigarette smoke-conditioned medium reduce HDAC2 expression in A549 epithelial cells in vitro. This reduction is due to increased proteasomal degradation following ubiquitination rather than reduction of mRNA expression or stability
-
additional information
HDAC is not inhibited by isovaleric acid, L-valine, sodium lactate, succinic acid, citric acid, benzylic acid, hippuric acid, antranilic acid (2-aminobenzoic acid), alpha-hydroxyacetonaphthone, and kojic acid
-
additional information
-
HDAC is not inhibited by isovaleric acid, L-valine, sodium lactate, succinic acid, citric acid, benzylic acid, hippuric acid, antranilic acid (2-aminobenzoic acid), alpha-hydroxyacetonaphthone, and kojic acid
-
additional information
methylselenocysteine and selenomethionine have little or no inhibitory activity up to 2 mM
-
additional information
-
methylselenocysteine and selenomethionine have little or no inhibitory activity up to 2 mM
-
additional information
-
3-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid shows no inhibition of HDAC1 at 0.01 mM, 2,2,2-trifluoro-1-[5-(pyridin-2-yl)thiophen-2-yl]ethanone is inactive against HDAC6, 2,2,2-trifluoro-1-[5-(1H-indol-5-yl)thiophen-2-yl]ethanone is essentially inactive against HDAC1 and 4
-
additional information
-
HDAC10 is not inhibited by SK7068, MS275, and oxamflatin
-
additional information
-
presence of 5-6 carbon units between the Zn2+ binding group and the 1,3,4-thiadiazole ring is optimal for inhibitory potency
-
additional information
enzyme binding mechanisms, overview; enzyme binding mechanisms, overview; enzyme binding mechanisms, overview
-
additional information
enzyme binding mechanisms, overview; enzyme binding mechanisms, overview; enzyme binding mechanisms, overview
-
additional information
enzyme binding mechanisms, overview; enzyme binding mechanisms, overview; enzyme binding mechanisms, overview
-
additional information
-
enzyme binding mechanisms, overview; enzyme binding mechanisms, overview; enzyme binding mechanisms, overview
-
additional information
pharmacokinetic optimization of class-selective histone deacetylase inhibitors and identification of associated candidate predictive biomarkers of hepatocellular carcinoma tumor response, structure-activity and structure-property relationships for trans-3,4-disubstituted pyrrolidine inhibitors, overview. No inhibition by (3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2-hydroxyethyl)pyrrolidine-3-carboxamide and (3R)-4-{4-[(1E)-3-(2-aminoanilino)-3-oxoprop-1-en-1-yl]phenyl}-N-(4-chlorophenyl)-1-(2-hydroxy-2-methylpropyl)pyrrolidine-3-carboxamide
-
additional information
determination of structure-activity and structure-kinetic relationships of a series of selective ortho-aminoanilide inhibitors of histone deacetylase isozymes (HDACs) 1 and 2, overview. Measurements of increases in neuronal histone acetylation in mouse fore-brain primary neuronal cultures induced by HDAC inhibitor compounds. Analysis of the stability of the compounds in murine plasma and liver microsomes; determination of structure-activity and structure-kinetic relationships of a series of selective ortho-aminoanilide inhibitors of histone deacetylase isozymes (HDACs) 1 and 2, overview. Measurements of increases in neuronal histone acetylation in mouse fore-brain primary neuronal cultures induced by HDAC inhibitor compounds. Analysis of the stability of the compounds in murine plasma and liver microsomes; determination of structure-activity and structure-kinetic relationships of a series of selective ortho-aminoanilide inhibitors of histone deacetylase isozymes (HDACs) 1 and 2, overview. Measurements of increases in neuronal histone acetylation in mouse fore-brain primary neuronal cultures induced by HDAC inhibitor compounds. Analysis of the stability of the compounds in murine plasma and liver microsomes
-
additional information
determination of structure-activity and structure-kinetic relationships of a series of selective ortho-aminoanilide inhibitors of histone deacetylase isozymes (HDACs) 1 and 2, overview. Measurements of increases in neuronal histone acetylation in mouse fore-brain primary neuronal cultures induced by HDAC inhibitor compounds. Analysis of the stability of the compounds in murine plasma and liver microsomes; determination of structure-activity and structure-kinetic relationships of a series of selective ortho-aminoanilide inhibitors of histone deacetylase isozymes (HDACs) 1 and 2, overview. Measurements of increases in neuronal histone acetylation in mouse fore-brain primary neuronal cultures induced by HDAC inhibitor compounds. Analysis of the stability of the compounds in murine plasma and liver microsomes; determination of structure-activity and structure-kinetic relationships of a series of selective ortho-aminoanilide inhibitors of histone deacetylase isozymes (HDACs) 1 and 2, overview. Measurements of increases in neuronal histone acetylation in mouse fore-brain primary neuronal cultures induced by HDAC inhibitor compounds. Analysis of the stability of the compounds in murine plasma and liver microsomes
-
additional information
determination of structure-activity and structure-kinetic relationships of a series of selective ortho-aminoanilide inhibitors of histone deacetylase isozymes (HDACs) 1 and 2, overview. Measurements of increases in neuronal histone acetylation in mouse fore-brain primary neuronal cultures induced by HDAC inhibitor compounds. Analysis of the stability of the compounds in murine plasma and liver microsomes; determination of structure-activity and structure-kinetic relationships of a series of selective ortho-aminoanilide inhibitors of histone deacetylase isozymes (HDACs) 1 and 2, overview. Measurements of increases in neuronal histone acetylation in mouse fore-brain primary neuronal cultures induced by HDAC inhibitor compounds. Analysis of the stability of the compounds in murine plasma and liver microsomes; determination of structure-activity and structure-kinetic relationships of a series of selective ortho-aminoanilide inhibitors of histone deacetylase isozymes (HDACs) 1 and 2, overview. Measurements of increases in neuronal histone acetylation in mouse fore-brain primary neuronal cultures induced by HDAC inhibitor compounds. Analysis of the stability of the compounds in murine plasma and liver microsomes
-
additional information
series of HDAC inhibitors, using 1,2,4-oxadiazole-containing as the cap group, are synthesized and evaluated in vitro, inhibitory effects and inhibition of diverse cancer cells, overview. Pharmacokinetic studies. Most HDAC inhibitors always have three parts: a cap group used as a selective vector, a ZBG group to bind with the Zn2+ ion, and a linker region that traditionally allows the ZBG group stretch into the catalytic binding; series of HDAC inhibitors, using 1,2,4-oxadiazole-containing as the cap group, are synthesized and evaluated in vitro, inhibitory effects and inhibition of diverse cancer cells, overview. Pharmacokinetic studies. Most HDAC inhibitors always have three parts: a cap group used as a selective vector, a ZBG group to bind with the Zn2+ ion, and a linker region that traditionally allows the ZBG group stretch into the catalytic binding
-
additional information
series of HDAC inhibitors, using 1,2,4-oxadiazole-containing as the cap group, are synthesized and evaluated in vitro, inhibitory effects and inhibition of diverse cancer cells, overview. Pharmacokinetic studies. Most HDAC inhibitors always have three parts: a cap group used as a selective vector, a ZBG group to bind with the Zn2+ ion, and a linker region that traditionally allows the ZBG group stretch into the catalytic binding; series of HDAC inhibitors, using 1,2,4-oxadiazole-containing as the cap group, are synthesized and evaluated in vitro, inhibitory effects and inhibition of diverse cancer cells, overview. Pharmacokinetic studies. Most HDAC inhibitors always have three parts: a cap group used as a selective vector, a ZBG group to bind with the Zn2+ ion, and a linker region that traditionally allows the ZBG group stretch into the catalytic binding
-
additional information
-
series of HDAC inhibitors, using 1,2,4-oxadiazole-containing as the cap group, are synthesized and evaluated in vitro, inhibitory effects and inhibition of diverse cancer cells, overview. Pharmacokinetic studies. Most HDAC inhibitors always have three parts: a cap group used as a selective vector, a ZBG group to bind with the Zn2+ ion, and a linker region that traditionally allows the ZBG group stretch into the catalytic binding; series of HDAC inhibitors, using 1,2,4-oxadiazole-containing as the cap group, are synthesized and evaluated in vitro, inhibitory effects and inhibition of diverse cancer cells, overview. Pharmacokinetic studies. Most HDAC inhibitors always have three parts: a cap group used as a selective vector, a ZBG group to bind with the Zn2+ ion, and a linker region that traditionally allows the ZBG group stretch into the catalytic binding
-
additional information
pharmacokinetic optimization of class-selective histone deacetylase inhibitors and identification of associated candidate predictive biomarkers of hepatocellular carcinoma tumor response, structure-activity and structure-property relationships for trans-3,4-disubstituted pyrrolidine inhibitors, overview
-
additional information
-
pharmacokinetic optimization of class-selective histone deacetylase inhibitors and identification of associated candidate predictive biomarkers of hepatocellular carcinoma tumor response, structure-activity and structure-property relationships for trans-3,4-disubstituted pyrrolidine inhibitors, overview
-
additional information
-
the CDK-related kinase 3-associated HDAC activities are sensitive to the class I/II HDAC inhibitor trichostatin A and to the sirtuin inhibitor nicotinamide
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-(cyclohexylcarbamothioyl)benzamide
-
10 microM, 5.6fold activation of HDAC8. No activation of other HDAC isoenzymes
N-(phenylcarbamothioyl)benzamide
-
10 microM, 12fold activation of HDAC8. No activation of other HDAC isoenzymes
N-[(3,5-dimethoxyphenyl)carbamothioyl]benzamide
-
10 microM, 8.4fold activation of HDAC8. No activation of other HDAC isoenzymes
additional information
-
in Tris/HCl buffer, optimum concentration of NaCl is 50 mM for isoforms HD1 and HD2 and 100 mM for the nuclear matrix form
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.078
benzyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1, 37°C, pH not specified in the publication
0.099
benzyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC6, 37°C, pH not specified in the publication
0.03
benzyloxycarbonyl-L-Lys(trifluoroacetyl)-7-amido-4-methylcoumarin
-
isoform HDAC8, 37°C, pH not specified in the publication
0.061
benzyloxycarbonyl-L-Lys(trifluoroacetyl)-7-amido-4-methylcoumarin
-
isoform HDAC7, 37°C, pH not specified in the publication
0.23
Fluor de Lys HDAC8 substrate
-
presence of activator N-(phenylcarbamothioyl)benzamide, pH not specified in the publication, temperature not specified in the publication
-
0.744
Fluor de Lys HDAC8 substrate
-
pH not specified in the publication, temperature not specified in the publication
-
additional information
additional information
-
Km value according to commercial HDAC Fluorescent Activity Assay Kit is 0.143 mM
-
additional information
additional information
enzyme kinetic calculations, overview
-
additional information
additional information
enzyme kinetic calculations, overview
-
additional information
additional information
enzyme kinetic calculations, overview
-
additional information
additional information
enzyme kinetic calculations, overview
-
additional information
additional information
-
enzyme kinetic calculations, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
Fluor de Lys HDAC8 substrate
-
pH not specified in the publication, temperature not specified in the publication
-
0.036
Fluor de Lys HDAC8 substrate
-
presence of activator N-(phenylcarbamothioyl)benzamide, pH not specified in the publication, temperature not specified in the publication
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
substrate specifcity, catalytic efficiencies with different peptides substrates of the enzyme with bound Fe2+ and/or Zn2+, overview
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0033 - 0.024
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid (3,4-dimethylphenyl)-amide hydroxyamide
0.0053 - 0.049
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid biphenyl-2-ylamide hydroxyamide
0.0014 - 0.0054
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide (4-phenylthiazol-2-yl)amide
0.011 - 0.029
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenyl-amide
0.000135
chlorogenic acid
pH and temperature not specified in the publication
0.00000821
Cinnamic acid
pH and temperature not specified in the publication
0.00819
gamma-aminobutyric acid
pH and temperature not specified in the publication
0.0000137
methyl (3R,6R,9R)-9-(acetylamino)-6-[6-(hydroxyamino)-6-oxohexyl]-5,8-dioxo-4,7-diazabicyclo[9.3.1]pentadeca-1(15),11,13-triene-3-carboxylate
-
HeLa cell nuclear extract
0.0028
phenyl butyric acid
pH and temperature not specified in the publication
0.365
sodium butyrate
pH and temperature not specified in the publication
0.00634
sodium phenylbutyrate
pH and temperature not specified in the publication
0.00247
suberoyl anilide hydroxamic acid
pH and temperature not specified in the publication
0.000504
trichostatin A
pH and temperature not specified in the publication
0.0033
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid (3,4-dimethylphenyl)-amide hydroxyamide
-
isoform HDAC7, 37°C, pH not specified in the publication
0.0088
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid (3,4-dimethylphenyl)-amide hydroxyamide
-
isoform HDAC1, 37°C, pH not specified in the publication
0.014
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid (3,4-dimethylphenyl)-amide hydroxyamide
-
isoform HDAC8, 37°C, pH not specified in the publication
0.024
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid (3,4-dimethylphenyl)-amide hydroxyamide
-
isoform HDAC6, 37°C, pH not specified in the publication
0.0053
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid biphenyl-2-ylamide hydroxyamide
-
isoform HDAC8, 37°C, pH not specified in the publication
0.0092
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid biphenyl-2-ylamide hydroxyamide
-
isoform HDAC6, 37°C, pH not specified in the publication
0.014
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid biphenyl-2-ylamide hydroxyamide
-
isoform HDAC7, 37°C, pH not specified in the publication
0.049
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid biphenyl-2-ylamide hydroxyamide
-
isoform HDAC1, 37°C, pH not specified in the publication
0.0014
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide (4-phenylthiazol-2-yl)amide
-
isoform HDAC7, 37°C, pH not specified in the publication
0.0015
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide (4-phenylthiazol-2-yl)amide
-
isoform HDAC8, 37°C, pH not specified in the publication
0.0026
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide (4-phenylthiazol-2-yl)amide
-
isoform HDAC1, 37°C, pH not specified in the publication
0.0054
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide (4-phenylthiazol-2-yl)amide
-
isoform HDAC6, 37°C, pH not specified in the publication
0.011
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenyl-amide
-
isoform HDAC6, 37°C, pH not specified in the publication
0.011
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenyl-amide
-
isoform HDAC7, 37°C, pH not specified in the publication
0.017
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenyl-amide
-
isoform HDAC8, 37°C, pH not specified in the publication
0.029
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenyl-amide
-
isoform HDAC1, 37°C, pH not specified in the publication
0.000044
suberoylanilide hydroxamic acid
presence of Co(II), 25°C. pH 8.0
additional information
additional information
inhibition kinetic calculations, Kd values, detailed overview
-
additional information
additional information
inhibition kinetic calculations, Kd values, detailed overview
-
additional information
additional information
inhibition kinetic calculations, Kd values, detailed overview
-
additional information
additional information
inhibition kinetic calculations, Kd values, detailed overview
-
additional information
additional information
-
inhibition kinetic calculations, Kd values, detailed overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000168 - 0.0137
(1R,5S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-6-oxabicyclo[3.1.1]heptane-3-carboxamide
0.00088
(2E)-3-[1,2-bis(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
Homo sapiens
-
-
0.00041
(2E)-3-[1-benzyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
Homo sapiens
-
-
0.0012
(2E)-3-[1-benzyl-2-(2-phenylethyl)-1H-benzimidazol-6-yl]-N-hydroxyprop-2-enamide
Homo sapiens
-
-
0.00022
(2E)-3-[1-ethyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
Homo sapiens
-
-
0.000052
(2E)-3-[1-[2-(diethylamino)ethyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
Homo sapiens
-
-
0.000041
(2E)-3-[1-[3-(dimethylamino)-2,2-dimethylpropyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
Homo sapiens
-
-
0.00019
(2E)-3-[1-[3-(dimethylamino)propyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
Homo sapiens
-
-
0.00016
(2E)-3-[1-[4-(dimethylamino)butyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
Homo sapiens
-
-
0.0032
(2E)-3-[2-cyclohexyl-1-(3-hydroxypropyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
Homo sapiens
-
-
0.00017
(2E)-3-[2-[(benzyloxy)methyl]-1-(3-hydroxypropyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
Homo sapiens
-
-
0.000045
(2E)-3-[4-([[2-(3a,7a-dihydro-1H-indol-3-yl)ethyl](2-hydroxyethyl)amino]methyl)phenyl]-N-hydroxyprop-2-enamide
Homo sapiens
pH and temperature not specified in the publication
0.1
(2E)-N-(2-aminophenyl)-3-[2-(2-phenylethyl)-1-(pyridin-2-ylmethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
larger than 0.10
0.00027
(2E)-N-hydroxy-3-[1-(2-morpholin-4-ylethyl)-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.0011
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.0017
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(1-methylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.0001
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-methylpropyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00017
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00008
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-phenylpropyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00053
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-octyl-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.0019
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-thiophen-3-yl-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00021
(2E)-N-hydroxy-3-[1-(3-methoxypropyl)-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00025
(2E)-N-hydroxy-3-[1-(3-morpholin-4-ylpropyl)-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00026
(2E)-N-hydroxy-3-[1-methyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00016
(2E)-N-hydroxy-3-[1-[3-(1H-imidazol-1-yl)propyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.0002
(2E)-N-hydroxy-3-[1-[3-(2-oxopyrrolidin-1-yl)propyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.000026
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(2-piperidin-1-ylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.000035
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(2-pyrrolidin-1-ylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.000047
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(3,4,5-trimethoxybenzyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00031
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(3-pyrrolidin-1-ylpropyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00025
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(pyridin-2-ylmethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00017
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-propyl-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00017
