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Information on EC 3.5.1.98 - histone deacetylase and Organism(s) Homo sapiens and UniProt Accession Q13547

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.98 histone deacetylase
IUBMB 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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This record set is specific for:
Homo sapiens
UNIPROT: Q13547
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
class II histone deacetylase
-
histone deacetylase
-
histone deacetylase 1
-
histone deacetylase-1
-
histone deacetylase1
-
acetyl-lysine deacetylase
-
class I acetyl-lysine deacetylase
-
class I histone deacetylase
-
-
class II histone deacetylase
-
class IIa HDAC
-
class IIa histone deacetylase
-
cytoplasmic deacetylase
-
-
HDAC1
HDAC10
-
-
HDAC2
HDAC3
HDAC4
HDAC5
-
-
HDAC6
HDAC6p114
-
splicing variant of histone deacetylase 6 lacking the first 152 amino acids from N-terminus in the major isoform HDAC6p131 protein
HDAC6p131
-
major isoform of histone deacetylase 6
HDAC7
HDAC8
histone deacetylase
histone deacetylase 1
-
-
histone deacetylase 10
-
a class IIb histone deacetylase
histone deacetylase 2
histone deacetylase 3
histone deacetylase 4
-
-
histone deacetylase 6
histone deacetylase 7
histone deacetylase 8
histone deacetylase-7
-
-
tubulin deacetylase
-
-
Zn(II)-dependent deacetylase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deacetylation
hydrolysis
deacetylation
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9076-57-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Boc-acetyl-Lys-7-amido-4-methylcoumarin + H2O
Boc-acetyl-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Fluor de Lys HDAC substrate + H2O
?
show the reaction diagram
-
-
-
?
AAKAVGK(Ac)VIPELN + H2O
AAKAVGKVIPELN + acetate
show the reaction diagram
-
-
-
?
Ac-DQK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-FEK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-GGK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-GS(PO3)K(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-GSK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-IHK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-ILK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-KGK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-KSK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-KWK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-KYK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-LIK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-LYK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-PFK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-VLK(acetyl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-GAK(acetyl)-7-amido-4-methylcoumarin + H2O
acetyl-GAK-7-amino-4-methylcoumarin + acetate
show the reaction diagram
-
-
-
?
acetyl-tubulin + H2O
tubulin + acetate
show the reaction diagram
-
major HDAC6 substrate
-
-
?
acetylated histone + H2O
acetate + histone
show the reaction diagram
-
-
-
-
?
AFKFFQK(Ac)DRKMAL + H2O
AFKFFQKDRKMAL + acetate
show the reaction diagram
-
-
-
?
alpha-tubulin + H2O
?
show the reaction diagram
-
splicing variant HDAC6p114 is intact in its deacetylase activity against a-tubulin
-
-
?
alpha-tubulin + H2O
acetate + ?
show the reaction diagram
-
-
-
-
?
ASKRAFK(Ac)QSPPAV + H2O
ASKRAFKQSPPAV + acetate
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Lys-7-amido-4-methylcoumarin + acetate
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Lys(trifluoroacetyl)-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Lys-7-amido-4-methylcoumarin + trifluoroacetate
show the reaction diagram
-
-
-
-
?
Boc-Lys(ac)-coumarin + H2O
Boc-Lys-coumarin + acetate
show the reaction diagram
i.e. Boc-K(ac)-Fluor-de-Lys
-
-
?
Boc-trifluoroacetyl-Lys-7-amido-4-methylcoumarin + H2O
Boc-trifluoroacetyl-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
CKDLK(ac)RLFS + H2O
CKDLKRLFS + acetate
show the reaction diagram
i.e. CREB94
-
-
?
DPGNEVK(Ac)LKLYAL + H2O
DPGNEVKLKLYAL + acetate
show the reaction diagram
-
-
-
?
EANPGEK(Ac)RKMTDS + H2O
EANPGEKRKMTDS + acetate
show the reaction diagram
-
-
-
?
Fluor de Lys + H2O
?
show the reaction diagram
Fluor de Lys H4-AcK16 + H2O
?
show the reaction diagram
-
-
-
-
?
Fluor de Lys HDAC substrate + H2O
?
show the reaction diagram
Fluor de Lys HDAC8 substrate + H2O
?
show the reaction diagram
GATYQDK(Ac)RYTNKY + H2O
GATYQDKRYTNKY + acetate
show the reaction diagram
-
-
-
?
GFGNGMK(Ac)QMRRTW + H2O
GFGNGMKQMRRTW + acetate
show the reaction diagram
-
-
-
?
GGK(Ac)FF + H2O
GGKFF + acetate
show the reaction diagram
-
-
-
?
GGMRGMK(Ac)GLVYET + H2O
GGMRGMKGLVYET + acetate
show the reaction diagram
-
-
-
?
GK(Ac)F + H2O
GKF + acetate
show the reaction diagram
-
-
-
?
HGGTILK(Ac)MIEEAG + H2O
HGGTILKMIEEAG + acetate
show the reaction diagram
-
-
-
?
LGDGK(ac)MKS + H2O
LGDGKMKS + acetate
show the reaction diagram
i.e. THRAP3, low activity
-
-
?
LGK(ac)FRR + H2O
LGKFRR + acetate
show the reaction diagram
i.e. La-related protein 1, LARP1, best peptide substrate
-
-
?
LYDRGTK(Ac)FGLFTP + H2O
LYDRGTKFGLFTP + acetate
show the reaction diagram
-
-
-
?
N-acetyl-arginine-histidine-acetyl-lysine-acetyl-lysine-coumarin + H2O
?
show the reaction diagram
substrate in crystallized enzyme-substrate complex
-
-
?
N-acetyl-lysine-alpha-tubulin + H2O
acetate + alpha-tubulin
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-heat shock protein 90 + H2O
acetate + heat shock protein 90
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-histone H3 + H2O
acetate + histone H3
show the reaction diagram
N-acetyl-lysine-histone H3 + H2O
histone H3 + acetate
show the reaction diagram
-
deacetylation occurs at Lys9 and Lys23
-
-
?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-MyoD + H2O
acetate + MyoD
show the reaction diagram
N6-lysine acetylated histone H2A + H2O
histone H2A + acetate
show the reaction diagram
-
substrate of isoforms HDAC1, HDAC2, HDAC. Isoform HDAC3 preferentially cleeaves lysines 5 H2A
-
-
?