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
Homo sapiens
-
-
0.00093
(2E)-N-hydroxy-3-[2-[(4-methoxyphenyl)sulfonyl]-2,3-dihydro-1H-isoindol-5-yl]prop-2-enamide
Homo sapiens
-
isoform HDAC1, pH not specified in the publication, temperature not specified in the publication
0.000016
(2E)-N-hydroxy-3-[2-[2-(1H-indol-3-yl)ethyl]-2,3-dihydro-1H-isoindol-5-yl]prop-2-enamide
Homo sapiens
-
isoform HDAC1, pH not specified in the publication, temperature not specified in the publication
0.000026
(2E)-N-hydroxy-3-[2-[2-(2-methyl-1H-indol-3-yl)ethyl]-2,3-dihydro-1H-isoindol-5-yl]prop-2-enamide
Homo sapiens
-
isoform HDAC1, pH not specified in the publication, temperature not specified in the publication
0.000078
(2E)-N-hydroxy-3-[2-[2-(pyrazolo[1,5-a]pyridin-3-yl)ethyl]-2,3-dihydro-1H-isoindol-5-yl]prop-2-enamide
Homo sapiens
-
isoform HDAC1, pH not specified in the publication, temperature not specified in the publication
4 - 8.1
(2S)-2-(acetylamino)-3-[3-[(2S)-2-[[(2S)-2-ammonio-7-(hydroxyamino)-7-oxoheptanoyl]amino]-3-methoxy-3-oxopropyl]phenyl]propanoate
0.00014
(2S)-8-oxo-2-[(3-piperidin-1-ylpropanoyl)amino]-N-quinolin-3-ylnonanamide
Homo sapiens
-
HDAC1
0.00011 - 0.013
(3S,15R,20aS)-15-methyl-3-[(1E)-4-sulfanylbut-1-en-1-yl]-3,4,6,7,14,15,18,19,20,20a-decahydro-1H,5H,16H-11,8:15,12-di(azeno)pyrrolo[2,1-c][1,8,12,4,15]oxadithiadiazacyclooctadecine-1,5,16-trione
0.0003 - 0.01
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
0.000025 - 0.01
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
0.00002 - 0.01
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
0.000012 - 0.01
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
0.00027 - 0.03
(4E)-N-(2-aminophenyl)-5-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]pent-4-enamide
0.03
(4Z)-6-[(5R,8S,11R)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]hex-4-enoic acid
Homo sapiens
larger than 0.030
0.014 - 0.03
(5E)-N-(2-aminophenyl)-6-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]hex-5-enamide
0.0000012 - 0.000049
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
0.00000032 - 0.000029
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3-thia-7,14,20,21-tetraazatricyclo[14.3.1.1-2,5]henicosa-1(20),2(21),16,18-tetraene-6,9,13-trione
0.0000019 - 0.00013
(5R,8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
0.0012 - 0.0031
(5S,8R,11R)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
0.00000069 - 0.000045
(5S,8S,11S,5'S,8'S,11'S)-11,11'-[disulfanediyldi(1E)but-1-ene-4,1-diyl]bis[5-methyl-8-(1-methylethyl)-3,10,17-trioxa-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione]
0.000077 - 0.03
(8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),4,16(19)-tetraene-6,9,13-trione
547.3
(E)-3-(2-(((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)pyrimidin-5-yl)-N-hydroxyacrylamide
Homo sapiens
pH and temperature not specified in the publication
0.000035 - 0.000086
(E)-3-[3-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]phenyl]-N-hydroxyacrylamide
292.5
(E)-N-hydroxy-3-(2-(methyl((3-(1-(4-methylbenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)amino)pyrimidin-5-yl)acrylamide
Homo sapiens
pH and temperature not specified in the publication
0.00016
(E)-N1-hydroxy-N5-(5-styryl-1,3,4-thiadiazol-2-yl)glutaramide
Homo sapiens
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37°C, pH not specified in the publication
0.00557
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-(4-methoxyphenyl)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00106
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-(naphthalen-1-yl)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00362
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-m-tolyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00413
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-o-tolyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00382
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-p-tolyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00354
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-pentyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00407
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-phenethyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00821
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-phenyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide hydrochloride
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.05
(S)-benzyl 3-(biphenyl-4-ylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
IC50 above 0.05 mM, in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00058
(S)-benzyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenethylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.05
(S)-benzyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
IC50 above 0.05 mM, in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00339
(S)-N-(2,4-dimethylphenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00334
(S)-N-(3-chloro-4-fluorophenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.0032
(S)-N-(3-chlorophenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00323
(S)-N-(4-fluorophenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00221
(S)-N-(biphenyl-4-yl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.0051
(S)-N-benzyl-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide hydrochloride
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00577
(S)-N-hexyl-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.01217
(S)-N-tert -butyl-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00378
(S)-tert-butyl 3-(2,4-dimethylphenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00155
(S)-tert-butyl 3-(3-chloro-4-fluorophenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00117
(S)-tert-butyl 3-(3-chlorophenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00256
(S)-tert-butyl 3-(4-fluorophenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00341
(S)-tert-butyl 3-(benzylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00198
(S)-tert-butyl 3-(biphenyl-4-ylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00442
(S)-tert-butyl 3-(hexylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00458
(S)-tert-butyl 3-(tert-butylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.001
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(4-methoxyphenylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00177
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(mtolylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00425
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(naphthalen-1-ylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.004
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(o-tolylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00165
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(p-tolylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00302
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(pentylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00267
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenethylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.00129
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
Homo sapiens
in 15 mM Tris-HCl, pH 8.0, at 37°C
0.000055
1-methyl-N-[(1S)-7-oxo-1-[(4-phenyl-1,3-thiazol-2-yl)carbamoyl]octyl]piperidine-2-carboxamide
Homo sapiens
-
HDAC1
0.000037 - 0.01
1-[5-(2,3-dihydro-1,4-benzodioxin-6-yl)thiophen-2-yl]-2,2,2-trifluoroethanone
0.098
15-deoxy-DELTA12,14-prostaglandin J2-biotin
Homo sapiens
-
recombinant HDAC3 in complex with CoR1, pH and temperature not specified in the publication
0.000024 - 0.0027
2,2,2-trifluoro-1-(5-[3-[(methylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
0.00003 - 0.0022
2,2,2-trifluoro-1-(5-[3-[(propylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
0.000035 - 0.0039
2,2,2-trifluoro-1-(5-[3-[(thiophen-2-ylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
0.00006 - 0.0066
2,2,2-trifluoro-1-[5-(3-[[(4-fluorobenzyl)sulfonyl]methyl]-1,2,4-oxadiazol-5-yl)thiophen-2-yl]ethanone
34.3
2-(((3-(1-(2,4-difluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
115.7
2-(((3-(1-(2-chloro-4-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
48.3
2-(((3-(1-(2-chlorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
98.6
2-(((3-(1-(2-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
116.6
2-(((3-(1-(4-cyanobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
22
2-(((3-(1-(4-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
27.6
2-(((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000026 - 0.01
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide
0.000059 - 0.01
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
0.0023
3-[5-[(1E)-3-(hydroxyamino)-3-oxoprop-1-en-1-yl]-2-(2-phenylethyl)-1H-benzimidazol-1-yl]propanoic acid
Homo sapiens
-
-
0.00023 - 0.0063
3-[5-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]furan-2-yl]-N-hydroxy-acrylamide
0.14
4-hydroxy-2-nonenal
Homo sapiens
-
recombinant HDAC3 in complex with CoR1, pH and temperature not specified in the publication
0.04316
4-[[(2E)-2-(4-chlorobenzylidene)hydrazinyl]carbonothioyl]-N-hydroxypiperazine-1-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000059
6-[(2E)-2-[(2-bromo-4-hydroxy-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
Plasmodium falciparum
-
0.000106
6-[(2E)-2-[(2-bromo-4-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
Plasmodium falciparum
-
0.000089
6-[(2E)-2-[(2-bromo-5-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
Plasmodium falciparum
-
0.0001 - 0.01
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
0.00007
6-[(9H-fluoren-3-ylmethyl)(3-phenoxybenzyl)amino]-N-hydroxyhexanamide
Homo sapiens
-
HDAC activity in HeLa nuclear cell extracts, 25°C, pH 8.0
0.00017
6-[(biphenyl-4-ylmethyl)[4-[(4-bromobenzyl)oxy]benzyl]amino]-N-hydroxyhexanamide
Homo sapiens
-
HDAC activity in HeLa nuclear cell extracts, 25°C, pH 8.0
0.0003159
6-[4-(2,6-dimethoxyphenyl)-1H-1,2,3-triazol-1-yl]-N-hydroxyhexanamide
Homo sapiens
-
-
0.00018
6-[[4-[(4-bromobenzyl)oxy]benzyl](9H-fluoren-3-ylmethyl)amino]-N-hydroxyhexanamide
Homo sapiens
-
HDAC activity in HeLa nuclear cell extracts, 25°C, pH 8.0
0.0000043
6-{4-[4-(dimethylamino)phenyl]-1H-1,2,3-triazol-1-yl}-N-hydroxyhexanamide
Homo sapiens
-
-
0.000059
7-[(2E)-2-[(2-bromo-4-hydroxy-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Plasmodium falciparum
-
0.000049
7-[(2E)-2-[(2-bromo-5-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Plasmodium falciparum
-
0.000022
7-[(2E)-2-[(2-bromo-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Plasmodium falciparum
-
0.000037
7-[(2E)-2-[(2-bromophenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Plasmodium falciparum
-
0.000036
7-[(2E)-2-[(2-bromopyridin-3-yl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Plasmodium falciparum
-
0.00009
7-[(2E)-2-[(2-chlorophenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Plasmodium falciparum
-
0.00002
7-[(2E)-2-[(6-bromo-1,3-benzodioxol-5-yl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Plasmodium falciparum
-
0.000037
7-[(2E)-2-[[4-(dimethylamino)-2-hydroxyphenyl]methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Plasmodium falciparum
-
0.0001061
7-{4-[4-(dimethylamino)phenyl]-1H-1,2,3-triazol-1-yl}-N-hydroxyheptanamide
Homo sapiens
-
-
0.00011
8-[(2E)-2-[(2,5-dihydroxyphenyl)methylidene]hydrazino]-N-hydroxy-8-oxooctanamide
Plasmodium falciparum
-
0.02
beta-methylselenopyruvate
Homo sapiens
HDAC8, at 37°C, pH not specified in the publication
0.375
chlorogenic acid
Homo sapiens
pH and temperature not specified in the publication
0.000046 - 0.231
methyl (3R,6R,9R)-9-(acetylamino)-6-[6-(hydroxyamino)-6-oxohexyl]-5,8-dioxo-4,7-diazabicyclo[9.3.1]pentadeca-1(15),11,13-triene-3-carboxylate
0.000167 - 0.000174
methyl N-[(2S)-2-[(N-acetyl-L-alanyl)amino]-7-(hydroxyamino)-7-oxoheptanoyl]-L-phenylalaninate
0.000045 - 0.0259
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-1H-2-benzopyran-3-carboxamide
0.000072 - 0.033
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-2H-1-benzopyran-3-carboxamide
0.000123 - 0.00149
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3-oxabicyclo[3.1.0]hexane-6-carboxamide
0.0000097
N-(8,8,8-trifluoro-7-oxooctyl)benzamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
-
0.0033
N-hydroxy-1-(3-hydroxypropyl)-2-(2-phenylethyl)-1H-benzimidazole-5-carboxamide
Homo sapiens
-
-
47.3
N-hydroxy-2-(methyl((3-(1-(3-methylbenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)amino)pyrimidine-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
207
N-hydroxy-2-(methyl((3-(1-(4-(trifluoromethyl)benzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)amino)pyrimidine-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
12.1
N-hydroxy-2-(methyl((3-(1-(4-methylbenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)amino)pyrimidine-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0013
N-hydroxy-2-[1-methyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]cyclopropanecarboxamide
Homo sapiens
-
-
0.01
N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-methylpropyl)-1H-benzimidazol-5-yl]propanamide
Homo sapiens
-
larger than 0.010
0.00017
N-hydroxy-3-[2-(2-phenylethyl)-1-(3,4,5-trimethoxybenzyl)-1H-benzimidazol-5-yl]propanamide
Homo sapiens
-
-
0.00002
N-hydroxy-3-[2-[(2-methyl-1H-indol-3-yl)acetyl]-2,3-dihydro-1H-isoindol-5-yl]propanamide
Homo sapiens
-
isoform HDAC1, pH not specified in the publication, temperature not specified in the publication
0.000044 - 0.000175
N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
0.03367
N-hydroxy-4-[[(2E)-2-(2-hydroxybenzylidene)hydrazinyl]carbonothioyl]piperazine-1-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0000002 - 0.01
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
0.0000006 - 0.01
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
0.0000018
N-hydroxy-6-[4-(6-methoxynaphthalen-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
Homo sapiens
-
-
0.0000023
N-hydroxy-6-{4-[4-(pyridin-4-yl)phenyl]-1H-1,2,3-triazol-1-yl}hexanamide
Homo sapiens
-
-
0.000041
N-hydroxy-7-[(2E)-2-[(2-hydroxynaphthalen-1-yl)methylidene]hydrazino]-7-oxoheptanamide
Plasmodium falciparum
-
0.000059
N-hydroxy-7-[(2E)-2-[(3-hydroxyphenyl)methylidene]hydrazino]-7-oxoheptanamide
Plasmodium falciparum
-
0.000015
N-hydroxy-7-[(2E)-2-[[4-(1H-imidazol-1-yl)phenyl]methylidene]hydrazino]-7-oxoheptanamide
Plasmodium falciparum
-
0.0000153
N-hydroxy-7-[4-(6-methoxynaphthalen-2-yl)-1H-1,2,3-triazol-1-yl]heptanamide
Homo sapiens
-
-
0.0000166
N-hydroxy-7-{4-[4-(pyridin-4-yl)phenyl]-1H-1,2,3-triazol-1-yl}heptanamide
Homo sapiens
-
-
0.000043
N-hydroxy-8-oxo-8-[(2E)-2-[(2,4,6-trihydroxyphenyl)methylidene]hydrazino]octanamide
Plasmodium falciparum
-
0.000089 - 0.00058
N-methyl-N-(quinoxalin-6-ylmethyl)-5-(trifluoroacetyl)thiophene-2-carboxamide
0.00067 - 0.01
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
0.00067 - 0.0016
N-[(2E)-3-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]prop-2-en-1-yl]-2-sulfanylacetamide
0.00024 - 0.0019
N-[(3E)-4-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]but-3-en-1-yl]-2-sulfanylacetamide
0.0000621
N-[1,1,2,2,3,3,4,4,5,5,6,6-dodecafluoro-7-(hydroxyamino)-7-oxoheptyl]benzamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.00022
N1-(5-benzyl-1,3,4-thiadiazol-2-yl)-N7-hydroxyheptanediamide
Homo sapiens
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37°C, pH not specified in the publication
0.00026
N1-(5-benzyl-1,3,4-thiadiazol-2-yl)-N8-hydroxyoctanediamide
Homo sapiens
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37°C, pH not specified in the publication
0.000089
N1-hydroxy-N7-(5-phenyl-1,3,4-thiadiazol-2-yl)heptanediamide
Homo sapiens
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37°C, pH not specified in the publication
0.00027
N1-hydroxy-N8-(5-phenyl-1,3,4-thiadiazol-2-yl)octanediamide
Homo sapiens
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37°C, pH not specified in the publication
0.013
sodium butyrate
Homo sapiens
-
recombinant HDAC3 in complex with CoR1, pH and temperature not specified in the publication
0.000045
[4-[(E)-[[6-(hydroxyamino)-6-oxohexanoyl]hydrazono]methyl]phenyl]boronic acid
Plasmodium falciparum
-
0.000168
(1R,5S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-6-oxabicyclo[3.1.1]heptane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.000192
(1R,5S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-6-oxabicyclo[3.1.1]heptane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.00145
(1R,5S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-6-oxabicyclo[3.1.1]heptane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.00159
(1R,5S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-6-oxabicyclo[3.1.1]heptane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.00228
(1R,5S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-6-oxabicyclo[3.1.1]heptane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
0.0137
(1R,5S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-6-oxabicyclo[3.1.1]heptane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
0.00002
(2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide
Homo sapiens
mutant H843Y
0.0043
(2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide
Homo sapiens
wild type
0.000467
(2R)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.00129
(2R)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.00573
(2R)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
4
(2S)-2-(acetylamino)-3-[3-[(2S)-2-[[(2S)-2-ammonio-7-(hydroxyamino)-7-oxoheptanoyl]amino]-3-methoxy-3-oxopropyl]phenyl]propanoate
Homo sapiens
-
isoform HDAC1
8.1
(2S)-2-(acetylamino)-3-[3-[(2S)-2-[[(2S)-2-ammonio-7-(hydroxyamino)-7-oxoheptanoyl]amino]-3-methoxy-3-oxopropyl]phenyl]propanoate
Homo sapiens
-
HeLa cell nuclear extract
0.00143
(2S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.00145
(2S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.00595
(2S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
0.00011
(3S,15R,20aS)-15-methyl-3-[(1E)-4-sulfanylbut-1-en-1-yl]-3,4,6,7,14,15,18,19,20,20a-decahydro-1H,5H,16H-11,8:15,12-di(azeno)pyrrolo[2,1-c][1,8,12,4,15]oxadithiadiazacyclooctadecine-1,5,16-trione
Homo sapiens
-
0.00058
(3S,15R,20aS)-15-methyl-3-[(1E)-4-sulfanylbut-1-en-1-yl]-3,4,6,7,14,15,18,19,20,20a-decahydro-1H,5H,16H-11,8:15,12-di(azeno)pyrrolo[2,1-c][1,8,12,4,15]oxadithiadiazacyclooctadecine-1,5,16-trione
Homo sapiens
-
0.0008
(3S,15R,20aS)-15-methyl-3-[(1E)-4-sulfanylbut-1-en-1-yl]-3,4,6,7,14,15,18,19,20,20a-decahydro-1H,5H,16H-11,8:15,12-di(azeno)pyrrolo[2,1-c][1,8,12,4,15]oxadithiadiazacyclooctadecine-1,5,16-trione
Homo sapiens
-
0.013
(3S,15R,20aS)-15-methyl-3-[(1E)-4-sulfanylbut-1-en-1-yl]-3,4,6,7,14,15,18,19,20,20a-decahydro-1H,5H,16H-11,8:15,12-di(azeno)pyrrolo[2,1-c][1,8,12,4,15]oxadithiadiazacyclooctadecine-1,5,16-trione
Homo sapiens
-
0.0003
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
Homo sapiens
-
HDAC1
0.0004
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
Homo sapiens
-
HDAC10
0.0004
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
Homo sapiens
-
HDAC2
0.0004
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
Homo sapiens
-
HDAC9
0.0015
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
Homo sapiens
-
HDAC3
0.0028
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
Homo sapiens
-
HDAC5
0.01
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
Homo sapiens
-
HDAC4, larger than 0.010
0.01
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
Homo sapiens
-
HDAC6, larger than 0.010
0.01
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
Homo sapiens
-
HDAC7, larger than 0.010
0.01
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
Homo sapiens
-
HDAC8, larger than 0.010
0.000025
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC9
0.000028
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC10
0.00004
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC2
0.00005
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC1
0.00006
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC5
0.00055
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC3
0.002
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC8
0.01
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC4, larger than 0.010
0.01
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC6, larger than 0.010
0.01
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC7, larger than 0.010
0.00002
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC10
0.00003
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC2
0.00003
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC9
0.000035
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC1
0.00007
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC5
0.00015
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC3
0.0022
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC8
0.01
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC4, larger than 0.010
0.01
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC6, larger than 0.010
0.01
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
Homo sapiens
-
HDAC7, larger than 0.010
0.000012
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
Homo sapiens
-
HDAC1
0.000015
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
Homo sapiens
-
HDAC10
0.000022
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
Homo sapiens
-
HDAC9
0.00004
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
Homo sapiens
-
HDAC2
0.00005
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
Homo sapiens
-
HDAC5
0.00028
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
Homo sapiens
-
HDAC3
0.0015
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
Homo sapiens
-
HDAC8
0.01
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
Homo sapiens
-
HDAC4, larger than 0.010
0.01
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
Homo sapiens
-
HDAC6, larger than 0.010
0.01
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
Homo sapiens
-
HDAC7, larger than 0.010
0.00027
(4E)-N-(2-aminophenyl)-5-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]pent-4-enamide
Homo sapiens
-
0.0041
(4E)-N-(2-aminophenyl)-5-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]pent-4-enamide
Homo sapiens
-
0.03
(4E)-N-(2-aminophenyl)-5-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]pent-4-enamide
Homo sapiens
larger than 0.030
0.014
(5E)-N-(2-aminophenyl)-6-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]hex-5-enamide
Homo sapiens
-
0.023
(5E)-N-(2-aminophenyl)-6-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]hex-5-enamide
Homo sapiens
-
0.029
(5E)-N-(2-aminophenyl)-6-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]hex-5-enamide
Homo sapiens
-
0.03
(5E)-N-(2-aminophenyl)-6-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]hex-5-enamide
Homo sapiens
larger than 0.030
0.0000012
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.0000034
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.0000035
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.000049
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.00000032
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3-thia-7,14,20,21-tetraazatricyclo[14.3.1.1-2,5]henicosa-1(20),2(21),16,18-tetraene-6,9,13-trione
Homo sapiens
-
0.00000086
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3-thia-7,14,20,21-tetraazatricyclo[14.3.1.1-2,5]henicosa-1(20),2(21),16,18-tetraene-6,9,13-trione
Homo sapiens
-
0.0000011
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3-thia-7,14,20,21-tetraazatricyclo[14.3.1.1-2,5]henicosa-1(20),2(21),16,18-tetraene-6,9,13-trione
Homo sapiens
-
0.000029
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3-thia-7,14,20,21-tetraazatricyclo[14.3.1.1-2,5]henicosa-1(20),2(21),16,18-tetraene-6,9,13-trione
Homo sapiens
-
0.0000019
(5R,8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.0000038
(5R,8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.0000048
(5R,8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.00013
(5R,8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.0012
(5S,8R,11R)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.0019
(5S,8R,11R)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.0022
(5S,8R,11R)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.0031
(5S,8R,11R)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Homo sapiens
-
0.00000069
(5S,8S,11S,5'S,8'S,11'S)-11,11'-[disulfanediyldi(1E)but-1-ene-4,1-diyl]bis[5-methyl-8-(1-methylethyl)-3,10,17-trioxa-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione]
Homo sapiens
-
0.0000015
(5S,8S,11S,5'S,8'S,11'S)-11,11'-[disulfanediyldi(1E)but-1-ene-4,1-diyl]bis[5-methyl-8-(1-methylethyl)-3,10,17-trioxa-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione]
Homo sapiens
-
0.0000017
(5S,8S,11S,5'S,8'S,11'S)-11,11'-[disulfanediyldi(1E)but-1-ene-4,1-diyl]bis[5-methyl-8-(1-methylethyl)-3,10,17-trioxa-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione]
Homo sapiens
-
0.000045
(5S,8S,11S,5'S,8'S,11'S)-11,11'-[disulfanediyldi(1E)but-1-ene-4,1-diyl]bis[5-methyl-8-(1-methylethyl)-3,10,17-trioxa-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione]
Homo sapiens
-
0.000077
(8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),4,16(19)-tetraene-6,9,13-trione
Homo sapiens
-
0.000085
(8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),4,16(19)-tetraene-6,9,13-trione
Homo sapiens
-
0.00012
(8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),4,16(19)-tetraene-6,9,13-trione
Homo sapiens
-
0.03
(8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),4,16(19)-tetraene-6,9,13-trione
Homo sapiens
larger than 0.030
0.000035
(E)-3-[3-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]phenyl]-N-hydroxyacrylamide
Homo sapiens
-
recombinant HDAC3, pH not specified in the publication, temperature not specified in the publication
0.000047
(E)-3-[3-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]phenyl]-N-hydroxyacrylamide
Homo sapiens
-
recombinant HDAC1, pH not specified in the publication, temperature not specified in the publication
0.000066
(E)-3-[3-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]phenyl]-N-hydroxyacrylamide
Homo sapiens
-
recombinant HDAC6, pH not specified in the publication, temperature not specified in the publication
0.000086
(E)-3-[3-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]phenyl]-N-hydroxyacrylamide
Homo sapiens
-
recombinant HDAC8, pH not specified in the publication, temperature not specified in the publication
0.000037
1-[5-(2,3-dihydro-1,4-benzodioxin-6-yl)thiophen-2-yl]-2,2,2-trifluoroethanone
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.01
1-[5-(2,3-dihydro-1,4-benzodioxin-6-yl)thiophen-2-yl]-2,2,2-trifluoroethanone
Homo sapiens
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication
0.01
1-[5-(2,3-dihydro-1,4-benzodioxin-6-yl)thiophen-2-yl]-2,2,2-trifluoroethanone
Homo sapiens
-
IC50 above 0.01 mM, HDAC4, pH and temperature not specified in the publication
0.000029
1-[5-(4-acetylphenyl)thiophen-2-yl]-2,2,2-trifluoroethanone
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.01
1-[5-(4-acetylphenyl)thiophen-2-yl]-2,2,2-trifluoroethanone
Homo sapiens
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication
0.072
1-[5-(4-acetylphenyl)thiophen-2-yl]-2,2,2-trifluoroethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.00013
2,2,2-trifluoro-1-(2-phenyl-1,3-thiazol-5-yl)ethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.00021
2,2,2-trifluoro-1-(2-phenyl-1,3-thiazol-5-yl)ethanone
Homo sapiens
-
HDAC6 pH and temperature not specified in the publication
0.0037
2,2,2-trifluoro-1-(2-phenyl-1,3-thiazol-5-yl)ethanone
Homo sapiens
-
HDAC1, pH and temperature not specified in the publication
0.0019
2,2,2-trifluoro-1-(4-phenylthiophen-2-yl)ethanone
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.0032
2,2,2-trifluoro-1-(4-phenylthiophen-2-yl)ethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.01
2,2,2-trifluoro-1-(4-phenylthiophen-2-yl)ethanone
Homo sapiens
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication
0.00017
2,2,2-trifluoro-1-(5-phenylthiophen-2-yl)ethanone
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.0028
2,2,2-trifluoro-1-(5-phenylthiophen-2-yl)ethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.02
2,2,2-trifluoro-1-(5-phenylthiophen-2-yl)ethanone
Homo sapiens
-
IC50 above 0.02 mM, HDAC1, pH and temperature not specified in the publication
0.000024
2,2,2-trifluoro-1-(5-[3-[(methylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.00023
2,2,2-trifluoro-1-(5-[3-[(methylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.0027
2,2,2-trifluoro-1-(5-[3-[(methylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
Homo sapiens
-
HDAC1, pH and temperature not specified in the publication
0.00003
2,2,2-trifluoro-1-(5-[3-[(propylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.00024
2,2,2-trifluoro-1-(5-[3-[(propylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.0022
2,2,2-trifluoro-1-(5-[3-[(propylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
Homo sapiens
-
HDAC1, pH and temperature not specified in the publication
0.000035
2,2,2-trifluoro-1-(5-[3-[(thiophen-2-ylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.00052
2,2,2-trifluoro-1-(5-[3-[(thiophen-2-ylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.0039
2,2,2-trifluoro-1-(5-[3-[(thiophen-2-ylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
Homo sapiens
-
HDAC1, pH and temperature not specified in the publication
0.005
2,2,2-trifluoro-1-[5-(1H-indol-5-yl)thiophen-2-yl]ethanone
Homo sapiens
-
IC50 above 0.005 mM, HDAC6, pH and temperature not specified in the publication
0.01
2,2,2-trifluoro-1-[5-(1H-indol-5-yl)thiophen-2-yl]ethanone
Homo sapiens
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication
0.01
2,2,2-trifluoro-1-[5-(1H-indol-5-yl)thiophen-2-yl]ethanone
Homo sapiens
-
IC50 above 0.01 mM, HDAC4, pH and temperature not specified in the publication
0.0063
2,2,2-trifluoro-1-[5-(2-methoxyphenyl)thiophen-2-yl]ethanone
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.01
2,2,2-trifluoro-1-[5-(2-methoxyphenyl)thiophen-2-yl]ethanone
Homo sapiens
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication
0.01
2,2,2-trifluoro-1-[5-(2-methoxyphenyl)thiophen-2-yl]ethanone
Homo sapiens
-
IC50 above 0.01 mM, HDAC4, pH and temperature not specified in the publication
0.0031
2,2,2-trifluoro-1-[5-(3-methoxyphenyl)thiophen-2-yl]ethanone
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.0038
2,2,2-trifluoro-1-[5-(3-methoxyphenyl)thiophen-2-yl]ethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.01
2,2,2-trifluoro-1-[5-(3-methoxyphenyl)thiophen-2-yl]ethanone
Homo sapiens
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication
0.00006
2,2,2-trifluoro-1-[5-(3-[[(4-fluorobenzyl)sulfonyl]methyl]-1,2,4-oxadiazol-5-yl)thiophen-2-yl]ethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.0007
2,2,2-trifluoro-1-[5-(3-[[(4-fluorobenzyl)sulfonyl]methyl]-1,2,4-oxadiazol-5-yl)thiophen-2-yl]ethanone
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.0066
2,2,2-trifluoro-1-[5-(3-[[(4-fluorobenzyl)sulfonyl]methyl]-1,2,4-oxadiazol-5-yl)thiophen-2-yl]ethanone
Homo sapiens
-
HDAC1, pH and temperature not specified in the publication
0.00011
2,2,2-trifluoro-1-[5-(4-methoxyphenyl)thiophen-2-yl]ethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.001
2,2,2-trifluoro-1-[5-(4-methoxyphenyl)thiophen-2-yl]ethanone
Homo sapiens
-
IC50 above 0.001 mM, HDAC1, pH and temperature not specified in the publication
0.001
2,2,2-trifluoro-1-[5-(4-methoxyphenyl)thiophen-2-yl]ethanone
Homo sapiens
-
IC50 above 0.001 mM, HDAC6, pH and temperature not specified in the publication
0.00054
2,2,2-trifluoro-1-[5-(pyridin-2-yl)thiophen-2-yl]ethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.001
2,2,2-trifluoro-1-[5-(pyridin-2-yl)thiophen-2-yl]ethanone
Homo sapiens
-
IC50 above 0.001 mM, HDAC1, pH and temperature not specified in the publication
0.001
2,2,2-trifluoro-1-[5-(pyridin-2-yl)thiophen-2-yl]ethanone
Homo sapiens
-
IC50 above 0.001 mM, HDAC6, pH and temperature not specified in the publication
0.000015
2,2,2-trifluoro-1-[5-(quinoxalin-6-yl)thiophen-2-yl]ethanone
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.00016
2,2,2-trifluoro-1-[5-(quinoxalin-6-yl)thiophen-2-yl]ethanone
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.00091
2,2,2-trifluoro-1-[5-(quinoxalin-6-yl)thiophen-2-yl]ethanone
Homo sapiens
-
HDAC1, pH and temperature not specified in the publication
0.000026
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide
Homo sapiens
-
HDAC1
0.000048
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide
Homo sapiens
-
HDAC3
0.000059
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide
Homo sapiens
-
HDAC2
0.01
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide
Homo sapiens
-
HDAC5, larger than 0.010
0.01
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide
Homo sapiens
-
HDAC7, larger than 0.010
0.000059
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
Homo sapiens
-
HDAC1
0.00011
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
Homo sapiens
-
HDAC2
0.00012
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
Homo sapiens
-
HDAC3
0.00034
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
Homo sapiens
-
HDAC6
0.005
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
Homo sapiens
-
HDAC8, larger than 0.005
0.01
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
Homo sapiens
-
HDAC5, larger than 0.010
0.01
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
Homo sapiens
-
HDAC7, larger than 0.010
0.00007
3-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.00031
3-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.0128
3-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
Homo sapiens
-
HDAC1, pH and temperature not specified in the publication
0.00023
3-[5-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]furan-2-yl]-N-hydroxy-acrylamide
Homo sapiens
-
recombinant HDAC8, pH not specified in the publication, temperature not specified in the publication
0.00061
3-[5-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]furan-2-yl]-N-hydroxy-acrylamide
Homo sapiens
-
recombinant HDAC3, pH not specified in the publication, temperature not specified in the publication
0.00063
3-[5-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]furan-2-yl]-N-hydroxy-acrylamide
Homo sapiens
-
recombinant HDAC1, pH not specified in the publication, temperature not specified in the publication
0.0063
3-[5-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]furan-2-yl]-N-hydroxy-acrylamide
Homo sapiens
-
recombinant HDAC6, pH not specified in the publication, temperature not specified in the publication
0.000027
4-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.0025
4-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
Homo sapiens
-
HDAC1, pH and temperature not specified in the publication
0.074
4-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.000041
4-[5-(trifluoroacetyl)thiophen-2-yl]benzonitrile
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.00016
4-[5-(trifluoroacetyl)thiophen-2-yl]benzonitrile
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.0027
4-[5-(trifluoroacetyl)thiophen-2-yl]benzonitrile
Homo sapiens
-
HDAC1, pH and temperature not specified in the publication
0.0001
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
Homo sapiens
-
HDAC1
0.0002
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
Homo sapiens
-
HDAC2
0.00028
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
Homo sapiens
-
HDAC10
0.00055
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
Homo sapiens
-
HDAC9
0.0006
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
Homo sapiens
-
HDAC3
0.0007
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
Homo sapiens
-
HDAC5
0.0023
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
Homo sapiens
-
HDAC6
0.0023
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
Homo sapiens
-
HDAC8
0.01
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
Homo sapiens
-
HDAC4, larger than 0.010
0.01
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
Homo sapiens
-
HDAC7, larger than 0.010
0.000046
methyl (3R,6R,9R)-9-(acetylamino)-6-[6-(hydroxyamino)-6-oxohexyl]-5,8-dioxo-4,7-diazabicyclo[9.3.1]pentadeca-1(15),11,13-triene-3-carboxylate
Homo sapiens
-
HeLa cell nuclear extract
0.000057
methyl (3R,6R,9R)-9-(acetylamino)-6-[6-(hydroxyamino)-6-oxohexyl]-5,8-dioxo-4,7-diazabicyclo[9.3.1]pentadeca-1(15),11,13-triene-3-carboxylate
Homo sapiens
-
isoform HDAC1
0.231
methyl (3R,6R,9R)-9-(acetylamino)-6-[6-(hydroxyamino)-6-oxohexyl]-5,8-dioxo-4,7-diazabicyclo[9.3.1]pentadeca-1(15),11,13-triene-3-carboxylate
Homo sapiens
-
isoform HDAC8
0.000167
methyl N-[(2S)-2-[(N-acetyl-L-alanyl)amino]-7-(hydroxyamino)-7-oxoheptanoyl]-L-phenylalaninate
Homo sapiens
-
HeLa cell nuclear extract
0.000174
methyl N-[(2S)-2-[(N-acetyl-L-alanyl)amino]-7-(hydroxyamino)-7-oxoheptanoyl]-L-phenylalaninate
Homo sapiens
-
isoform HDAC1
0.00967
N-(4-amino-3'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.0123
N-(4-amino-3'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.033
N-(4-amino-3'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, above, HDAC3 isozyme
0.00152
N-(4-amino-4'-chloro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.00253
N-(4-amino-4'-chloro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.0142
N-(4-amino-4'-chloro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
0.000045
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-1H-2-benzopyran-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.000119
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-1H-2-benzopyran-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.0259
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-1H-2-benzopyran-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
0.000072
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.000156
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.033
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-2H-1-benzopyran-3-carboxamide
Homo sapiens
pH 7.4, 22°C, above, HDAC3 isozyme
0.000123
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3-oxabicyclo[3.1.0]hexane-6-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.000219
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3-oxabicyclo[3.1.0]hexane-6-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.00149
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3-oxabicyclo[3.1.0]hexane-6-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
0.00122
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.00473
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.00559
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.00626
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
0.00656
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.0198
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-3-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
0.00002
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.000062
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.00109
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
0.000119
N-(4-amino[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.000312
N-(4-amino[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.00385
N-(4-amino[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
0.000044
N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
Homo sapiens
isoform HDAC3
0.000086
N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
Homo sapiens
isoform HDAC1
0.000175
N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
Homo sapiens
isoform HDAC8
0.0000002
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
Homo sapiens
-
HDAC10
0.0000006
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
Homo sapiens
-
HDAC9
0.0000015
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
Homo sapiens
-
HDAC1
0.0000025
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
Homo sapiens
-
HDAC5
0.000005
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
Homo sapiens
-
HDAC2
0.000025
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
Homo sapiens
-
HDAC3
0.00003
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
Homo sapiens
-
HDAC6
0.00012
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
Homo sapiens
-
HDAC8
0.01
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
Homo sapiens
-
HDAC4, larger than 0.010
0.01
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
Homo sapiens
-
HDAC7, larger than 0.010
0.0000006
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