N6-lysine acetylated histone H3 + H2O
histone H3 + acetate
show the reaction diagram
N6-lysine acetylated histone H4 + H2O
histone H4 + acetate
show the reaction diagram
N6-lysine acetylated histone H4 peptide + H2O
histone H4 peptide + acetate
show the reaction diagram
peptide of N-terminal 20 amino acids
-
-
?
N6-lysine-acetylated histone H4 peptide + H2O
acetate + histone H4 peptide
show the reaction diagram
-
-
-
?
NARRKPK(Ac)GSPRVP + H2O
NARRKPKGSPRVP + acetate
show the reaction diagram
-
-
-
?
QSVQPSK(Ac)FNSYGR + H2O
QSVQPSKFNSYGR + acetate
show the reaction diagram
-
-
-
?
QTSPNPK(Ac)YRGFFH + H2O
QTSPNPKYRGFFH + acetate
show the reaction diagram
-
-
-
?
RGGK(Ac)FFR + H2O
RGGKFFR + acetate
show the reaction diagram
-
-
-
?
RHK(ac)K(ac)-coumarin + H2O
RHKK-coumarin + 2 acetate
show the reaction diagram
i.e. HDAC8 Fluor-de-Lys or HDAC8 p53 FdL, low activity
-
-
?
RHK(acetyl)K(acetyl)-fluorophore + H2O
RHKK-fluorophore + acetate
show the reaction diagram
RHKK(ac)-coumarin + H2O
RHKK-coumarin + acetate
show the reaction diagram
i.e. SIRT1 Fluor-de-Lys
-
-
?
RIANRTK(Ac)NSLTLQ + H2O
RIANRTKNSLTLQ + acetate
show the reaction diagram
-
-
-
?
RINSGGK(Ac)LPNFGF + H2O
RINSGGKLPNFGF + acetate
show the reaction diagram
-
-
-
?
RSLKYGK(Ac)VSPSLV + H2O
RSLKYGKVSPSLV + acetate
show the reaction diagram
-
-
-
?
RTSGRDK(Ac)YGPPVR + H2O
RTSGRDKYGPPVR + acetate
show the reaction diagram
-
-
-
?
RTSLGPK(Ac)SMMKML + H2O
RTSLGPKSMMKML + acetate
show the reaction diagram
-
-
-
?
RVIGAKK(ac)DQ + H2O
RVIGAKKDQ + acetate
show the reaction diagram
a SMC3 9mer
-
-
?
RVIGAKK(ac)DQY + H2O
RVIGAKKDQY + acetate
show the reaction diagram
a SMC3 10mer
-
-
?
RYSSRRK(Ac)ARPYML + H2O
RYSSRRKARPYML + acetate
show the reaction diagram
-
-
-
?
SQSEEEK(Ac)FFRRFP + H2O
SQSEEEKFFRRFP + acetate
show the reaction diagram
-
-
-
?
SRGGK(Ac)FFRR + H2O
SRGGKFFRR + acetate
show the reaction diagram
-
-
-
?
STPRFGK(Ac)TFDAPP + H2O
STPRFGKTFDAPP + acetate
show the reaction diagram
-
-
-
?
STPVK(ac)FISR + H2O
STPVKFISR + acetate
show the reaction diagram
i.e. CSRP2BP
-
-
?
tert-butyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Lys-7-amido-4-methylcoumarin + acetate
show the reaction diagram
-
-
-
?
TGKYFDK(Ac)ASYRVY + H2O
TGKYFDKASYRVY + acetate
show the reaction diagram
-
-
-
?
TKQTARK(ac)STGGKA + H2O
TKQTARKSTGGKA + acetate
show the reaction diagram
a H3K9 13mer
-
-
?
TLKKTGK(Ac)TVSYLG + H2O
TLKKTGKTVSYLG + acetate
show the reaction diagram
-
-
-
?
TYSRGGK(Ac)FFRRFP + H2O
TYSRGGKFFRRFP + acetate
show the reaction diagram
-
-
-
?
TYSRGGK(Ac)KSEESE + H2O
TYSRGGKKSEESE + acetate
show the reaction diagram
-
-
-
?
VLRNGGK(Ac)NFPAIF + H2O
VLRNGGKNFPAIF + acetate
show the reaction diagram
-
-
-
?
VRGFGGK(Ac)FGVQMD + H2O
VRGFGGKFGVQMD + acetate
show the reaction diagram
-
-
-
?
WEALGGK(Ac)AAYRTS + H2O
WEALGGKAAYRTS + acetate
show the reaction diagram
-
-
-
?
YSRGGK(Ac)FFRRF + H2O
YSRGGKFFRRF + acetate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-tubulin + H2O
?
show the reaction diagram
-
splicing variant HDAC6p114 is intact in its deacetylase activity against a-tubulin
-
-
?
alpha-tubulin + H2O
acetate + ?