Homo sapiens
-
HDAC1
0.0000035
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
Homo sapiens
-
HDAC2
0.000035
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
Homo sapiens
-
HDAC3
0.000035
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
Homo sapiens
-
HDAC6
0.00018
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
Homo sapiens
-
HDAC8
0.01
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
Homo sapiens
-
HDAC4, larger than 0.010
0.01
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
Homo sapiens
-
HDAC7, larger than 0.010
0.000089
N-methyl-N-(quinoxalin-6-ylmethyl)-5-(trifluoroacetyl)thiophene-2-carboxamide
Homo sapiens
-
HDAC6, pH and temperature not specified in the publication
0.000098
N-methyl-N-(quinoxalin-6-ylmethyl)-5-(trifluoroacetyl)thiophene-2-carboxamide
Homo sapiens
-
HDAC4, pH and temperature not specified in the publication
0.00058
N-methyl-N-(quinoxalin-6-ylmethyl)-5-(trifluoroacetyl)thiophene-2-carboxamide
Homo sapiens
-
HDAC1, pH and temperature not specified in the publication
0.00067
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
Homo sapiens
-
HDAC1
0.00088
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
Homo sapiens
-
HDAC2
0.00097
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
Homo sapiens
-
HDAC6
0.001
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
Homo sapiens
-
HDAC3
0.01
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
Homo sapiens
-
HDAC5, larger than 0.010
0.01
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
Homo sapiens
-
HDAC7, larger than 0.010
0.01
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
Homo sapiens
-
HDAC8, larger than 0.010
0.00067
N-[(2E)-3-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]prop-2-en-1-yl]-2-sulfanylacetamide
Homo sapiens
-
0.0007
N-[(2E)-3-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]prop-2-en-1-yl]-2-sulfanylacetamide
Homo sapiens
-
0.00096
N-[(2E)-3-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]prop-2-en-1-yl]-2-sulfanylacetamide
Homo sapiens
-
0.0016
N-[(2E)-3-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]prop-2-en-1-yl]-2-sulfanylacetamide
Homo sapiens
-
0.00024
N-[(3E)-4-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]but-3-en-1-yl]-2-sulfanylacetamide
Homo sapiens
-
0.001
N-[(3E)-4-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]but-3-en-1-yl]-2-sulfanylacetamide
Homo sapiens
-
0.0015
N-[(3E)-4-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]but-3-en-1-yl]-2-sulfanylacetamide
Homo sapiens
-
0.0019
N-[(3E)-4-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]but-3-en-1-yl]-2-sulfanylacetamide
Homo sapiens
-
0.00645
N-[2-amino-5-(pyridin-3-yl)phenyl]oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.00732
N-[2-amino-5-(pyridin-3-yl)phenyl]oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.0208
N-[2-amino-5-(pyridin-3-yl)phenyl]oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC3 isozyme
0.00142
N-[2-amino-5-(pyridin-4-yl)phenyl]oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC2 isozyme
0.00235
N-[2-amino-5-(pyridin-4-yl)phenyl]oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.033
N-[2-amino-5-(pyridin-4-yl)phenyl]oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, above, HDAC3 isozyme
0.0267
N-[4-amino-4'-(trifluoromethyl)[1,1'-biphenyl]-3-yl]oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.033
N-[4-amino-4'-(trifluoromethyl)[1,1'-biphenyl]-3-yl]oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, above, HDAC2 isozyme
0.033
N-[4-amino-4'-(trifluoromethyl)[1,1'-biphenyl]-3-yl]oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, above, HDAC3 isozyme
0.000185
pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
Homo sapiens
isoform HDAC1
0.000201
pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
Homo sapiens
isoform HDAC3
0.01
pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
Homo sapiens
isoform HDAC8
0.00015
suberoylanilide hydroxamic acid
Homo sapiens
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37°C, pH not specified in the publication
0.000022
trichostatin A
Homo sapiens
-
HDAC activity in HeLa nuclear cell extracts, 25°C, pH 8.0
0.008
trichostatin A
Homo sapiens
-
recombinant HDAC3 in complex with CoR1, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54.1
induced Escherichia coli cells expressing the recombinant enzyme, pH 7.6, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.98
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
5.04
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
5.06
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
5.22
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
5.24
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
5.25
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
5.26
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
5.28
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
5.3
5.35
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
5.44
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
5.91
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
6.09
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
6.29
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
6.31
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
7.39
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
8.88
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
5.3
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
sequence calculation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
UniProt
brenda
isoform HdaA, major part of total histone deacetylase activity is due to HdaA
SwissProt
brenda
-
711764, 711850, 711956, 712181, 712402, 712434, 712485, 712691, 713009, 713036, 713087, 713157, 713181, 713487, 718758, 719058, 719061, 719092, 719095, 719304, 719441, 719941, 720187, 720815
-
-
brenda
isoform HDAC6, contains two potentially functional catalytic domains
SwissProt
brenda
isoform HDAC7, class II enzyme, and isoform HDAC3, class I enzyme
SwissProt
brenda
isoform HDAC9, class II enzyme with several alternatively spliced isoforms
SwissProt
brenda
histone deacetylase HD2 isoform 1; cultivars Caresse and Ippolytos
UniProt
brenda
histone deacetylase HD2 isoform 2; cultivars Caresse and Ippolytos
UniProt
brenda
sake strain Kyokai No 701 and diverse deletion mutants
UniProt
brenda
sake strain Kyokai No 701 and diverse deletion mutants
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
of 5-day-old plants
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
of 5-day-old plants
brenda
expressed in gametocytes and mature blood stages of the malaria parasite life cycle
brenda
additional information
-
atlas on distribution of eleven histone deacetylase isoforms in the brain
brenda
expression levels of enzyme isoforms differ during early embryo germination
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
young
brenda
-
-
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
of 5-day-old plants
brenda
-
K562 erythroleukemia cells treated with the HbF inducers hemin, trichostatin A, and sodium butanoate have significantly reduced mRNA levels of HDAC9 and its splice variant histone deacetylase-related protein
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
of 14-day-old plants
brenda
-
in liver, class IIa HDACs HDAC4, 5, and 7, are phosphorylated and excluded from the nucleus by AMPK family kinases. In response to the fasting hormone glucagon, these HDACs are rapidly dephosphorylated and translocated to the nucleus where they associate with the promoters of gluconeogenic enzymes such as G6Pase. In turn, HDAC4/5 recruit HDAC3, which results in the acute transcriptional induction of these genes via deacetylation and activation of FOXO family transcription factors. Loss of class IIa HDACs in murine liver results in inhibition of FOXO target genes and lowers blood glucose, resulting in increased glycogen storage
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
of 5-day-old plants
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
-
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
-
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
of 14-day-old plants
brenda
class I and class IIa histone deacetylases (HDACs) are overexpressed in non-type and basal human bladder cancer (BC) cell lines at the mRNA level, overview
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class I and class IIa histone deacetylases (HDACs) are overexpressed in non-type and basal human bladder cancer cell lines at the mRNA level, overview. Basal-squamous bladder cancer (BC) clinical samples are enriched for histone deacetylase (HDAC)4 and HDAC9 expression. Histone deacetylase (HDAC4) and HDAC9 expression co-clusters with basal markers in muscle-invasive bladder cancer
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additional information
tissue dependent expression level of enzyme AhHDA1, overview
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additional information
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tissue dependent expression level of enzyme AhHDA1, overview
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
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additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
-
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2. Real-time quantitative PCR tissue distribution analysis, differential expression across various tissues
brenda
additional information
isoform HDAC10 is expressed in most of the cancer cells examined
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additional information
quantitative real-time PCR enzyme expression analysis, high expression of class IIa HDACs in non-type and basal molecular subtype groupings of human BC cells
brenda
additional information
quantitative real-time PCR enzyme expression analysis, high expression of class IIa HDACs in non-type and basal molecular subtype groupings of human BC cells
brenda
additional information
quantitative real-time PCR enzyme expression analysis, high expression of class IIa HDACs in non-type and basal molecular subtype groupings of human BC cells
brenda
additional information
-
quantitative real-time PCR enzyme expression analysis, high expression of class IIa HDACs in non-type and basal molecular subtype groupings of human BC cells
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA13
brenda
additional information
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA10
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA14
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA16
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA3
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA8
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA1
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA10
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA11
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA12
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA13
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA14
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA15
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA17
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA18
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA2
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA3
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA4
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA5
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA6
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA9
brenda
enrichment of enzyme is cytoplasm is not sensitive to leptomycin B
brenda
shuttling of isoform HDAC7 between cytoplasm and nucleus. Catalytic activity of HDAC7 requires interaction with isoform HDAC3 in the nucleus
brenda
depending on phosphorylation status
brenda
-
cytoplasmic expression of HDAC1, 2 and 3 is significantly increased in carcinomas compared with benign tumors
brenda
-
subcellular localization of the class II HDACs 4, 5, and 7 is regulated by phosphorylation-dependent shuttling between the cytoplasmic and nuclear compartments
brenda
-
Set3C is a conserved nuclear complex, Set3 interacts with Hos2, immunohistochemic subcellular localization analysis, overview
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA1
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA11
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA12
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA15
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA16
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA17
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA18
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA2
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA5
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA6
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA7
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA8
brenda
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
isozyme GmHDA9
brenda
predominant localization of isoform HDAC7, which shuttles between cytoplasm and nucleus. Catalytic activity of HDAC7 requires interaction with isoform HDAC3 in the nucleus
brenda
depending on phosphorylation status
brenda
-
isozymes HDACs 1 and 2 are exclusively localized in the nucleus
brenda
additional information
isoform AtHD1 is excluded from the nucleolus
-
brenda
additional information
-
isoform AtHD1 is excluded from the nucleolus
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
additional information
-
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
GmHDACs fall into three major groups previously named RPD3/HDA1, SIR2, and HD2, phylogenetic analysis. Chromosomal localization and duplications of HDAC genes in soybean, overview
evolution
histone deacetylase 8 (HDAC8) is a member of the class I acetyl-lysine deacetylase (HDAC) family
evolution
human histone deacetylases belong to all three known classes, class I: HDAC1, HDAC2, HDAC3, HDAC8, class II: HDAC4, HDAC5, HDAC6, HDAC7, HDAC9, HDAC10, and class III: HDAC11
evolution
the enzyme belongs to the histone deacetylase (HDAC) superfamily
evolution
the enzyme belongs to the RPD3/HDA1-like superfamily of histone deacetylases (HDACs)
evolution
the protruded arm regions are conserved among the Hda1 homologies, and residues Ile512, Ile523 and Leu525 that play key role in the domain-domain interaction are relatively conserved. The ARB2 domain of Hda1 shows structural similarity to the alpha/beta fold hydrolases
evolution
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the enzyme belongs to the histone deacetylase (HDAC) superfamily
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evolution
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the enzyme belongs to the histone deacetylase (HDAC) superfamily
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evolution
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the enzyme belongs to the histone deacetylase (HDAC) superfamily
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evolution
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the enzyme belongs to the histone deacetylase (HDAC) superfamily
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evolution
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the enzyme belongs to the histone deacetylase (HDAC) superfamily
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evolution
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the enzyme belongs to the histone deacetylase (HDAC) superfamily
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evolution
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the protruded arm regions are conserved among the Hda1 homologies, and residues Ile512, Ile523 and Leu525 that play key role in the domain-domain interaction are relatively conserved. The ARB2 domain of Hda1 shows structural similarity to the alpha/beta fold hydrolases
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evolution
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the enzyme belongs to the histone deacetylase (HDAC) superfamily
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malfunction
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alkylation (carbonylation) of conserved cysteine residues in HDAC1, -2 and -3 antagonizes their deacetylase activity and transcriptional co-repressor function
malfunction
down-regulation of HDAC gene HDA710 induces a semi-dwarf phenotype, down-regulation of HDAC gene HDA704 affects plant height and flag leaf development
malfunction
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down-regulation of HDAC gene HDA710 induces a semi-dwarf phenotype, down-regulation of HDAC gene HDA704 affects plant height and flag leaf development
malfunction
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HDAC inhibition improves DELTAF508 cystic fibrosis transmembrane conductance regulator stability and trafficking, silencing of HDAC2 and HDAC3 causes a 2.5fold and 1.5fold increase in DELTAF508 cystic fibrosis transmembrane conductance regulator mRNA, respectively, as well as an about 5fold increase in total DELTAF508 protein. Silencing of HDAC1 induces a 1.4fold stimulation of iodide efflux. In contrast, silencing of HDAC7 exhibits a 3.6fold stimulation of cAMP-mediated iodide efflux comparable to 30°C efflux
malfunction
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HDAC1 and HDAC2 with carboxy-terminal domains deleted, retain enzymatic activity but are unable to repress cartilage gene expression
malfunction
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HDAC7 knockdown causes increased nuclear beta-catenin, decreased transcription of HDAC7, decreased expression of E2F2, cyclin-D1 and cyclin-E2, and increased retinoblastoma protein
malfunction
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inhibition of histone deacetylase activity down-regulates urokinase plasminogen activator and matrix metalloproteinase-9 expression in gastric cancer
malfunction
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inhibition of SIRT1 activity leads to a recovery from the intrinsic repressive activity of orphan nuclear receptor small heterodimer partner (SHP) but not of DAX1. Inhibition of SIRT1 significantly diminishes the repressive effect of SHP on liver receptor homolog 1 transactivity. Inhibition of SIRT1 activity significantly reverses SHP-mediated inhibition of bile-acid synthesis by liver receptor homolog 1 overexpression
malfunction
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knockdown of HDAC1 can generate a remarkable defect in proliferation and also can significantly induce apoptosis and S-phase arrest in PaTu-8988 cells
malfunction
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knockdown of HDAC10 significantly increases the mRNA expression levels of thioredoxin-interacting protein and induces release of cytochrome c and activated apoptotic signaling molecules through accumulation of reactive oxygen species in SNU-620 human gastric cancer cells
malfunction
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short hairpin-RNA silencing of either HDAC2 or HDAC4 is sufficient to induce p21 expression
malfunction
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suppression of HDAC3 reduces the migration and induces the expression of E-cadherin in ovarian cancer cells
malfunction
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while brain development and adult stem cell fate are normal upon conditional deletion of HDAC2 or in mice lacking the catalytic activity of HDAC2, neurons derived from both zones of adult neurogenesis die at a specific maturation stage
malfunction
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deletion of Hos2, the catalytic subunit of the Set3 complex, produces a phenotype resembling inhibition of the Set3C by trichostatin-A
malfunction
depleting maternal isozyme HDAC2 results in hyperacetylation of H4K16, while normal deacetylation of other lysine residues of histone H3 or H4 is observed, and defective chromosome condensation and segregation during oocyte maturation occurs in a subpopulation of oocytes, leading to increased incidence of aneuploidy likely accounts for the observed sub-fertility of mice harboring Hdac2-defective oocytes. The infertility of mice harboring Hdac1-/+/Hdac2-/- oocytes is attributed to failure of those few eggs that properly mature to metaphase II to initiate DNA replication following fertilization. Hdac1-/+/Hdac2-/- eggs are fertilized but fail to initiate DNA replication. The increased amount of acetylated H4K16 likely impairs kinetochore function in oocytes lacking isozyme HDAC2 because kinetochores in mutant oocytes are less able to form coldstable microtubule attachments and less CENP-A is located at the centromere. Phenotype, overview