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-alpha-tubulin + H2O
acetate + alpha-tubulin
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-heat shock protein 90 + H2O
acetate + heat shock protein 90
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-histone H3 + H2O
acetate + histone H3
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-MyoD + H2O
acetate + MyoD
show the reaction diagram
-
transcription factor MyoD, its activity is co-dependent on isoform HDAC1 and transcriptional co-activator P/CAF
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,5S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-6-oxabicyclo[3.1.1]heptane-3-carboxamide
(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-{[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
-
(2R)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
-
(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-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,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
-
(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
65% inhibition at 100 nM
(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
61% inhibition at 100 nM
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenylamide
-
2-(((3-(1-(2,4-difluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
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
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
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
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
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
92% inhibition at 100 nM
2-(((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
96% inhibition at 100 nM
2-(4-((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacetamide
18% inhibition at 100 nM
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
3-(4-((3-(1-(2-chlorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
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
3-(4-((3-(1-(2-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
31% 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
3-(4-((3-(1-(3-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
35% inhibition at 100 nM
3-(4-((3-(1-(4-bromobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
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
3-(4-((3-(1-allylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
34% inhibition at 100 nM
3-(4-((3-(1-allylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxypropanamide
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
3-(4-((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
35% inhibition at 100 nM
4-((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)-N-hydroxybenzamide
29% inhibition at 100 nM
belinostat
i.e. PXD-101
chidamide
entinostat
-
HDAC1 siRNA
-
-
MC1568
specificity for class II HDACs
MC1575
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
-
mocetinostat
-
MS-275
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, possesses kinetic selectivity for isozyme HDAC1 versus HDAC2, inhibition kinetics
N-(4-amino[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
-
N-hydroxy-2-(methyl((3-(1-(3-methylbenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)amino)pyrimidine-5-carboxamide
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
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
96% inhibition at 100 nM
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
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
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
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
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
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
N-hydroxy-3-(4-((3-(1-propylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)acrylamide
40% inhibition at 100 nM
N-hydroxy-3-(4-((3-(1-propylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)propanamide
5% inhibition at 100 nM
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-6-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}hexanamide
-
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-N~3~-[5-(propan-2-yl)naphthalene-1-sulfonyl]-beta-alaninamide
-
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-[2-amino-5-(pyridin-3-yl)phenyl]oxane-4-carboxamide
-
N-[2-amino-5-(pyridin-4-yl)phenyl]oxane-4-carboxamide
-
N-[4-amino-4'-(trifluoromethyl)[1,1'-biphenyl]-3-yl]oxane-4-carboxamide
-
panobinostat
resminostat
-
romidepsin
i.e. FK-228
SAHA
i.e. vorinostat
suberoylanilide hydroxamic acid
suberoylanilide trifluoromethylketone
-
trichostatin A
vorinostat
-
(1R,5S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-6-oxabicyclo[3.1.1]heptane-3-carboxamide
(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-[2-(2-phenylethyl)-1-(pyridin-2-ylmethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
(2E)-N-hydroxy-3-naphthalen-1-ylprop-2-enamide
-
HDAC8-selective inhibitor
(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)-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-(2-phenylethyl)-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
(2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide
-
(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)-8-oxo-2-[(3-piperidin-1-ylpropanoyl)amino]-N-quinolin-3-ylnonanamide
-
-
(2S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-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
(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
(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
-
-
1-[5-(4-acetylphenyl)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-(2-phenyl-1,3-thiazol-5-yl)ethanone
-
-
2,2,2-trifluoro-1-(4-phenylthiophen-2-yl)ethanone
-
-
2,2,2-trifluoro-1-(5-phenylthiophen-2-yl)ethanone
-
-
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-(1H-indol-5-yl)thiophen-2-yl]ethanone
-
-
2,2,2-trifluoro-1-[5-(2-methoxyphenyl)thiophen-2-yl]ethanone
-
-
2,2,2-trifluoro-1-[5-(3-methoxyphenyl)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
-
-
2,2,2-trifluoro-1-[5-(4-methoxyphenyl)thiophen-2-yl]ethanone
-
-
2,2,2-trifluoro-1-[5-(pyridin-2-yl)thiophen-2-yl]ethanone
-
-
2,2,2-trifluoro-1-[5-(quinoxalin-6-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
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenylamide
-
2,3-dihydrobenzoic acid
98% residual activity at 0.5 mM
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