malfunction
hda9 and hda19 mutants show a warm-temperature-insensitive phenotype at 27°C, whereas hda15 plants displays a constitutive warm-temperature-induced phenotype at 20°C and an enhanced thermal response at 27°C. Hda9 mutation leads to differential expression of a large number of genes at 20°C and impaired induction of warm-temperature-responsive genes at 27°C. The hda15-1, hda9-1, hda9-2 and hda19 mutants display distinct hypocotyl elongation phenotypes at 20°C and 27°C under short-day conditions
malfunction
hda9 and hda19 mutants show a warm-temperature-insensitive phenotype at 27°C, whereas hda15 plants displays a constitutive warm-temperature-induced phenotype at 20°C and an enhanced thermal response at 27°C. The hda19 mutation leads to upregulation of genes mostly related to stress response at both 20°C and 27°C. The hda15-1, hda9-1, hda9-2 and hda19 mutants display distinct hypocotyl elongation phenotypes at 20°C and 27°C under short-day conditions
malfunction
histone deacetylase 7 (HDAC7) controls the thymic effector programming of natural killer T (NKT) cells, and interference with this function contributes to tissue-specific autoimmunity. Gain of HDAC7 function in thymocytes blocks both negative selection and NKT development, and diverts Va14/Ja18 TCR transgenic thymocytes into a Tconv-like lineage. Conversely, HDAC7 deletion promotes thymocyte apoptosis and causes expansion of innate-effector cells, mechanisms, overview. A mutation in HDAC7 can create problems only for specific organs in the body. In humans, mutations in HDAC7 are also associated with autoimmune disorders of the digestive tract and liver. These include inflammatory bowel diseases such as ulcerative colitis or Crohn's disease. Alteration of HDAC7 function dysregulates thymic innate effector programming and interferes with iNKT development
malfunction
histone deacetylase 7 (HDAC7) controls the thymic effector programming of natural killer T (NKT) cells, and interference with this function contributes to tissue-specific autoimmunity. Gain of HDAC7 function in thymocytes blocks both negative selection and NKT development, and diverts Va14/Ja18 TCR transgenic thymocytes into a Tconv-like lineage. Conversely, HDAC7 deletion promotes thymocyte apoptosis and causes expansion of innate-effector cells, mechanisms, overview. Alteration of HDAC7 function dysregulates thymic innate effector programming and interferes with iNKT development. While the wild-type-derived population reconstitutes hepatic iNKT cells efficiently, HDAC7-DELTAP bone marrow makes almost no contribution to this compartment in the liver, where iNKT cells are most abundant. This is also true in the thymus and spleen, demonstrating that the abnormalities observed in the intact transgenic mice are due to a cell-autonomous mechanism. Analysis of effects of loss of HDAC7 in the thymus on these phenotypes. Deletion of Hdac7 does not result in expansion of NK1.1-expressing T-cells, but significant abnormalities in the effector programming of non-tetramer-reactive thymocytes are observed
malfunction
K701 rpd3DELTA and K701 hda1DELTA alter the response to oxygen of isoamyl acetate production
malfunction
knockdown of HDT1/2 (hdt1,2i) results in an earlier switch and causes a reduced root meristem cell number. Overexpression of GA2ox2 in the RM phenocopies the hdt1,2i phenotype. Conversely, knockout of GA2ox2 partially rescues the root growth defect of hdt1,2i. The hdt1,2i-1 root tip has a gibberellin-deficient phenotype
malfunction
perturbation of the dimer interface abolishes the histone binding ability of the ARB2 domain
malfunction
RNAi-mediated HDAC1 knockdown in Gnatocerus cornutus larvae causes specific curtailment of mandibles in adults, whereas HDAC3 knockdown leads to hypertrophy. These knockdowns confer opposite effects on wing size, but little effect on the size of the core body and genital modules. PcG RNAi also reduces adult mandible size. Phenotypes, overview
malfunction
the hda15 mutation results in upregulation of many warm temperature-responsive as well as metabolic genes at 20°C and 27°C. HDA15 is associated with thermosensory mark genes at 20°C. That the association is decreased after shifting to 27°. In addition, the hda15 mutation also leads to upregulation of many metabolic genes and accumulation of primary metabolites. The hda15-1, hda9-1, hda9-2 and hda19 mutants display distinct hypocotyl elongation phenotypes at 20°C and 27°C under short-day conditions. Additive effects of the hda15-1/hfr1 double mutations on the hypocotyl and petiole lengths
malfunction
transcript levels of ILV2, ILV3 and ILV5 are elevated in Rpd3L-deficient strains (rpd3DELTA, ume1DELTA, dep1DELTA, and sds3DELTA) but not in Rpd3S-single deficient strain (rco1DELTA and eaf3DELTA) compared to wild-type K701. The transcript levels of ATF2, a minor alcohol acetyltransferase, are higher in the rpd3DELTA and ume1DELTA strains than in the parental strain. K701 rpd3DELTA and K701 hda1DELTA alter the response to oxygen of isoamyl acetate production
malfunction
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histone deacetylase 7 (HDAC7) controls the thymic effector programming of natural killer T (NKT) cells, and interference with this function contributes to tissue-specific autoimmunity. Gain of HDAC7 function in thymocytes blocks both negative selection and NKT development, and diverts Va14/Ja18 TCR transgenic thymocytes into a Tconv-like lineage. Conversely, HDAC7 deletion promotes thymocyte apoptosis and causes expansion of innate-effector cells, mechanisms, overview. Alteration of HDAC7 function dysregulates thymic innate effector programming and interferes with iNKT development. While the wild-type-derived population reconstitutes hepatic iNKT cells efficiently, HDAC7-DELTAP bone marrow makes almost no contribution to this compartment in the liver, where iNKT cells are most abundant. This is also true in the thymus and spleen, demonstrating that the abnormalities observed in the intact transgenic mice are due to a cell-autonomous mechanism. Analysis of effects of loss of HDAC7 in the thymus on these phenotypes. Deletion of Hdac7 does not result in expansion of NK1.1-expressing T-cells, but significant abnormalities in the effector programming of non-tetramer-reactive thymocytes are observed
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malfunction
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transcript levels of ILV2, ILV3 and ILV5 are elevated in Rpd3L-deficient strains (rpd3DELTA, ume1DELTA, dep1DELTA, and sds3DELTA) but not in Rpd3S-single deficient strain (rco1DELTA and eaf3DELTA) compared to wild-type K701. The transcript levels of ATF2, a minor alcohol acetyltransferase, are higher in the rpd3DELTA and ume1DELTA strains than in the parental strain. K701 rpd3DELTA and K701 hda1DELTA alter the response to oxygen of isoamyl acetate production
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malfunction
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perturbation of the dimer interface abolishes the histone binding ability of the ARB2 domain
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malfunction
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K701 rpd3DELTA and K701 hda1DELTA alter the response to oxygen of isoamyl acetate production
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malfunction
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deletion of Hos2, the catalytic subunit of the Set3 complex, produces a phenotype resembling inhibition of the Set3C by trichostatin-A
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metabolism
nitrative/oxidative stress reduce HDAC2 expression via nitration of distinct tyrosine residues. Peroxynitrite, hydrogen peroxide and cigarette smoke-conditioned medium reduce HDAC2 expression in A549 epithelial cells in vitro. This reduction is due to increased proteasomal degradation following ubiquitination rather than reduction of mRNA expression or stability
metabolism
epigenetic modifications including DNA methylation and histone post-translational modifications are closely associated with bladder cancer (BC) initiation and development, some HDACs play roles in the tumorigenicity of bladder cancer, overview. HDAC4 and HDAC9 expression is inversely correlated with Forkhead Box A1 (FOXA1), an important transcription factor in maintaining urothelial differentiation, and peroxisome proliferator-activated receptor gamma (PPARG), a steroid hormone receptor known for its oncogenic role in the development of BC
metabolism
epigenetic modifications including DNA methylation and histone post-translational modifications are closely associated with bladder cancer initiation and development, some HDACs play roles in the tumorigenicity of bladder cancer, overview
metabolism
metabolite profiling, mass spectrometric analysis
metabolism
two Arabidopsis thaliana paralogues encoding plant-specific histone deacetylases, HDT1 and HDT2, regulate a second switch from transit-amplifying cells to expanding cells
physiological function
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regulator of cellular pathways like response to stress, protein folding, microtubule stability and cell migration
physiological function
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ectopic overexpression of HDAC6 isotype increases the levels of phosphorylated epidermal growth factor receptor and phosphorylated AKT expression. HDAC6 plays an important role in the modulation of radiation response of epidermal growth factor receptor and human epidermal growth factor receptor 2-activated cells
physiological function
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HDAC catalyze the removal of acetyl groups from core histones inducing local condensation of chromatin. Therefore, HDACs are generally considered repressors of transcription. Coiled-coil domain-containing protein 6 physically interacts with HDAC1 on the amphiregulin promoter. Coiled-coil domain-containing protein 6 requires HDAC1 activity to repress cAMP responsive element binding protein 1 target gene transcription
physiological function
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HDAC1 and HDAC2 repress aggrecan and collagen 2(alpha1) expression but differ in their repression of collagen 9(alpha1), collagen 11(alpha1), dermatopontin, and cartilage oligomeric matrix protein. Carboxy-terminal domains of HDAC1 and HDAC2 are not required for enzymatic activity in vitro but are required for optimal deacetylation in vivo and repression of cartilage-specific gene expression
physiological function
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HDAC1 enhances cell proliferation of ovarian cancer cells, the expression of HDAC1 and HDAC2 is correlated with the proliferation marker Ki-67 expression, and HDAC3 stimulates cell migration with downregulation of E-cadherin in ovarian carcinoma
physiological function
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HDAC10 is involved in transcriptional downregulation of thioredoxin-interacting protein, leading to altered reactive oxygen species signaling in human gastric cancer cells
physiological function
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HDAC2 and HDAC1 are required for glucocorticoid receptor-mediated gene activation. HDAC2, however, is regulated through a different mechanism from that of HDAC1. Acetylated HDAC1 can trans-regulate HDAC2 through heterodimerization. Both HDAC1 and HDAC2 are required for mouse mammary tumor virus transcription
physiological function
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HDAC6 is necessary for protein aggregate formation and degradation
physiological function
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HDAC6 mediates TGF-beta1-induced epithelial-mesenchymal transition in A-549 cells. Splicing variant HDAC6p114 is required for TGF-beta1-activated gene expression associated with epithelial-mesenchymal transition in A-549 cells
physiological function
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HDAC7 overexpression has the ability to trump vascular endothelial growth factor signaling to inhibit endothelial cell proliferation, overexpression of HDAC7 leads to decreased nuclear beta-catenin and decreased activity of beta-catenin-dependent effectors and an associated inhibition of endothelial cell proliferation
physiological function
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HDAC7 plays a central role in restoration of DELTAF508 cystic fibrosis transmembrane conductance regulator function
physiological function
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HDACs regulate hepatocyte growth factor-induced urokinase plasminogen activator and matrix metalloproteinase-9 expression through a protein kinase C-dependent signal pathway in gastric cancer cells
physiological function
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orphan nuclear receptor small heterodimer partner (SHP) interacts and co-localizes specifically with SIRT1 in vivo. SHP recruits SIRT1 on liver receptor homolog 1 target gene promoters and SIRT1 deacetylates template-dependent histone H3 and H4 to inhibit transcription of liver receptor homolog 1 target genes
physiological function
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SIRT6 is a site-specific histone deacetylase that regulates chromatin structure. SIRT6 is implicated in fundamental biological processes in aging, including maintaining telomere integrity, fine-tuning aging-associated gene expression programs, preventing genomic instability, and maintaining metabolic homeostasis. The N-terminal extension of SIRT6 is critical for chromatin association and intrinsic catalytic activity
physiological function
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the catalytic function of HDAC2 is required in adult but not embryonic neurogenesis. HDAC2 is critically required to silence progenitor transcripts during neuronal differentiation of adult generated neurons
physiological function
the HDAC gene HDA703 is involved in histone H4 acetylation in rice, HDAC gene HDA703 has a function during plant reproductive development and seed morphology, HDA702/HDAC1 and HDA710 play a similar but important role in root and vegetative growth
physiological function
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the HDAC gene HDA703 is involved in histone H4 acetylation in rice, HDAC gene HDA703 has a function during plant reproductive development and seed morphology, HDA702/HDAC1 and HDA710 play a similar but important role in root and vegetative growth
physiological function
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the HDAC1 overexpression plays an important role in tumorigenesis of pancreatic cancer
physiological function
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activity of histone deacetylases influences splice site selection. Splicing of 700 genes in heLa cells is altered after HDAC inhibition. HDAC inhibition induces histone H4 acetylation and increases RNA Polymerase II processivity along an alternatively spliced element. In addition, HDAC inhibition reduces co-transcriptional association of the splicing regulator SRp40 with the target fibronectin exon. The depletion of HDAC1 has similar effect on fibronectin alternative splicing as global HDAC inhibition. This effect is reversed upon expression of mouse HDAC1 but not a catalytically inactive mutant
physiological function
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embryos injected with mRNA encoding a dominant-negative form of histone deacetylase lacked expression of gene Nodal related, Nr1, and exhibit randomized sidedness of the heart and viscera at stage 45. Pharmacological blockade of HDACs implicates cleavage stages as the active period. Inhibition during these early stages is correlated with an absence of Nr1 expression at stage 21, high levels of heterotaxia at stage 45, and the deposition of the epigenetic marker H3K4me2 on the Nr1 gene. The known HDAC partner protein Mad3 is a 5HT-binding regulator. While Mad3 overexpression leads to an absence of Nr1 transcription and randomizes the left-right axis, a mutant form of Mad3 lacking 5HT binding sites is not able to induce heterotaxia
physiological function
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HDAC9 gene knockdown produces dose-dependent gamma-globin gene silencing over an 80-320 nM range. Enforced expression of HDAC9 produces a dose-dependent 2.5fold increase in gammaglobin mRNA. HDAC9 binds in vivo in the upstream Ggamma-globin gene promoter region. Treatment of primary erythroid progenitors with HDAC9 siRNA results in 40 and 60% gamma-globin gene silencing in day 11 (early) and day 28 (late) progenitors, respectively. Enforced HDAC9 expression increases gamma-globin mRNA levels by 2.5fold with a simultaneous 7fold increase in fetal hemoglobin
physiological function
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in liver, class IIa HDACs HDAC4, 5, and 7, are phosphorylated and excluded from the nucleus by AMPK family kinases. In response to the fasting hormone glucagon, these HDACs are rapidly dephosphorylated and translocated to the nucleus where they associate with the promoters of gluconeogenic enzymes such as G6Pase. In turn, HDAC4/5 recruit HDAC3, which results in the acute transcriptional induction of these genes via deacetylation and activation of FOXO family transcription factors. Loss of class IIa HDACs in murine liver results in inhibition of FOXO target genes and lowers blood glucose, resulting in increased glycogen storage
physiological function
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Lysine-specific demethylase 1 has a repressive role in proinflammatory cytokine expression such as IL1alpha, IL1b,eta IL6 and IL8 and classical complement components. HDAC1 and lysine-specific demethylase 1 synergistically regulate these inflammatory-related genes
physiological function
mutation of HDA-1 by repeat-induced point mutation causes partial loss of DNA methylation. The site-specific loss of DNA methylation in hda-1 correlates with loss of H3 lysine 9 trimethylation and increased H3 acetylation. In addition, an increase in H2B acetylation is observed by two-dimensional gel electrophoresis of histones of the hda-1 mutant
physiological function
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role for Clr6 in transcriptional regulation of amino acid permease gene per1. When ammonia is used as the nitrogen source, low levels of per1 are transcribed and histones in the coding and surrounding regions of per1 are acetylated. In the presence of proline, histones at per1 are deacetylated in a Clr6-dependent manner
physiological function
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simultaneous treatment with IFNalpha2 and inhibitor trichostatin A, as well as combined HDAC1/HDAC2 silencing, restores STAT3-dependent reporter gene and endogenous gene expression, strongly suggesting that HDAC1 and HDAC2 are directly involved in repressing IFNalpha2-activated STAT3. In contrast, HDAC1 and HDAC2 activities are required for ISGF3-dependent gene expression. HDAC1 and HDAC2 differentially modulate STAT activity in response to IFNalpha2, while they are required for the induction of ISGF3-responsive genes, they impair the transcription of STAT3-dependent genes
physiological function
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Sir2 is involved in protection against Hog1-induced cell death and can suppress Hog1-induced reactive oxygen species accumulation. Therefore, cell death seems to be dictated by the balance of reactive oxygen species induced by Hog1 and the protective effect of Sir2. Prolonged activation of stress-activated protein kinase leads to cell death, by causing accumulation of reactive oxygen species. Mutations of the SCF-CDC4 ubiquitin ligase complex suppress cell death by preventing the degradation of Msn2 and Msn4 transcription factors. Accumulation of transcription factors Msn2 and Msn4 leads to the induction of PNC1, which is an activator of the Sir2 histone acetylase