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
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
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
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
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
2-(((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methyl)(methyl)amino)-N-hydroxypyrimidine-5-carboxamide
63% 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
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
-
-
2-hydroxybutyric acid
96% residual activity at 0.5 mM
2-[(methylsulfonyl)sulfanyl]ethanaminium bromide
-
-
2-[(methylsulfonyl)sulfanyl]ethyl 2-propylpentanoate
-
-
3,4-Dihydroxyphenyl acetic acid
90% residual activity at 0.5 mM
3-(1-methyl-4-phenylacetyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamide
APHA
3-(4-((3-(1-(2,4-difluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
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
3-(4-((3-(1-(2-cyanobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
65% inhibition at 100 nM
3-(4-((3-(1-(2-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
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
60% inhibition at 100 nM
3-(4-((3-(1-(3-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
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
3-(4-((3-(1-(4-fluorobenzyl)piperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
75% inhibition at 100 nM
3-(4-((3-(1-allylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
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
3-(4-((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N- hydroxypropanamide
22% inhibition at 100 nM
3-(4-((3-(1-benzylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)-N-hydroxyacrylamide
71% inhibition at 100 nM
3-hydroxycinnamic acid
96% residual activity at 0.5 mM
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
66% inhibition at 100 nM
4-(3-thioxo-3H-1,2-dithiol-5-yl)phenyl 2-propylpentanoate
-
-
4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide
M344
4-hydroxy-2-nonenal
-
maximal inhibition of recombinant HDAC3 in complex with CoR1 is 70%
4-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
-
-
4-[5-(trifluoroacetyl)thiophen-2-yl]benzonitrile
-
-
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
-
5-(4-benzyl-1H-1,2,3-triazol-1-yl)-N-hydroxypentanamide
-
-
5-(4-hydroxyphenyl)-3H-1,2-dithiol-3-thione
-
-
6-mercapto-N-phenylhexanamide
-
6-[(1-(mercaptomethyl)vinyl)amino]-N-phenylhexanamide
-
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-[(9H-fluoren-3-ylmethyl)(3-phenoxybenzyl)amino]-N-hydroxyhexanamide
-
-
6-[(biphenyl-4-ylmethyl)[4-[(4-bromobenzyl)oxy]benzyl]amino]-N-hydroxyhexanamide
-
-
6-[4-(2,6-dimethoxyphenyl)-1H-1,2,3-triazol-1-yl]-N-hydroxyhexanamide
-
-
6-[4-(biphenyl-2-yl)-1H-1,2,3-triazol-1-yl]-N-hydroxyhexanamide
-
-
6-[4-(biphenyl-3-yl)-1H-1,2,3-triazol-1-yl]-N-hydroxyhexanamide
-
-
6-[4-(biphenyl-4-yl)-1H-1,2,3-triazol-1-yl]-N-hydroxyhexanamide
-
-
6-[[4-[(4-bromobenzyl)oxy]benzyl](9H-fluoren-3-ylmethyl)amino]-N-hydroxyhexanamide
-
-
6-{4-[4-(dimethylamino)phenyl]-1H-1,2,3-triazol-1-yl}-N-hydroxyhexanamide
-
-
7-mercapto-N-(2-phenyl-1,3-thiazol-5-yl)heptanamide
-
7-mercapto-N-(3-phenoxyphenyl)heptanamide
-
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-mercapto-N-pyridin-3-ylheptanamide
-
7-mercapto-N-quinolin-3-ylheptanamide
-
7-[4-(biphenyl-3-yl)-1H-1,2,3-triazol-1-yl]-N-hydroxyheptanamide
-
-
7-{4-[4-(dimethylamino)phenyl]-1H-1,2,3-triazol-1-yl}-N-hydroxyheptanamide
-
-
8-hydroxyquinoline
85% residual activity at 0.5 mM
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
apicidin
apicidin A
-
-
azumamide A
-
-
azumamide E
-
-
Baclofen
98% residual activity at 0.5 mM
belinostat
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
Butyrate
Butyric acid
caffeic acid
80% residual activity at 0.5 mM
chlorogenic acid
highly potent HDAC inhibitor, 40% residual activity at 0.5 mM
Cinnamic acid
95% residual activity at 0.5 mM
curcumin
highly potent HDAC inhibitor, 52% residual activity at 0.5 mM
D-(-)-quinic acid
96% residual activity at 0.5 mM
dihydrocaffeic acid
86% residual activity at 0.5 mM
entinostat
-
MS-275
ferulic acid
80% residual activity at 0.5 mM
FK-228
FK228
-
-
FOXP
-
FOXP3 specifically inhibits binding of histone deacetylase 2 and 4 to the site and increases local histone H3 acetylation
-
FR235222
-
-
FR901375
-
-
gamma-aminobutyric acid
-
HC-toxin
-
-
indol-2-carboxylic acid
97% residual activity at 0.5 mM
isobutyric acid
80% residual activity at 0.5 mM
Isothiocyanate
found in cruciferous vegetables
ITF-2357
JNJ-26481585
-
broad-spectrum or pan-HDAC inhibitor
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
LAQ-824
-
-
LAQ824
largazole
LBH-589
LBH589
Mandelic acid
85% residual activity at 0.5 mM
MC1568
specificity for class II HDACs
MC1575
specificity for class II HDACs
MC1863
-
-
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-0103
MS-275
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-aminophenyl)-6-(6-oxo-4-phenyl-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
N-(4-aminopyrimidin-5-yl)-5-[(6-oxo-4-phenyl-1,6-dihydropyrimidin-2-yl)sulfanyl]pentanamide
-
-
N-(4-amino[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
-
N-(6-mercaptohexyl)-1-benzofuran-2-carboxamide
-
N-(6-mercaptohexyl)-1H-indole-2-carboxamide
-
N-(6-mercaptohexyl)-2-naphthamide
-
N-(6-mercaptohexyl)benzamide
-
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-biphenyl-3-yl-7-mercaptoheptanamide
-
N-hydroxy-1-(3-hydroxypropyl)-2-(2-phenylethyl)-1H-benzimidazole-5-carboxamide
-
-
N-hydroxy-1-methyl-indole-6-carboxamide
-
HDAC8-selective inhibitor
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
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
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
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
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
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
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
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
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
28% inhibition at 100 nM
N-hydroxy-3-(4-((3-(1-propylpiperidin-4-yl)-1,2,4-oxadiazol-5-yl)methoxy)phenyl)acrylamide
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
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-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