physiological function
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Sirt1 inhibits T cell activation by suppressing the transcription of Bcl2-associated factor 1, Bclaf1, a protein required for T cell activation. Sirt1-null T cells have increased acetylation of the histone 3 lysine 56 residue, H3K56, at the bclaf1 promoter, as well as increasing Bclaf1 transcription. Sirt1 binds to bclaf1 promoter upon T cell receptor/CD28 stimulation by forming a complex with histone acetyltransferase p300 and NF-kappaB transcription factor Rel-A. The recruitment of Sirt1, but not p300, requires Rel-A. Knockdown of Bclaf1 suppresses the hyperactivation observed in Sirt1-/- T cells. Therefore, Sirt1 negatively regulates T cell activation via H3K56 deacetylation at the promoter region to inhibit transcription of Bclaf1
physiological function
the hda-2 mutation does not affect DNA methylation at any region tested, and the deletion and repeat-induced point mutation alleles give identical results
physiological function
the hda-3 mutation leads to global increases in histones H3 and H4 acetylation levels and to partial loss of DNA methylation
physiological function
the hda-4 mutation leads to global increases in histones H3 and H4 acetylation levels
physiological function
histone deacetylase 2 regulates chromosome segregation and kinetochore function via H4K16 deacetylation during oocyte maturation in mouse. HDAC2 is the major isozyme that regulates global histone acetylation during oocyte development and is largely responsible for the deacetylation of H4K16 during maturation. Histone deacetylation that occurs during oocyte maturation is critical for proper chromosome segregation
physiological function
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the enzyme activity promotes liver regeneration by regulating hepatocellular cell cycle progression at a step downstream of cyclin D1 induction
physiological function
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the Hos2/Set3 histone deacetylase complex (Set3C) plays a key role in the conversion of white phase to virulent opaque phase in Candida albicans. Azole resistance can be reversed by the co-administration of a histone deacetylase inhibitor, suggesting that resistance is mediated by epigenetic mechanisms possibly involving the fungal deacetylase Hos2
physiological function
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the Set3 complex acts as a repressor of hyphal differentiation and its function requires functional cAMP/PKA signaling, Set3C also controls morphogenesis through a transcription factor cluster, it is a co-factor of glycolysis and morphogenesis regulators, Set3C recruitment predicts induction and depletion predicts repression of yeast-to-hypha transition, molecular mechanism, overview. The Set3C decorates highly transcribed genes. The four phase-specific Set3C target transcription factors form a core transcriptional circuit
physiological function
Arabidopsis thaliana histone deacetylase genes HDA9, HDA15 and HDA19 play distinct roles in plant response to elevated ambient temperature. The histone deacetylases target to different sets of genes and play distinct roles in plant response to elevated ambient temperature, overview
physiological function
Arabidopsis thaliana histone deacetylase genes HDA9, HDA15 and HDA19 play distinct roles in plant response to elevated ambient temperature. The histone deacetylases target to different sets of genes and play distinct roles in plant response to elevated ambient temperature, overview. HDA15 is associated with thermosensory mark genes at 20°C. HDA15 is a direct repressor of plant thermal-responsive genes at normal temperature. HDA15 interacts with the transcription factor HFR1 (long Hypocotyl in Far Red1) to cooperatively repress warm-temperature response. HDA15 may be recruited by HFR1 to chromatin to epigenetically repress downstream target genes involved in hypocotyl elongation during plant response to low light and high temperature. HDA15 may stabilize HFR1 or enhances its function in negatively regulating PIF proteins that promote hypocotyl elongation during plant response to the growth conditions
physiological function
Arabidopsis thaliana histone deacetylase genes HDA9, HDA15 and HDA19 play distinct roles in plant response to elevated ambient temperature. The histone deacetylases target to different sets of genes and play distinct roles in plant response to elevated ambient temperature, overview. The hda9 mutation also leads to upregulation of many metabolic genes and accumulation of primary metabolites
physiological function
Hda1 is the catalytic core component of the H2B- and H3-specific histone deacetylase (HDAC) complex from Saccharomyces cerevisiae, which is involved in the epigenetic repression and plays a crucial role in transcriptional regulation and developmental events
physiological function
HDA1 might be involved in the epigenetic regulation of stress resistance genes that comprise the responses to osmotic stress and abscisic acid
physiological function
HDAC genes are non-essential in yeast, functional analysis of genes, RPD3, HDA1, SIR2, and HST1 in the Sake yeast strain Kyokai No. 701 (K701). RPD3 and Hda1 are translation regulatory proteins and histone deacetylases. Rpd3 and Hda1 may regulate isoamyl acetate production via oxygen in a Rox1-independent manner. Yeast HDACs, and maybe also HAT and their regulatory subunits, are keys to determine fermentation characteristics, and these genes may be an important target for improvement of yeast strains used for alcoholic beverage production
physiological function
HDAC genes are non-essential in yeast, functional analysis of genes, RPD3, HDA1, SIR2, and HST1 in the Sake yeast strain Kyokai No. 701 (K701). RPD3 and Hda1 are translation regulatory proteins and histone deacetylases. Rpd3L-dependent regulation of genes ILV2, ILV3 and ILV5. Rpd3 and Hda1 may regulate isoamyl acetate production via oxygen in a Rox1-independent manner. Yeast HDACs, and maybe also HAT and their regulatory subunits, are keys to determine fermentation characteristics, and these genes may be an important target for improvement of yeast strains used for alcoholic beverage production
physiological function
histone deacetylase 7 mediates tissue-specific autoimmunity via control of innate effector function in invariant natural killer T cells. HDAC7 binds transcription factor promyelocytic leukemia zinc finger protein (PLZF, ZBTB16) and modulates PLZF-dependent transcription. Autoimmune diseases are observed in HDAC7 gain-of-function in mice. Association between HDAC7 and hepatobiliary autoimmunity. Tconv development is regulated by the class IIA histone deacetylase histone deacetylase 7 (HDAC7), a TCR signal-regulated corepressor abundantly expressed in thymocytes. The activity of HDAC7 is controlled by nuclear exclusion in response to phosphorylation of conserved serine residues in their N-terminal adapter domains. HDAC7 regulates the effector programming of NKT cells in a manner that mirrors the function of PLZF. HDAC7 and PLZF inversely regulate a shared innate effector gene network that is highly relevant to autoimmune disease. HDAC7 nuclear export licenses innate effector development. HDAC7 serves as a gatekeeper of this developmental fate decision in the thymus
physiological function
histone deacetylase 7 mediates tissue-specific autoimmunity via control of innate effector function in invariant natural killer T cells. HDAC7 binds transcription factor promyelocytic leukemia zinc finger protein (PLZF, ZBTB16) and modulates PLZF-dependent transcription. HDAC7 and many of its transcriptional targets are human risk loci for IBD and PSC, autoimmune diseases that strikingly resemble the disease observed in HDAC7 gain-of-function in mice. Association between HDAC7 and hepatobiliary autoimmunity. Tconv development is regulated by the class IIA histone deacetylase histone deacetylase 7 (HDAC7), a TCR signal-regulated corepressor abundantly expressed in thymocytes. The activity of HDAC7 is controlled by nuclear exclusion in response to phosphorylation of conserved serine residues in their N-terminal adapter domains. HDAC7 regulates the effector programming of NKT cells in a manner that mirrors the function of PLZF. HDAC7 and PLZF inversely regulate a shared innate effector gene network that is highly relevant to autoimmune disease. HDAC7 nuclear export licenses innate effector development. HDAC7 serves as a gatekeeper of this developmental fate decision in the thymus
physiological function
histone deacetylases (HDACs) and polycomb group (PcG) proteins preferentially influence the size of mandibles (exaggerated male weapon) and demonstrate nutrition-dependent hypervariability in the broad-horned flour beetle, Gnatocerus cornutus. The plastic development of exaggerated traits is controlled in a module-specific manner by HDACs. The two HDACs, HDAC1 and HDAC3, appear to regulate size plasticity of mandibles and wings antagonistically, irrespective of which stage is perturbed, overview
physiological function
histone deacetylases (HDACs) and polycomb group (PcG) proteins preferentially influence the size of mandibles (exaggerated male weapon) and demonstrate nutrition-dependent hypervariability in the broad-horned flour beetle, Gnatocerus cornutus. The two HDACs, HDAC1 and HDAC3, appear to regulate size plasticity of mandibles and wings antagonistically, irrespective of which stage is perturbed, overview
physiological function
histone deacetylases (HDACs) are specifically responsible for the deacetylation of lysine residues at the N-terminal regions of the core histones (H2A, H2B, H3 and H4). In addition, HDACs may deacetylate other non-histone proteins and thus are involved in several cellular processes (e.g. differentiation, apoptosis, cancer development)
physiological function
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
histone deacetylases play roles in response to abiotic stresses in soybean. Histone deacetylases (HDACs) function as key epigenetic factors in repressing the expression of genes in multiple aspects of plant growth, development and plant response to abiotic or biotic stresses. Differential changes in GmHDACs transcripts accumulation occur in response to several abiotic cues, indicating that these epigenetic modifiers might potentially be part of a dynamic transcriptional response to stress in soybean. The levels of histone marks associated with plant HDACs are modulated by cold and heat in this legume
physiological function
increased expression of HDAC4 and -9 in patients with invasive squamous cell carcinoma supporting the idea that class IIa HDACs are important in the development of a basal molecular subtype and squamous differentiation in bladder cancer
physiological function
increased expression of HDAC4 and HDAC9 in patients with invasive squamous cell carcinoma supporting the idea that class IIa HDACs are important in the development of a basal molecular subtype and squamous differentiation in bladder cancer
physiological function
plant-specific histone deacetylases HDT1/2 regulate gibberellin2-oxidase2 gene expression to control Arabidopsis thaliana meristem cell number. HDT1/2 directly negatively regulate the acetylation level of the C19-gibberellin2-oxidase2 (GA2ox2) locus and repress the expression of GA2ox2 in the RM and elongation zone, transcriptome analyses. HDT1 and 2 function as part of a mechanism that modulates root growth in response to environmental factors
physiological function
the active site metal identity alters histone deacetylase 8 substrate selectivity, which may be a potential regulatory mechanism
physiological function
-
histone deacetylase 7 mediates tissue-specific autoimmunity via control of innate effector function in invariant natural killer T cells. HDAC7 binds transcription factor promyelocytic leukemia zinc finger protein (PLZF, ZBTB16) and modulates PLZF-dependent transcription. Autoimmune diseases are observed in HDAC7 gain-of-function in mice. Association between HDAC7 and hepatobiliary autoimmunity. Tconv development is regulated by the class IIA histone deacetylase histone deacetylase 7 (HDAC7), a TCR signal-regulated corepressor abundantly expressed in thymocytes. The activity of HDAC7 is controlled by nuclear exclusion in response to phosphorylation of conserved serine residues in their N-terminal adapter domains. HDAC7 regulates the effector programming of NKT cells in a manner that mirrors the function of PLZF. HDAC7 and PLZF inversely regulate a shared innate effector gene network that is highly relevant to autoimmune disease. HDAC7 nuclear export licenses innate effector development. HDAC7 serves as a gatekeeper of this developmental fate decision in the thymus
-
physiological function
-
HDAC genes are non-essential in yeast, functional analysis of genes, RPD3, HDA1, SIR2, and HST1 in the Sake yeast strain Kyokai No. 701 (K701). RPD3 and Hda1 are translation regulatory proteins and histone deacetylases. Rpd3L-dependent regulation of genes ILV2, ILV3 and ILV5. Rpd3 and Hda1 may regulate isoamyl acetate production via oxygen in a Rox1-independent manner. Yeast HDACs, and maybe also HAT and their regulatory subunits, are keys to determine fermentation characteristics, and these genes may be an important target for improvement of yeast strains used for alcoholic beverage production
-
physiological function
-
Hda1 is the catalytic core component of the H2B- and H3-specific histone deacetylase (HDAC) complex from Saccharomyces cerevisiae, which is involved in the epigenetic repression and plays a crucial role in transcriptional regulation and developmental events
-
physiological function
-
HDAC genes are non-essential in yeast, functional analysis of genes, RPD3, HDA1, SIR2, and HST1 in the Sake yeast strain Kyokai No. 701 (K701). RPD3 and Hda1 are translation regulatory proteins and histone deacetylases. Rpd3 and Hda1 may regulate isoamyl acetate production via oxygen in a Rox1-independent manner. Yeast HDACs, and maybe also HAT and their regulatory subunits, are keys to determine fermentation characteristics, and these genes may be an important target for improvement of yeast strains used for alcoholic beverage production
-
physiological function
-
the Hos2/Set3 histone deacetylase complex (Set3C) plays a key role in the conversion of white phase to virulent opaque phase in Candida albicans. Azole resistance can be reversed by the co-administration of a histone deacetylase inhibitor, suggesting that resistance is mediated by epigenetic mechanisms possibly involving the fungal deacetylase Hos2
-
additional information
-
enzyme Hos2 is not inhibited by class I inhibitors such as MS-275
additional information
-
isoform-specific regulation of zinc-dependent histone deacetylase expression, subcellular localization, and activity in regenerating liver. The signals that regulate the PH-induced metabolic response to hepatic insufficiency are not downstream, but might be upstream, of the target of suberoylanilide hydroxyamic acid's anti-regenerative activity
additional information
similar histones substrate conversion is observed in the presence of octameric and monomeric enzyme
additional information
-
similar histones substrate conversion is observed in the presence of octameric and monomeric enzyme
additional information
the ARB2 domain displays an alpha/beta sandwich architecture with an arm protruding outside. Two ARB2 domain molecules form a compact homodimer via the arm elements, and assemble as an inverse V shape. The pull-down and ITC results reveal that the ARB2 domain possesses the histone binding ability, recognizing both the H2A-H2B dimer and H3-H4 tetramer. the unique dimer architecture of the ARB2 domain coincides with the function for anchoring to histone. Hda1 consists of an N-terminal catalytic domain and a C-terminal non-catalytic domain (ARB2). The catalytic domain of Hda1 shows high sequence homology to the HDACs structures. Role of the C-terminal non-catalytic domain of Hda1 functioning in the deacetylation process, overview
additional information
-
the ARB2 domain displays an alpha/beta sandwich architecture with an arm protruding outside. Two ARB2 domain molecules form a compact homodimer via the arm elements, and assemble as an inverse V shape. The pull-down and ITC results reveal that the ARB2 domain possesses the histone binding ability, recognizing both the H2A-H2B dimer and H3-H4 tetramer. the unique dimer architecture of the ARB2 domain coincides with the function for anchoring to histone. Hda1 consists of an N-terminal catalytic domain and a C-terminal non-catalytic domain (ARB2). The catalytic domain of Hda1 shows high sequence homology to the HDACs structures. Role of the C-terminal non-catalytic domain of Hda1 functioning in the deacetylation process, overview
additional information
transcript analysis of genes responsible for the production of flavor components
additional information
transcript analysis of genes responsible for the production of flavor components
additional information
-
transcript analysis of genes responsible for the production of flavor components
additional information
-
transcript analysis of genes responsible for the production of flavor components
-
additional information
-
the ARB2 domain displays an alpha/beta sandwich architecture with an arm protruding outside. Two ARB2 domain molecules form a compact homodimer via the arm elements, and assemble as an inverse V shape. The pull-down and ITC results reveal that the ARB2 domain possesses the histone binding ability, recognizing both the H2A-H2B dimer and H3-H4 tetramer. the unique dimer architecture of the ARB2 domain coincides with the function for anchoring to histone. Hda1 consists of an N-terminal catalytic domain and a C-terminal non-catalytic domain (ARB2). The catalytic domain of Hda1 shows high sequence homology to the HDACs structures. Role of the C-terminal non-catalytic domain of Hda1 functioning in the deacetylation process, overview
-
additional information
-
enzyme Hos2 is not inhibited by class I inhibitors such as MS-275
-
Show AA Sequence and Transmembrane Helices (22117 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
x * 105000, calculated, x * 119000, SDS-PAGE of FLAG-tagged protein
119000
x * 105000, calculated, x * 119000, SDS-PAGE of FLAG-tagged protein
120000
220000
400000 - 500000
gel filtration, enzyme is part of a high molecular weight complex
42000
51200
-
x * 51200, isozyme HDAC3, SDS-PAGE, x * 77200, recombinant GST-tagged isozyme HDAC3, SDS-PAGE
600000
77200
-
x * 51200, isozyme HDAC3, SDS-PAGE, x * 77200, recombinant GST-tagged isozyme HDAC3, SDS-PAGE
600000
gel filtration, enzyme is part of a high molecular weight complex insensitive to trichostatin A
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
additional information
?
-
x * 51200, isozyme HDAC3, SDS-PAGE, x * 77200, recombinant GST-tagged isozyme HDAC3, SDS-PAGE
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 41180, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 22260, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 26740, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 38500, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 45280, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 45540, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 48940, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 52180, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 52920, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 53300, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 55950, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 55960, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 56120, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 56280, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 59600, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 72990, sequence calculation
?