-
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-4-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}butanamide
-
N-hydroxy-5-(4-phenyl-1H-1,2,3-triazol-1-yl)pentanamide
-
-
N-hydroxy-5-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}pentanamide
-
N-hydroxy-6-(4-phenyl-1H-1,2,3-triazol-1-yl)hexanamide
-
-
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-6-[4-(2-methoxyphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-[4-(3-methoxyphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-[4-(3-methylphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-[4-(4-methoxyphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-[4-(4-methylphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-[4-(6-methoxynaphthalen-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-[4-(pyridin-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-[4-(pyridin-3-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-[4-(pyridin-4-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-[4-(quinolin-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-[4-(quinolin-7-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-[4-(thiophen-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
N-hydroxy-6-{4-[4-(pyridin-4-yl)phenyl]-1H-1,2,3-triazol-1-yl}hexanamide
-
-
N-hydroxy-6-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}hexanamide
-
N-hydroxy-7-(4-phenyl-1H-1,2,3-triazol-1-yl)heptanamide
-
-
N-hydroxy-7-[4-(6-methoxynaphthalen-2-yl)-1H-1,2,3-triazol-1-yl]heptanamide
-
-
N-hydroxy-7-[4-(pyridin-2-yl)-1H-1,2,3-triazol-1-yl]heptanamide
-
-
N-hydroxy-7-{4-[4-(pyridin-4-yl)phenyl]-1H-1,2,3-triazol-1-yl}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-N~3~-[5-(propan-2-yl)naphthalene-1-sulfonyl]-beta-alaninamide
-
N-hydroxynaphthalene-1-carboxamide
-
HDAC8-selective inhibitor
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-[2-amino-5-(pyridin-3-yl)phenyl]oxane-4-carboxamide
-
N-[2-amino-5-(pyridin-4-yl)phenyl]oxane-4-carboxamide
-
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
N1-hydroxy-N8-(5-phenyl-1,3,4-thiadiazol-2-yl)octanediamide
-
-
N1-methyl-2-oxo-N9-phenylnonanediamide
-
NVP-LAQ824
-
oxamflatin
-
p300
-
p300 can inactivate HDAC6 by acetylation
-
panobinostat
PAOA
-
-
PCI-24781
-
broad-spectrum or pan-HDAC inhibitor
PCI-34051
-
HDAC8-selective inhibitor
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
phenyl butyric acid
-
phenylbutyrate
Buphenyl
phenylbutyric acid
-
propionic acid
80% residual activity at 0.5 mM
PXD-101
PXD101
-
-
pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
i.e. MS27-275
romidepsin
S-(2-hydroxyethyl) methanesulfonothioate
-
-
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-[2-[(2-propylpentanoyl)amino]ethyl]methanesulfonothioate
-
-
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
salicylic acid
92% residual activity at 0.5 mM
scriptaid
-
-
shRNA
-
-
-
SK7041
-
i.e. 4-dimethylamino-N-[4-(2-hydroxylcarbamoyl-vinyl)benzyl] benzamide
sodium butyrate
sodium phenylbutyrate
-
sorbic acid
91% residual activity at 0.5 mM
spiruchostatin
-
-
suberoyl anilide hydroxamic acid
suberoylanilide hydroxamic acid
suberoylanilide trifluoromethylketone
-
sulforaphane
tartaric acid
90% residual activity at 0.5 mM
trapoxin
trapoxin A
-
-
trapoxin B
trichostatin A
troglitazone
-
-
tubacin
Valeric acid
83% residual activity at 0.5 mM
Valproate
-
class I-selective HDAC inhibitor
Valproic acid
vorinostat
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066 - 0.088
Fluor de Lys HDAC substrate
-
0.00244 - 0.01646
Ac-DQK(acetyl)-7-amido-4-methylcoumarin
0.00228 - 0.0359
Ac-FEK(acetyl)-7-amido-4-methylcoumarin
0.0043 - 0.0877
Ac-GGK(acetyl)-7-amido-4-methylcoumarin
0.0123 - 0.0666
Ac-GS(PO3)K(acetyl)-7-amido-4-methylcoumarin
0.00405 - 0.0241
Ac-GSK(acetyl)-7-amido-4-methylcoumarin
0.00069 - 0.108
Ac-IHK(acetyl)-7-amido-4-methylcoumarin
0.0124
Ac-ILK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC3
0.0054
Ac-KGK(acetyl)-7-amido-4-methylcoumarin
-
isoform FB188 HDAH
0.019
Ac-KSK(acetyl)-7-amido-4-methylcoumarin
-
isoform FB188 HDAH
0.005
Ac-KWK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1
0.0044 - 0.107
Ac-KYK(acetyl)-7-amido-4-methylcoumarin
0.00303
Ac-LIK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1
0.0069 - 0.03
Ac-LYK(acetyl)-7-amido-4-methylcoumarin
0.01
Ac-PFK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC8
0.0119 - 0.0221
Ac-VLK(acetyl)-7-amido-4-methylcoumarin
0.078 - 0.099
benzyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin
0.03 - 0.061
benzyloxycarbonyl-L-Lys(trifluoroacetyl)-7-amido-4-methylcoumarin
0.000015 - 0.0038
Fluor de Lys
-
0.013 - 0.017
Fluor de Lys HDAC substrate
-
0.14 - 1.1
Fluor de Lys HDAC8 substrate
-
0.0351
GGK(Ac)FF
pH 7.4, 37°C, recombinant enzyme
0.0517
GK(Ac)F
pH 7.4, 37°C, recombinant enzyme
0.0128
RGGK(Ac)FFR
pH 7.4, 37°C, recombinant enzyme
0.16 - 1.1
RHK(acetyl)K(acetyl)-fluorophore
0.0195
RYSSRRK(Ac)ARPYML
pH 7.4, 37°C, recombinant enzyme
0.021
SQSEEEK(Ac)FFRRFP
pH 7.4, 37°C, recombinant enzyme
0.0122
SRGGK(Ac)FFRR
pH 7.4, 37°C, recombinant enzyme
0.0056
TYSRGGK(Ac)FFRRFP
pH 7.4, 37°C, recombinant enzyme
0.0687
TYSRGGK(Ac)KSEESE
pH 7.4, 37°C, recombinant enzyme
0.0104
YSRGGK(Ac)FFRRF
pH 7.4, 37°C, recombinant enzyme
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019 - 0.29
Fluor de Lys
-
0.0002 - 1.1
Fluor de Lys HDAC substrate
-
0.007 - 1.2
Fluor de Lys HDAC8 substrate
-
1.09
GGK(Ac)FF
pH 7.4, 37°C, recombinant enzyme
1.88
GK(Ac)F
pH 7.4, 37°C, recombinant enzyme
1.53
RGGK(Ac)FFR
pH 7.4, 37°C, recombinant enzyme
0.48 - 1.2
RHK(acetyl)K(acetyl)-fluorophore
0.92
RYSSRRK(Ac)ARPYML
pH 7.4, 37°C, recombinant enzyme
0.02
SQSEEEK(Ac)FFRRFP
pH 7.4, 37°C, recombinant enzyme
2.28
SRGGK(Ac)FFRR
pH 7.4, 37°C, recombinant enzyme
0.71
TYSRGGK(Ac)FFRRFP
pH 7.4, 37°C, recombinant enzyme
0.12
TYSRGGK(Ac)KSEESE
pH 7.4, 37°C, recombinant enzyme
1.66
YSRGGK(Ac)FFRRF
pH 7.4, 37°C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31.1
GGK(Ac)FF
pH 7.4, 37°C, recombinant enzyme
36.36
GK(Ac)F
pH 7.4, 37°C, recombinant enzyme
119.5
RGGK(Ac)FFR
pH 7.4, 37°C, recombinant enzyme
47.18
RYSSRRK(Ac)ARPYML
pH 7.4, 37°C, recombinant enzyme
0.95
SQSEEEK(Ac)FFRRFP
pH 7.4, 37°C, recombinant enzyme
186.9
SRGGK(Ac)FFRR
pH 7.4, 37°C, recombinant enzyme
126.78
TYSRGGK(Ac)FFRRFP
pH 7.4, 37°C, recombinant enzyme
1.75
TYSRGGK(Ac)KSEESE
pH 7.4, 37°C, recombinant enzyme
159.6
YSRGGK(Ac)FFRRF
pH 7.4, 37°C, recombinant enzyme
additional information
additional information
substrate specifcity, catalytic efficiencies with different peptides substrates of the enzyme with bound Fe2+ and/or Zn2+, overview
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0007
(2E)-N-hydroxy-3-naphthalen-1-ylprop-2-enamide
-
HDAC8 inhibition
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
0.0007
7-mercapto-N-phenylheptanamide
-
0.024
allyl mercaptan
human HDAC8
0.046
Butyrate
-
0.136
Butyric acid
pH and temperature not specified in the publication
0.01084
caffeic acid
pH and temperature not specified in the publication
0.000135
chlorogenic acid
pH and temperature not specified in the publication
0.00000821
Cinnamic acid
pH and temperature not specified in the publication
0.000539
curcumin
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
0.0013 - 0.0085
N-hydroxy-1-methyl-indole-6-carboxamide
0.014
N-hydroxynaphthalene-1-carboxamide
-
HDAC8 inhibition
0.000015
PCI-34051
-
HDAC8 inhibition
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
0.000044 - 0.00025
suberoylanilide hydroxamic acid
0.000504
trichostatin A
pH and temperature not specified in the publication
0.564
Valproic acid
pH and temperature not specified in the publication
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000192 - 0.00145
(1R,5S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-6-oxabicyclo[3.1.1]heptane-3-carboxamide
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
0.00143
(2S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.00011
(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
-
0.00027
(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
-
0.03
(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
0.023
(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
-
0.0000012
(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
-
0.00000032
(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
-
0.0000019
(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
-
0.0012
(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
-
0.00000069
(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
-
0.000077
(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
-
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
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
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
0.000045
MS-275
Homo sapiens
-
0.00967
N-(4-amino-3'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.00152
N-(4-amino-4'-chloro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 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
0.000072
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
0.000123
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
0.00122 - 0.00559
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-3-carboxamide
0.00002
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.000119
N-(4-amino[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
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
0.00067
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
-
0.001
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
-
0.00645
N-[2-amino-5-(pyridin-3-yl)phenyl]oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 isozyme
0.00235
N-[2-amino-5-(pyridin-4-yl)phenyl]oxane-4-carboxamide
Homo sapiens
pH 7.4, 22°C, HDAC1 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
0.00001
suberoylanilide hydroxamic acid
Homo sapiens
-
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
0.00002 - 0.0043
(2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide
0.00129 - 0.00573
(2R)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
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
0.00145 - 0.00595
(2S)-N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-2-carboxamide
0.00058 - 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
0.0041 - 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
0.0000034 - 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
0.00000086 - 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
0.0000038 - 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
0.0019 - 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
0.0000015 - 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]
0.000085 - 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
0.000029 - 0.072
1-[5-(4-acetylphenyl)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
0.00013 - 0.0037
2,2,2-trifluoro-1-(2-phenyl-1,3-thiazol-5-yl)ethanone
0.0019 - 0.01
2,2,2-trifluoro-1-(4-phenylthiophen-2-yl)ethanone
0.00017 - 0.02
2,2,2-trifluoro-1-(5-phenylthiophen-2-yl)ethanone
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
0.005 - 0.01
2,2,2-trifluoro-1-[5-(1H-indol-5-yl)thiophen-2-yl]ethanone
0.0063 - 0.01
2,2,2-trifluoro-1-[5-(2-methoxyphenyl)thiophen-2-yl]ethanone
0.0031 - 0.01
2,2,2-trifluoro-1-[5-(3-methoxyphenyl)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
0.00011 - 0.001
2,2,2-trifluoro-1-[5-(4-methoxyphenyl)thiophen-2-yl]ethanone
0.00054 - 0.001
2,2,2-trifluoro-1-[5-(pyridin-2-yl)thiophen-2-yl]ethanone
0.000015 - 0.00091
2,2,2-trifluoro-1-[5-(quinoxalin-6-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
0.198
2-[(methylsulfonyl)sulfanyl]ethanaminium bromide
Homo sapiens
-
-
0.0096
2-[(methylsulfonyl)sulfanyl]ethyl 2-propylpentanoate
Homo sapiens
-
-
0.00007 - 0.0128
3-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
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
0.0564
4-(3-thioxo-3H-1,2-dithiol-5-yl)phenyl 2-propylpentanoate
Homo sapiens
-
-
0.14
4-hydroxy-2-nonenal
Homo sapiens
-
recombinant HDAC3 in complex with CoR1, pH and temperature not specified in the publication
0.000027 - 0.074
4-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
0.000041 - 0.0027
4-[5-(trifluoroacetyl)thiophen-2-yl]benzonitrile
0.04316
4-[[(2E)-2-(4-chlorobenzylidene)hydrazinyl]carbonothioyl]-N-hydroxypiperazine-1-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00045
5-(4-hydroxyphenyl)-3H-1,2-dithiol-3-thione
Homo sapiens
-
ADTOH
0.00037
6-mercapto-N-phenylhexanamide
Homo sapiens
37°C
0.00039
6-[(1-(mercaptomethyl)vinyl)amino]-N-phenylhexanamide
Homo sapiens
37°C
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
-
-
0.0001626
6-[4-(biphenyl-2-yl)-1H-1,2,3-triazol-1-yl]-N-hydroxyhexanamide
Homo sapiens
-
-
0.0000019
6-[4-(biphenyl-3-yl)-1H-1,2,3-triazol-1-yl]-N-hydroxyhexanamide
Homo sapiens
-
-