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
x * 73040, sequence calculation
additional information
-
enzyme interacts directly with transcription factor MEF-2
additional information
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isoform HD2 dissociates into HD1 when treated with 1.6 M NaCl or applied to a Q-Sepharose column. The active form of enzyme is a high-molecular-mass complex associated with proteins that are components of the nuclear matrix
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
-
class II histone deacetylases bind myocyte enhancer factor-2
additional information
enzyme contains an amino-terminal catalytic domain and a carboxyl pseudo-repeat that shares significant homology with its catalytic domain
additional information
enzyme has a bipartite modular structure consisting of a N-terminal putative deacetylase domain and a C-terminal leucine-rich domain. Isoform HDAC10 interacts with enzyme isoform HDAC3, but not with HDAC4 or HDAC6
additional information
-
enzyme has a bipartite modular structure consisting of a N-terminal putative deacetylase domain and a C-terminal leucine-rich domain. Isoform HDAC10 interacts with enzyme isoform HDAC3, but not with HDAC4 or HDAC6
additional information
histone deacetylase activity of isoform HDAC7 maps to a C-terminal domain and is dependent on interaction with isoform HDAC3 in the nucleus. Cytoplasmic HDAC7 that is not bound to HDAC3 is inactive. Transcriptional corepressors SMRT and N-CoR may serve as critical mediators of interaction between HDAC7 and HDAC3
additional information
-
histone deacetylase activity of isoform HDAC7 maps to a C-terminal domain and is dependent on interaction with isoform HDAC3 in the nucleus. Cytoplasmic HDAC7 that is not bound to HDAC3 is inactive. Transcriptional corepressors SMRT and N-CoR may serve as critical mediators of interaction between HDAC7 and HDAC3
additional information
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in undifferentiatied muscle cells, isoform HDAC1 associates with transcription factor MyoD resulting in silencing of MyoD-dependent transcription of endogenous p21 as well as muscle-specific genes
additional information
-
isoforms HDAC1 and HDAC2 are associated in vivo, complex is able to deacetylate all four core histones in vitro
additional information
-
isoforms HDAC1, HDAC2, HDAC3 co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70
additional information
similar histones substrate conversion is observed in the presence of octameric and monomeric enzyme
additional information
-
similar histones substrate conversion is observed in the presence of octameric and monomeric enzyme
additional information
the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
additional information
-
the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
additional information
-
the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
-
additional information
-
the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
-
additional information
-
the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
-
additional information
-
the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
-
additional information
-
the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
-
additional information
-
the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
-
additional information
-
the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
-
additional information
the ARB2 domain of Hda1 exists as a homodimer. The ARB2 domain displays an alpha/beta sandwich architecture with an arm protruding outside. Two ARB2 domain molecules form a compact homodimer via the arm elements, and assemble as an inverse V shape, overall structure analysis, overview. Perturbation of the dimer interface abolishes the histone binding ability of the ARB2 domain. Hda1 consists of an N-terminal catalytic domain and a C-terminal non-catalytic domain (ARB2). The catalytic domain of Hda1 shows high sequence homology to the HDACs
additional information
-
the ARB2 domain of Hda1 exists as a homodimer. The ARB2 domain displays an alpha/beta sandwich architecture with an arm protruding outside. Two ARB2 domain molecules form a compact homodimer via the arm elements, and assemble as an inverse V shape, overall structure analysis, overview. Perturbation of the dimer interface abolishes the histone binding ability of the ARB2 domain. Hda1 consists of an N-terminal catalytic domain and a C-terminal non-catalytic domain (ARB2). The catalytic domain of Hda1 shows high sequence homology to the HDACs
additional information
-
the ARB2 domain of Hda1 exists as a homodimer. The ARB2 domain displays an alpha/beta sandwich architecture with an arm protruding outside. Two ARB2 domain molecules form a compact homodimer via the arm elements, and assemble as an inverse V shape, overall structure analysis, overview. Perturbation of the dimer interface abolishes the histone binding ability of the ARB2 domain. Hda1 consists of an N-terminal catalytic domain and a C-terminal non-catalytic domain (ARB2). The catalytic domain of Hda1 shows high sequence homology to the HDACs
-
additional information
enzyme copurifies as a complex with a protein related to the retinoblastoma-associated protein, Rbap46
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
phosphoprotein
-
isoform HDAC1 is phosphorylated at S423 and S421. Loss of phosphorylation reduces the enzyme acivity and complex formation
phosphoprotein
in thymocytes, TCR stimulation results in HDAC7 phosphorylation and nuclear exclusion via protein kinase D
phosphoprotein
in thymocytes, TCR stimulation results in HDAC7 phosphorylation and nuclear exclusion via protein kinase D
phosphoprotein
-
in thymocytes, TCR stimulation results in HDAC7 phosphorylation and nuclear exclusion via protein kinase D
-
additional information
sequence contains a potential N-glycosylation site at D616, 3 putative protein kinase C phosphorylation sites, and several putative casein kinase phosphorylation sites
additional information
sequence includes a potential N-glycosylation site at N136, a cAMP-dependent kinase phosphorylation site at S39, and two potential casein kinase II phosphorylation sites
additional information
-
sequence includes a potential N-glycosylation site at N136, a cAMP-dependent kinase phosphorylation site at S39, and two potential casein kinase II phosphorylation sites
additional information
-
cyclopentenone prostaglandins covalently alkylate (carbonylate) class I HDAC1, -2, and -3
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and in complexes with inhibitors trichostatin A and suberoylanilide hydroxamic acid. Active site consists of a tubular pocket, a zinc-binding site and two D-H charge-relay systems
-
modeling studies using inhibitor 6-[(9H-fluoren-3-ylmethyl)(3-phenoxybenzyl)amino]-N-hydroxyhexanamide and histone deacetylase-like protein, PDB ID: 1C3R. Inhibitor fills the equivalent space at the protein surface and occupies the catalytic binding site, coordinating the fundamental zinc ion
complex of isoform HDAC9 with myocyte enhancer factor-2 and DNA. HDAC9 binds to a hydrophobic groove of the myocyte enhancer factor-2 dimer. General mechainsm, by which class II histone deacetylases are recruited by myocyte enhancer factor-2
-
docking studies of the representative compound 4 to the homology model of HDAC1 and the X-ray structures of HDAH, PDB 1ZZ1, and HDAC8, PDB 1T67
-
molecular modeling of isoform HDAC8 in complex with inhibitor N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
molecular modelling of structure of isoform HDAC8 in complex with suberoylanilide hydroxamic acid and with 7-mercapto-N-phenylheptanamide
N-terminal glutamine-rich fragment, residues 62-153. The glutamine-rich domain folds into an alpha-helix that assembles as a tetramer lacking regularly arranged apolar residues and an extended hydrophobic core. Instead, the protein interfaces consist of multiple hydrophobic patches interspersed with polar interaction networks, wherein clusters of glutamines engage in extensive intra- and interhelical interactions. In solution, the tetramer undergoes rapid equilibrium with monomer and intermediate species
seven structures of wild-type HDAC8 and mutants in complex with inhibitors or substrate are determined to a resolution of 1.8 to 3.3 A
the crystal structures of the catalytic domain of HDAC7 and its complexes with suberoylanilide hydroxamic acid and trichostatin A are solved
crystal structure of PA3774 from Pseudomonas aeruginosa as ligand-free enzyme and as protein-ligand complexes with a trifluoromethylketone inhibitor and the reaction product acetate, and of inhibitor-free PA3774H143A mutant, the inhibitor-free PA3774Y313F mutant, and the PA3774Y313F mutant in complex with the highly selective hydroxamate inhibitor N-[1,1,2,2,3,3,4,4,5,5,6,6-dodecafluoro-7-(hydroxyamino)-7-oxoheptyl]benzamide, from 0.5 M K2HPO4, 0.5 M Na2HPO4, and 0.1 M (NH4)2SO4, pH 7.5, X-ray diffraction structure determination and analysis
Hda1 ARB2 domain, native and selenomethionine-labebeed protein, hanging drop vapour diffusion method, from 0.1 M sodium acetate trihydrate, pH 4.6, and 2.0 M sodium formate, 12°C, 1 day, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement method and modelling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C261S
-
the single mutant forms about 70% less covalent adduct with 5-deoxy-DELTA12,14-prostaglandin J2-biotin compared to the wild type enzyme
C261S/C273S
-
the double mutant shows about 95% less alkylation by 0.005 mM 5-deoxy-DELTA12,14-prostaglandin J2-biotin compared to the wild type enzyme
C273S
-
the single mutant forms about 70% less covalent adduct with 5-deoxy-DELTA12,14-prostaglandin J2-biotin compared to the wild type enzyme
D101A
mutant, confirms that the strictly conserved side chain of D101 is crucial for the function of the L2 loop
D101E
mutant, confirms that the strictly conserved side chain of D101 is crucial for the function of the L2 loop
D101L
mutant, confirms that the strictly conserved side chain of D101 is crucial for the function of the L2 loop
D101N
mutant, confirms that the strictly conserved side chain of D101 is crucial for the function of the L2 loop
D174N
-
isoform HDAC1 mutant, about 5% of wild-type activity, reduced ability to bind a trapoxin-affinity matrix and decreased interaction with proteins RbAp48 and mSin3A
D174N/D176N
-
isoform HDAC1 mutant, about 3% of wild-type activity, reduced ability to bind a trapoxin-affinity matrix and decreased interaction with proteins RbAp48 and mSin3A
D176A
-
the mutation increases the K1/2 for potassium inhibition by more than 40fold
D176N
-
isoform HDAC1 mutant, about 3% of wild-type activity, reduced ability to bind a trapoxin-affinity matrix and decreased interaction with proteins RbAp48 and mSin3A
H141A
H141F/H199A
-
isoform HDAC1 mutant, about 10% of wild-type activity, reduced ability to bind a trapoxin-affinity matrix and decreased interaction with proteins RbAp48 and mSin3A
H142A
-
the mutation increases the K1/2 for potassium inhibition by more than 40fold
H199A
-
isoform HDAC1 mutant, about 10% of wild-type activity, reduced ability to bind a trapoxin-affinity matrix and decreased interaction with proteins RbAp48 and mSin3A
H216A
H216A/H611A
site-directed mutagenesis, catalytically inactive DD1/DD2 domains mutant
H611A
L175A
-
mutation in fragment 155-220 of isoform HDAC4, binding to myocyte enhancer factor-2 is diminished
L175K
-
mutation in fragment 155-220 of isoform HDAC4, binding to myocyte enhancer factor-2 is diminished
L180A
-
mutation in fragment 155-220 of isoform HDAC4, little effect on binding to myocyte enhancer factor-2
L180K
-
mutation in fragment 155-220 of isoform HDAC4, little effect on binding to myocyte enhancer factor-2
S421A
-
mutation of phosphorylation site, reduces the enzyme activity to 33% and disturbs complex formation. Mutant activates transcription of luciferase reporter gene under conditions where the wild-type does not activate
S421A/S423A
-
mutation of phosphorylation sites, reduces the enzyme activity to 22% and disturbs complex formation. Mutant activates transcription of luciferase reporter gene under conditions where the wild-type does not activate
S423A
-
mutation of phosphorylation site, reduces the enzyme activity to 25% and disturbs complex formation. Mutant activates transcription of luciferase reporter gene under conditions where the wild-type does not activate
V171A
-
mutation in fragment 155-220 of isoform HDAC4, little effect on binding to myocyte enhancer factor-2
V171K
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mutation in fragment 155-220 of isoform HDAC4, binding to myocyte enhancer factor-2 is diminished
V179A
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mutation in fragment 155-220 of isoform HDAC4, binding to myocyte enhancer factor-2 is diminished
Y146A
Y153A
Y253A
H604A/H608A/R609A
site-directed mutagenesis, the mutant ARB2-M4 completely loses the binding ability to histone H3-H4, histone binding kinetics, overview
Q463A/D471A
site-directed mutagenesis, histone binding kinetics, overview
V481A/S482A/M483A/D484A
site-directed mutagenesis, histone binding kinetics, overview
Y468A/E472A
site-directed mutagenesis, histone binding kinetics, overview
H604A/H608A/R609A
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site-directed mutagenesis, the mutant ARB2-M4 completely loses the binding ability to histone H3-H4, histone binding kinetics, overview
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Q463A/D471A
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site-directed mutagenesis, histone binding kinetics, overview
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V481A/S482A/M483A/D484A
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site-directed mutagenesis, histone binding kinetics, overview
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Y468A/E472A
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site-directed mutagenesis, histone binding kinetics, overview
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additional information
H141A
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isoform HDAC1 mutant, about 20% of wild-type activity, reduced ability to bind a trapoxin-affinity matrix
H141A
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not able to deacetylate MyoD transcription factor or to repress MyoD-mediated transcription in vivo
H216A
mutation in the first catalytic domain of enzyme, slight decrease in catalytic rate
H216A
site-directed mutagenesis, catalytically almost inactive DD1 domain mutant
H611A
mutation in second catalytic domain of enzyme, more than 5000fold decrease in catalytic rate
H611A
site-directed mutagenesis, catalytically almost inactive DD2 domain mutant
Y146A
mutant, constructed for identification of tyrosine residues responsible for HDAC2 degradation
Y146A
in presence of peroxynitrite, activity is reduced by 32%. In presence of 3-morpholinosydonomine, activity is reduced similar to wild-type
Y153A
mutant, constructed for identification of tyrosine residues responsible for HDAC2 degradation
Y153A
in presence of 3-morpholinosydonomine, activity is reduced similar to wild-type. In presence of peroxynitrite, activity is abolished
Y253A
mutant, constructed for identification of tyrosine residues responsible for HDAC2 degradation
Y253A
Y253 is at least partly responsible for the proteasomal degradation of HDAC2 under nitrative stress. Activity is not reduced in presence of 3-morpholinosydonomine
additional information
generation of a HDA15 mutant line, and a hda15-1/hfr1 double mutant
additional information
generation of a HDA15 mutant line, and a hda15-1/hfr1 double mutant
additional information
generation of a HDA15 mutant line, and a hda15-1/hfr1 double mutant
additional information
knockdown of HDT1/2 (hdt1,2i), phenotypes. GA2ox2 expression is increased in all transit-amplifying cells in hdt1,2i-1
additional information
knockdown of HDT1/2 (hdt1,2i), phenotypes. GA2ox2 expression is increased in all transit-amplifying cells in hdt1,2i-1
additional information
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deletion of enzyme gene hdaA causes transcriptional activation of two telomere-proximal gene clusters and subsequent increased levels of the corresponding molecules, but not of a telomere-distal cluster
additional information
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knock-down by RNAi does not result in muscle function or developmental defects
additional information
generation of HDAC1 knockout mutants, phenotypes, and comparison to HDAC3, molecular basis for epigenetic control of phenotypic variability, expression analysis of HDAC genes from different classes, overview
additional information
generation of HDAC1 knockout mutants, phenotypes, and comparison to HDAC3, molecular basis for epigenetic control of phenotypic variability, expression analysis of HDAC genes from different classes, overview
additional information
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generation of HDAC1 knockout mutants, phenotypes, and comparison to HDAC3, molecular basis for epigenetic control of phenotypic variability, expression analysis of HDAC genes from different classes, overview
additional information
generation of HDAC3 knockout mutants, phenotypes, and comparison to HDAC1, molecular basis for epigenetic control of phenotypic variability, expression analysis of HDAC genes from different classes, overview
additional information
generation of HDAC3 knockout mutants, phenotypes, and comparison to HDAC1, molecular basis for epigenetic control of phenotypic variability, expression analysis of HDAC genes from different classes, overview
additional information
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generation of HDAC3 knockout mutants, phenotypes, and comparison to HDAC1, molecular basis for epigenetic control of phenotypic variability, expression analysis of HDAC genes from different classes, overview
additional information
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deletion of casein kinase 2 consensus sequence resulting in loss of phosphorylation reduces the enzyme activity and complex formation. Deletion of the highly charged C-terminal region decreases catalytic activity to 22% of wild-type and protein associations
additional information
enzyme contains two potentially functional catalytic domains. Expression of first domain alone does not result in catalytic activity. The catalytic domain II alone shows only a modest decrease in substrate binding and product formation rate compared to wild-type
additional information
knock-down of isoform HDAC8 expression by RNAi inhibits growth of human lung, colon, and cervical cancer cell lines
additional information
-
knock-down of isoform HDAC8 expression by RNAi inhibits growth of human lung, colon, and cervical cancer cell lines
additional information
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silencing of enzyme isoforms HDAC, HDAC6, and HDAC8 expression impairs transforming growth factor beta1-induced expression of smooth muscle alpha-actin. HDAC4 silencing is most efficient and also prevents transforming growth factor beta1-mediated morphological changes. Forced down-regulation of HDAC4 stimulates the expression of 5-TG-3-interacting factor and TGIF2 homeoproteins
additional information
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silencing of isoforms HDAC1, HDAC2, HDAC3 by RNAi markedly decreases interferon gamma-driven gene activation. Overexpression of the enzymes enhances STAT1-driven transcriptional activity
additional information
-
complex of HDAC6-microtubule directly bind to alpha subunit of FTase
additional information
a constitutively nuclear mutant of human HDAC7 (HDAC7-DP) is transiently expressed at normal levels during thymic T cell development but not in mature T cells, autoreactive cells that would normally die by negative selection instead exit the thymus as native Tconv
additional information
-
a constitutively nuclear mutant of human HDAC7 (HDAC7-DP) is transiently expressed at normal levels during thymic T cell development but not in mature T cells, autoreactive cells that would normally die by negative selection instead exit the thymus as native Tconv
additional information
-
knock-down of isoform HDAC2 expression by small hairpin RNA inhibits cellular proliferation in a dose-dependent manner, which is also partly p53-dependent and induces cellular senescence. Knock-down enhances p53-dependent trans-repression and trans-activation of a subset of target genes. Enhancement is due to increased p53-DNA binding activity
additional information
generation of homozygous Hdac2-/- and heterozygous Hdac1-/+/Hdac2-/- isozyne HDAC2 knockout mutant oocytes, penotypes overview
additional information
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generation of homozygous Hdac2-/- and heterozygous Hdac1-/+/Hdac2-/- isozyne HDAC2 knockout mutant oocytes, penotypes overview
additional information
a gain-of-function HDAC7 mutant, HDAC7-DP, arrests thymic iNKT development, phenotype, overview. iNKT phenotype of HDAC7-DP transgenic mice, and of wild-type:HDAC7-DELTAP mixed hematopoietic chimeric mutants. The HDAC7-DELTAP transgenic population contributed robustly to the pool of CD4 and CD8 SP thymocytes, although there is a transient reduction in prevalence at the immature single positive (ISP) stage
additional information
-