0.0000524
6-[4-(biphenyl-4-yl)-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
-
-
0.00017
7-mercapto-N-(2-phenyl-1,3-thiazol-5-yl)heptanamide
Homo sapiens
37°C
0.00021
7-mercapto-N-(3-phenoxyphenyl)heptanamide
Homo sapiens
37°C
0.00021
7-mercapto-N-phenylheptanamide
Homo sapiens
37°C
0.00011
7-mercapto-N-pyridin-3-ylheptanamide
Homo sapiens
37°C
0.000072
7-mercapto-N-quinolin-3-ylheptanamide
Homo sapiens
37°C
0.0000054
7-[4-(biphenyl-3-yl)-1H-1,2,3-triazol-1-yl]-N-hydroxyheptanamide
Homo sapiens
-
-
0.0001061
7-{4-[4-(dimethylamino)phenyl]-1H-1,2,3-triazol-1-yl}-N-hydroxyheptanamide
Homo sapiens
-
-
0.0000007 - 0.01
apicidin
0.02
beta-methylselenopyruvate
Homo sapiens
HDAC8, at 37°C, pH not specified in the publication
0.35
Butyrate
Homo sapiens
pH 8.0
2.54
caffeic acid
Homo sapiens
pH and temperature not specified in the publication
0.375
chlorogenic acid
Homo sapiens
pH and temperature not specified in the publication
0.115
curcumin
Homo sapiens
pH and temperature not specified in the publication
0.0036 - 0.553
LAQ824
0.00013 - 0.0154
LBH589
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
0.00012 - 0.03
MS-275
0.0123 - 0.033
N-(4-amino-3'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
0.00253 - 0.0142
N-(4-amino-4'-chloro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
0.000119 - 0.0259
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-1H-2-benzopyran-3-carboxamide
0.000156 - 0.033
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3,4-dihydro-2H-1-benzopyran-3-carboxamide
0.000219 - 0.00149
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)-3-oxabicyclo[3.1.0]hexane-6-carboxamide
0.00473 - 0.0198
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-3-carboxamide
0.000062 - 0.00109
N-(4-amino-4'-fluoro[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
0.000312 - 0.00385
N-(4-amino[1,1'-biphenyl]-3-yl)oxane-4-carboxamide
0.000079
N-(6-mercaptohexyl)-1-benzofuran-2-carboxamide
Homo sapiens
37°C
0.0001
N-(6-mercaptohexyl)-1H-indole-2-carboxamide
Homo sapiens
37°C
0.000085
N-(6-mercaptohexyl)-2-naphthamide
Homo sapiens
37°C
0.00036
N-(6-mercaptohexyl)benzamide
Homo sapiens
37°C
0.000075
N-biphenyl-3-yl-7-mercaptoheptanamide
Homo sapiens
37°C
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
0.00011
N-hydroxy-5-(4-phenyl-1H-1,2,3-triazol-1-yl)pentanamide
Homo sapiens
-
-
0.0000142
N-hydroxy-6-(4-phenyl-1H-1,2,3-triazol-1-yl)hexanamide
Homo sapiens
-
-
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
0.000076
N-hydroxy-6-[4-(2-methoxyphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
Homo sapiens
-
-
0.0000139
N-hydroxy-6-[4-(3-methoxyphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
Homo sapiens
-
-
0.0000174 - 0.0000319
N-hydroxy-6-[4-(3-methylphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
0.0000021
N-hydroxy-6-[4-(4-methoxyphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
Homo sapiens
-
-
0.0000434
N-hydroxy-6-[4-(4-methylphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
Homo sapiens
-
-
0.0000018
N-hydroxy-6-[4-(6-methoxynaphthalen-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
Homo sapiens
-
-
0.0000676
N-hydroxy-6-[4-(pyridin-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
Homo sapiens
-
-
0.0002872
N-hydroxy-6-[4-(pyridin-3-yl)-1H-1,2,3-triazol-1-yl]hexanamide
Homo sapiens
-
-
0.0001125
N-hydroxy-6-[4-(pyridin-4-yl)-1H-1,2,3-triazol-1-yl]hexanamide
Homo sapiens
-
-
0.0000021
N-hydroxy-6-[4-(quinolin-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
Homo sapiens
-
-
0.0001515
N-hydroxy-6-[4-(quinolin-7-yl)-1H-1,2,3-triazol-1-yl]hexanamide
Homo sapiens
-
-
0.0000317
N-hydroxy-6-[4-(thiophen-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
-
-
0.0000096
N-hydroxy-7-(4-phenyl-1H-1,2,3-triazol-1-yl)heptanamide
Homo sapiens
-
-
0.0000153
N-hydroxy-7-[4-(6-methoxynaphthalen-2-yl)-1H-1,2,3-triazol-1-yl]heptanamide
Homo sapiens
-
-
0.0000239
N-hydroxy-7-[4-(pyridin-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
-
-
0.000089 - 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
0.0007 - 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
0.00732 - 0.0208
N-[2-amino-5-(pyridin-3-yl)phenyl]oxane-4-carboxamide
0.00142 - 0.033
N-[2-amino-5-(pyridin-4-yl)phenyl]oxane-4-carboxamide
0.033
N-[4-amino-4'-(trifluoromethyl)[1,1'-biphenyl]-3-yl]oxane-4-carboxamide
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
0.00034
N1-methyl-2-oxo-N9-phenylnonanediamide
Homo sapiens
37°C
0.0026 - 0.098
oxamflatin
0.000185 - 0.01
pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
0.102
S-(2-hydroxyethyl) methanesulfonothioate
Homo sapiens
-
-
0.0175
S-[2-[(2-propylpentanoyl)amino]ethyl]methanesulfonothioate
Homo sapiens
-
-
0.013
sodium butyrate
Homo sapiens
-
recombinant HDAC3 in complex with CoR1, pH and temperature not specified in the publication
0.000013 - 0.113
suberoylanilide hydroxamic acid
0.0000006 - 0.008
trichostatin A
0.0008 - 0.225
tubacin
0.4 - 0.995
Valproic acid
0.00003 - 0.01
vorinostat
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
primary erythroid progenitor cell
Manually annotated by BRENDA team
prominent expression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
prominent expression
Manually annotated by BRENDA team
prominent expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
depending on phosphorylation status
Manually annotated by BRENDA team
depending on phosphorylation status
Manually annotated by BRENDA team
-
mitotic spindle
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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)
evolution
histone deacetylase 8 (HDAC8) is a member of the class I acetyl-lysine deacetylase (HDAC) family
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HDAC1_HUMAN
482
0
55103
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
dimeric recombinant enzyme, gel filtration
105000
x * 105000, calculated, x * 119000, SDS-PAGE of FLAG-tagged protein
114000
-
truncated isoform of the HDAC6p114 protein, SDS-PAGE
119000
x * 105000, calculated, x * 119000, SDS-PAGE of FLAG-tagged protein
131000
-
HDAC6p131, major isoform of histone deacetlyase 6, SDS-PAGE
220000
sucrose gradient
39000
x * 39000, calculated
42000
45240
x * 45240, calculated
600000
gel filtration
65000
determined by SDS-PAGE and Western Blot analysis
70000
x * 70000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 55000, recombinant enzyme, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