a gain-of-function HDAC7 mutant, HDAC7-DP, arrests thymic iNKT development, phenotype, overview. iNKT phenotype of HDAC7-DP transgenic mice, and of wild-type:HDAC7-DELTAP mixed hematopoietic chimeric mutants. The HDAC7-DELTAP transgenic population contributed robustly to the pool of CD4 and CD8 SP thymocytes, although there is a transient reduction in prevalence at the immature single positive (ISP) stage
-
additional information
construction of four mutants, ARB2-M1 (residues Gln463, His467 and Asp471 mutated to Ala), ARB2-M2 (residues Tyr468 and Glu472 mutated to Ala), ARB2-M3 (residues Val481, Ser482, Met483 and Asp484 mutated to Ala) and ARB2-M4 (residues His604, His608 and Arg609 mutated to Ala). The binding affinity of mutants ARB2-M1, ARB2-M2, ARB2-M3 and ARB2-M4 to histone H2A-H2B dimer is 0.0204 mM, 0.0169 mM, 0.0277 mM, and 0.0174 mM, respectively. And the binding affinity of mutants ARB2-M1, ARB2-M2 and ARB2-M3 to histone H3-H4 tetramer is 0.00984 mM, 0.00693 mM, and 0.00819 mM, respectively. Mutant ARB2-M4 completely loses the binding ability to histone H3-H4
additional information
-
construction of four mutants, ARB2-M1 (residues Gln463, His467 and Asp471 mutated to Ala), ARB2-M2 (residues Tyr468 and Glu472 mutated to Ala), ARB2-M3 (residues Val481, Ser482, Met483 and Asp484 mutated to Ala) and ARB2-M4 (residues His604, His608 and Arg609 mutated to Ala). The binding affinity of mutants ARB2-M1, ARB2-M2, ARB2-M3 and ARB2-M4 to histone H2A-H2B dimer is 0.0204 mM, 0.0169 mM, 0.0277 mM, and 0.0174 mM, respectively. And the binding affinity of mutants ARB2-M1, ARB2-M2 and ARB2-M3 to histone H3-H4 tetramer is 0.00984 mM, 0.00693 mM, and 0.00819 mM, respectively. Mutant ARB2-M4 completely loses the binding ability to histone H3-H4
additional information
establishment of HDAC RPD3 and accessory protein gene-disrupted strains, sake strain 701 with deleted gened encoding for other transcription regulatory proteins, e.g. RPD3, HDA1, SDS3, DEP1, and UME1, and NAD-dependent protein deacetylases, e.g. HST1, and quantitative real-time PCR of fusel alcohol or acetate ester synthesis related-genes in these strains, overview. Evaluation of sake fermenatation with the mutant strains, small-scale sake production test
additional information
establishment of HDAC RPD3 and accessory protein gene-disrupted strains, sake strain 701 with deleted gened encoding for other transcription regulatory proteins, e.g. RPD3, HDA1, SDS3, DEP1, and UME1, and NAD-dependent protein deacetylases, e.g. HST1, and quantitative real-time PCR of fusel alcohol or acetate ester synthesis related-genes in these strains, overview. Evaluation of sake fermenatation with the mutant strains, small-scale sake production test
additional information
-
establishment of HDAC RPD3 and accessory protein gene-disrupted strains, sake strain 701 with deleted gened encoding for other transcription regulatory proteins, e.g. RPD3, HDA1, SDS3, DEP1, and UME1, and NAD-dependent protein deacetylases, e.g. HST1, and quantitative real-time PCR of fusel alcohol or acetate ester synthesis related-genes in these strains, overview. Evaluation of sake fermenatation with the mutant strains, small-scale sake production test
additional information
-
establishment of HDAC RPD3 and accessory protein gene-disrupted strains, sake strain 701 with deleted gened encoding for other transcription regulatory proteins, e.g. RPD3, HDA1, SDS3, DEP1, and UME1, and NAD-dependent protein deacetylases, e.g. HST1, and quantitative real-time PCR of fusel alcohol or acetate ester synthesis related-genes in these strains, overview. Evaluation of sake fermenatation with the mutant strains, small-scale sake production test
-
additional information
-
construction of four mutants, ARB2-M1 (residues Gln463, His467 and Asp471 mutated to Ala), ARB2-M2 (residues Tyr468 and Glu472 mutated to Ala), ARB2-M3 (residues Val481, Ser482, Met483 and Asp484 mutated to Ala) and ARB2-M4 (residues His604, His608 and Arg609 mutated to Ala). The binding affinity of mutants ARB2-M1, ARB2-M2, ARB2-M3 and ARB2-M4 to histone H2A-H2B dimer is 0.0204 mM, 0.0169 mM, 0.0277 mM, and 0.0174 mM, respectively. And the binding affinity of mutants ARB2-M1, ARB2-M2 and ARB2-M3 to histone H3-H4 tetramer is 0.00984 mM, 0.00693 mM, and 0.00819 mM, respectively. Mutant ARB2-M4 completely loses the binding ability to histone H3-H4
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography on a 5-ml HiTrap Chelating column charged with Ni2+ and by anion exchange chromatography on a Source 30Q column
cytoplasmic lysates are prepared
enzyme copurifies as a complex with a protein related to the retinoblastoma-associated protein, Rbap46
partially by isolation of nuclei from Arachis hygogaea leaves, recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
proteins are expressed in Escherichia coli BL21DE3 cells and purified using nickel nitrilotriacetic acid or TALON affinity resin, a GE HiTrap Q HP and a Superdex 26-60 column
recombinant enzyme purified aerobically from Escherichia coli contains 8fold more iron than zinc before dialysis
recombinant HDAC1 from Escherichia coli strain TOP10 by anion exchange chromatography, ultrafiltration, heparin affinity chromatography, poly-L-lysine affinity chromatography, and gel filtration. The effects of chaotropic species, weak kosmotropes, amino acids, reducing or denaturing agents, detergents, alcohols, and saturated fatty acids are tested to dissociate the protein aggregates, overview
recombinant His-tagged wild-type and mutant ARB2 domains from Escherichia coli strain BL21(DE3) by nickel affinity chroatography and gel filtration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant N-terminally His6-atgegd enzyme from Spodoptera frugiperda Sf9 cells by nickel affinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA1 is located on chromosome 1
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA10 is located on chromosome 6
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA11 is located on chromosome 11
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA12 is located on chromosome 11
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA13 is located on chromosome 12
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA14 is located on chromosome 12
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA15 is located on chromosome 17
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA16 is located on chromosome 17
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA17 is located on chromosome 17
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA18 is located on chromosome 17
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA2 is located on chromosome 4
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA3 is located on chromosome 4
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA4 is located on chromosome 4
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA5 is located on chromosome 5
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA6 is located on chromosome 5
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA7 is located on chromosome 5
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA8 is located on chromosome 5
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
28 HDAC genes from soybean genome are identified, which are asymmetrically distributed on 12 chromosomes, genotyping and phylogenetic analysis, genetic structure, real-time quantitative PCR enzyme expression analysis, recombinant expression of YFP-tagged isozymes in transgenic Glycine max, gene GmHDA9 is located on chromosome 6
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
a pET20b-derived HDAC8-His expression plasmid with optimized codon usage, pHD2-His, is modified to add a factor Xa cleavage site, generating pHD2-Xa-His
a synthetic gene coding for HDAC1 is optimised for Escherichia coli codon usage, cloning into pBADHisB, generating vector pBAD-rHDAC1, and recombinant overexpression in Escherichia coli strain TOP10, method evaluation. The overexpression of HDAC1 is induced for 15 h at 30°C with 1.3 mM arabinose, when bacterial populations reach an OD600 equal to 0.8-0.9
DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of GST-tagged isozyme HDAC3 in Escherichia coli
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expression in Escherichia coli
expression in Sf9 cells of full-length protein and of 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
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FLAG-tagged HDAC1 deletion mutants, aa 1-482, 1-140 and 141-482, are constructed in pcDNA3 FLAG expression plasmid
full lengtht cDNAs for hdac1 and hdac3 are cloned into the pGEM-T easy vector and confirmed by sequencing, for functional analysis the genes are subcloned into the vector pCS2
full-length HDAC1 with COOH-terminal His tag is expressed using baculovirus expression system
full-length HDAC2 with COOH-terminal His tag is expressed using baculovirus expression system
full-length HDAC3 with COOH-terminal His tag is expressed using baculovirus expression system
full-length HDAC4 with COOH-terminal His tag is expressed using baculovirus expression system
full-length HDAC8 with COOH-terminal His tag is expressed using baculovirus expression system
gene HDA1, DNA and amino acid sequence dteermination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression of His-tagged enzyme in Escherichia coli strain BL21, quantitative RT-PCR enzyme expression analysis
gene HDA15, quantitative expression analysis of wild-type and mutant enzymes at 20°C and 27°C in transgenic Arabidosis thaliana lines
gene HDA19, quantitative expression analysis of wild-type and mutant enzymes at 20°C and 27°C in transgenic Arabidosis thaliana lines, recombinant expression of HA-tagged HDA19 in hda19 or hda9-1 mutants via Agrobacterium tumefaciens strain GV3101 transfection using the floral dip method
gene HDA9, quantitative expression analysis of wild-type and mutant enzymes at 20°C and 27°C in transgenic Arabidosis thaliana lines, recombinant expression of HA-tagged HDA9 in hda19 or hda9-1 mutants via Agrobacterium tumefaciens strain GV3101 transfection using the floral dip method
gene HDAC4, histone deacetylase expression within in vitro and in vivo bladder cancer model systems, quantitative real-time PCR enzyme expression analysis, overview. Basal-squamous bladder cancer (BC) clinical samples are enriched for histone deacetylase (HDAC)4 and HDAC9 expression
gene HDAC7, histone deacetylase expression within in vitro and in vivo bladder cancer model systems, quantitative real-time PCR enzyme expression analysis, overview
gene HDAC9, histone deacetylase expression within in vitro and in vivo bladder cancer model systems, quantitative real-time PCR enzyme expression analysis, overview. Basal-squamous bladder cancer clinical samples are enriched for histone deacetylase (HDAC)4 and HDAC9 expression
gene HOS2, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His6-atgegd enzyme in Spodoptera frugiperda Sf9 cells
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gene pa3774, DNA and amino acid sequence determination and analysis, recombinant expression of wild-type and mutant enzymes
into the pAc5.1 expression vector for expression in S2 insect cells
isoform HDAC8, expression in Escherichia coli. Isoforms HDAC1, HDAC6, expression in HEK-293 cell, HDAC3, expression in insect system, FLAg-tagged proteins
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Myc-, HA- or, GFP-tagged HDAC6 are constructed in a CMV promoter-derrived mammalian expression vector, pCS4+
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overexpression in Escherichia coli as glutathione S-transferase fusion protein
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recombinant expression of His-tagged wild-type and mutant ARB2 domains (residues Hda1457-698) in Escherichia coli strain BL21(DE3)
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
residues 483 to 903 of isoform 1 of chHDAC7 are cloned into a modified pET28a vector for expression in Escherichia coli BL21DE3 Codon Plus RIL cells
transient and stable expression of green fluorescent protein-tagged enzyme in onion cells and roots, seeds and leaves of Arabidopsis. For control of enzymic activity, expression in bacterial cells. Expression in insect cells does not result in catalytically active enzyme
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
HDAC1 and HDAC2 protein levels are elevated in chondrocytes from osteoarthritic patients
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hepatocyte growth factor induces HDAC-5 expression in gastric cancer cells. GO6976, a PKC inhibitor, significantly inhibits hepatocyte growth factor-induced HDAC5 expression
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histone deacetylase 1 mRNA in pancreatic cancer tissues are significantly higher than in paracancerous tissues
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isoform HDAC2-1 is significantly induced at 6 and 24 h after spraying of seedlings with 0.1 mM jasmonic acid, isoform HDAC2-1 shows a marked induction at 24 h after 0.1 mM abscisic acid treatment, isoform HDAC2-1 transcript levels show an increase upon treatment with 0.1 mM salicylic acid after 24 h
isoform HDAC2-2 transcript levels decline 6 h after abscisic acid treatment and show no significant difference in 24 h after abscisic acid treatment
K562 erythroleukemia cells treated with the HbF inducers hemin, trichostatin A, and sodium butanoate have significantly reduced mRNA levels of HDAC9 and its splice variant histone deacetylase-related protein
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knockdown of transactive response DNA-binding protein TDP-43 downregulates histone deacetylase 6 mRNA and protein expression and reduces HDAC6 enzyme activity in non-neuronal as well as in neuronal cells
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mutations of the SCF-CDC4 ubiquitin ligase complex suppress cell death by preventing the degradation of Msn2 and Msn4 transcription factors. Accumulation of transcription factors Msn2 and Msn4 leads to the induction of PNC1, which is an activator of the Sir2 histone acetylase
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no conclusions can be drawn for isoform HDAC2-2 after 0.1 mM salicylic acid treatment as transcripts levels increase both in treated and untreated plants at 6 and 24 h, but with no significant differences between them
nuclear HDAC activity is significantly higher in rheumatoid arthritis than in osteoarthritis and normal controls. The mRNA expression of HDAC1 in rheumatoid arthritis synovial tissue is higher than in osteoarthritis and normal controls, and shows positive correlation with tumor necrosis factor-alpha mRNA expression. Stimulation with tumor necrosis factor-alpha (10 ng/ml) significantly increases the nuclear HDAC activity and HDAC1 mRNA expression at 24 h and HDAC1 protein expression at 48 h in synovial fibroblasts from rheumatoid arthritis
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redox signaling, alkylation (carbonylation) of conserved cysteines inactivates class I histone deacetylases 1, 2, and 3. Covalent modification at Cys261 and Cys273 in HDAC1, coincides with attenuation of histone deacetylase activity
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responses of GmHDACs to abscisic acid (ABA) treatment, which is the most important stress-protective phytohormone, differ. Two HD2 family genes (GmHDT2 and GmHDT4) are induced and two RPD3/HDA1 family genes (GmHDA8 and GmHDA16) are markedly suppressed, the expression of five other HDAC genes (GmHDA6, 13, 14, GmSRT2 and GmSRT4) is only slightly modulated. The status of H3K4me2 and H3K4me3 is also modulated by the both cold and heat treatments. High levels of H3K4me2 and low levels of H3K4me3 are observed following cold treatment. The level of H3K4me2 is upregulated in response to heat stress, while this treatment only has a mild effect on H3K4me3 levels
A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69
the AhHDA1 encoding gene is upregulated by PEG-induced water limitation and ABA signaling
the hepatic enzyme activity is significantly increased in nuclear and cytoplasmic fractions following partial hepatectomy. Isoform-specific effects of partial hepatectomy on isozyme HDAC mRNA and protein expression, with increased isozyme expression of the class I HDACs, 1 and 8, and class II HDAC4 in regenerating liver. Hepatic expression of (class II) HDAC5 is unchanged after partial hepatectomy, HDAC5 exhibits transient nuclear accumulation in regenerating liver
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the immunohistochemical expression of nuclear HDAC1, HDAC2 and HDAC3 proteins increases stepwise in benign, borderline and malignant tumors of ovarian carcinoma. Cytoplasmic expression of HDAC1, 2 and 3 is significantly increased in carcinomas compared with benign tumors
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
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the enzyme might be a promising target for the development of novel anti-babesial drugs
medicine
medicine
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general inhibition of histone deacetylases alters the balance of T helper 1 and T helper 2 effector cell activation and migration
medicine
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inhibitors of histone deacetylase activity sensitize colon cancer cells to interferon gamma-induced apoptosis through cooperative negative regulation of the Bcl-x expression
medicine
knock-down of isoform HDAC8 expression by RNAi inhibits growth of human lung, colon, and cervical cancer cell lines
medicine
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a representative compound, (2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(2-pyrrolidin-1-ylethyl)-1H-benzimidazol-5-yl]prop-2-enamide, SB639, has demonstrated antitumor activity in a colon cancer xenograft model
medicine
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application of HDAC inhibitors in cancer cell lines and mouse model systems leads to interruption of the cell cycle, differentiation and apoptosis, clinical studies have shown tumor repression and improvement of patient symptoms without significant side effects
medicine
because of their fundamental role in gene expression, histone deacetylase proteins are promising targets for cancer treatment
medicine
-
class I and II HDACs are generally considered valuable therapeutic targets for the treatment of leukemia and solid tumors
medicine
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HDAC inhibition is a clinically validated therapeutic strategy for cancer treatment
medicine
-
HDAC inhibitors have attracted a great deal of interest as drug targets
medicine
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HDAC inhibitors have attracted a great deal of interest as drug targets in recent years
medicine
HDAC inhibitors in food may help reverse aberrant patterns of histone changes in cancer cells
medicine
HDACs are the most relevant, tractible cancer targets
medicine
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histone deacetylase activities are elevated in patients with primary myelofibrosis
medicine
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inhibition of HDAC activity has emerged as a promising approach for reversing the anomalous epigenetic states associated with cancer and other chronic diseases
medicine
it is proposed that induction of Hsp70 and subsequent activation of HDAC2 are important triggering signals of cardiac hypertrophy
medicine
type I ribosome-inactivating proteins derived from plants are HDAC inhibitors that can be utilized in the prevention and treatment of prostate cancer
medicine
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histone deacetylase 1 is a gene therapy target in pancreatic ductal adenocarcinoma
medicine
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compared with healthy non-smokers, HDAC activity in the peripheral blood mononuclear cells of patients with chronic obstructive pulmonary disease is decreased by 40%. In patients with chronic obstructive pulmonary disease, HDAC activity is negatively correlated to smoke intensity. In chronic obstructive pulmonary disease patients who have smoked for more than 40 pack-years, HDAC activity in peripheral blood mononuclear cells is 40% lower than that in chronic obstructive pulmonary disease patients who have smoked fewer than 40 pack-years. Serum CXCL8 levels in patients with chronic obstructive pulmonary disease are significantly higher than that in controls and are negatively correlated to HDAC activities
medicine
HDAC2 is nitrated under nitrative/oxidative stress and in the peripheral lung tissues of smokers and patients with chronic obstructive pulmonary disease
medicine
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loss of class IIa HDACs in murine liver results in inhibition of FOXO target genes and lowers blood glucose, resulting in increased glycogen storage. Suppression of class IIa HDACs in mouse models of type 2 diabetes ameliorates hyperglycemia, suggesting that inhibitors of class I/II HDACs may be potential therapeutics for metabolic syndrome
medicine
1,2,4-oxadiazole-containing hydroxamic acid derivatives are discovered as histone deacetylase inhibitors for potential application in cancer therapy
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Release 2023.1 (January 2023)
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