-
HDAC, but not HDAC2 is acetylated by p300
phosphoprotein
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D99A
mutated channel residue, 25% deacetylase activity
E98A
mutated channel residue, 120% deacetylase activity
F150A
mutated channel residue, 12% deacetylase activity
F205A
mutated channel residue, 20% deacetylase activity
G149A
mutated channel residue, 10% deacetylase activity
H141A
mutated channel residue, 20% deacetylase activity
H28A
mutated channel residue, 20% deacetylase activity
L271A
mutated channel residue, 12% deacetylase activity
P29A
mutated channel residue, 18% deacetylase activity
Y204A
mutated channel residue, 40% deacetylase activity
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
H135A
loss of catalytic activity
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
H142A/H143A
less than 20% residual activity
H143A
mutant, the substitution abolishes enzyme activity
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
H843A
mutant, constructed to assess the role of the active site His-843
H843F
mutant, constructed to assess the role of the active site His-843
H843Y
mutant, constructed to assess the role of the active site His-843
K432R
-
the HDAC1 mutant only partially loses acetylation modification
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
R433K
-
the HDAC2 mutant is only acetylated at low levels
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
S421D
-
mutation of phosphorylation site, 82.5% of wild-type activity
S421D/S423D
-
mutation of phosphorylation site, 34% of wild-type activity
S421E
-
mutation of phosphorylation site, 81.8% of wild-type activity
S421E/S423E
-
mutation of phosphorylation site, 38.5% of wild-type activity
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
S423D
-
mutation of phosphorylation site, 40% of wild-type activity
S423E
-
mutation of phosphorylation site, 48% of wild-type activity
V171A
-
mutation in fragment 155-220 of isoform HDAC4, little effect on binding to myocyte enhancer factor-2
V171K
-
mutation in fragment 155-220 of isoform HDAC4, binding to myocyte enhancer factor-2 is diminished
V179A
-
mutation in fragment 155-220 of isoform HDAC4, binding to myocyte enhancer factor-2 is diminished
Y146A
Y153A
Y253A
Y298H
-
deacetylase-dead mutant
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Co(2+)-HDAC8 is stable in the presence of oxygen
-
712485
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
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 His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
using a mono Q HR5-5 column
-
via affinity chromatography using irreversible inhibitor trapoxin
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
FLAG-tagged HDAC1 deletion mutants, aa 1-482, 1-140 and 141-482, are constructed in pcDNA3 FLAG expression plasmid
full-length HDAC1 with COOH-terminal His tag is expressed using baculovirus expression system
HDAC1 mutants are cloned into pBJ5HDAC1-F
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
expression in 293 cells
expression in 293T, HeLa and Neuro2A cells
-
expression in baculoviral system, His-tagged protein
expression in Escherichia coli
expression in HEK-293 cells and Escherichia coli
expression in HeLa and Sf9 cells, FLAG-tagged protein
expression in SV40 T-Ag Jurkat cells
-
expression in U2OS and 293T cells
expression of FLAG-tagged enzyme in T-Ag Jurkat cells
-
expression of FLAG-tagged protein in 293 cells
expression with FLAG-tag in HEK-293 cells
FLAG-tagged protein, expression in C2 or 10T1/2 cells
-
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 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
isoform HDAC1
-
isoform HDAC8, expression in Escherichia coli
isoform HDAC8, expression in Escherichia coli. Isoforms HDAC1, HDAC6, expression in HEK-293 cell, HDAC3, expression in insect system, FLAg-tagged proteins
-
Myc-, HA- or, GFP-tagged HDAC6 are constructed in a CMV promoter-derrived mammalian expression vector, pCS4+
-
recombinant expression of His-tagged isozyme HDAC8
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant HDAC1, HDAC8, HDAC6 and HDAC7
-
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
HDAC1 and HDAC2 protein levels are elevated in chondrocytes from osteoarthritic patients
-
hepatocyte growth factor induces HDAC-5 expression in gastric cancer cells. GO6976, a PKC inhibitor, significantly inhibits hepatocyte growth factor-induced HDAC5 expression
-
histone deacetylase 1 mRNA in pancreatic cancer tissues are significantly higher than in paracancerous tissues
-
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
-
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
-
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
-
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zou, H.; Wu, Y.; Navre, M.; Sang, B.C.
Characterization of the two catalytic domains in histone deacetylase 6
Biochem. Biophys. Res. Commun.
341
45-50
2006
Homo sapiens (Q9UBN7)
Manually annotated by BRENDA team
Riester, D.; Hildmann, C.; Gruenewald, S.; Beckers, T.; Schwienhorst, A.
Factors affecting the substrate specificity of histone deacetylases
Biochem. Biophys. Res. Commun.
357
439-445
2007
Homo sapiens
Manually annotated by BRENDA team
Buggy, J.J.; Sideris, M.L.; Mak, P.; Lorimer, D.D.; McIntosh, B.; Clark, J.M.
Cloning and characterization of a novel human histone deacetylase, HDAC8
Biochem. J.
350
199-205
2000
Homo sapiens (Q9BY41), Homo sapiens
Manually annotated by BRENDA team
Gantt, S.L.; Gattis, S.G.; Fierke, C.A.
Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion
Biochemistry
45
6170-6178
2006
Homo sapiens (Q9BY41), Homo sapiens
Manually annotated by BRENDA team
Glenisson, W.; Castronovo, V.; Waltregny, D.
Histone deacetylase 4 is required for TGFbeta 1-induced myofibroblastic differentiation
Biochim. Biophys. Acta
1773
1572-1582
2007
Homo sapiens
Manually annotated by BRENDA team
Brogdon, J.L.; Xu, Y.; Szabo, S.J.; An, S.; Buxton, F.; Cohen, D.; Huang, Q.
Histone deacetylase activities are required for innate immune cell control of Th1 but not Th2 effector cell function
Blood
109
1123-1130
2007
Homo sapiens
Manually annotated by BRENDA team
Myzak, M.C.; Hardin, K.; Wang, R.; Dashwood, R.H.; Ho, E.
Sulforaphane inhibits histone deacetylase activity in BPH-1, LnCaP and PC-3 prostate epithelial cells
Carcinogenesis
27
811-819
2006
Homo sapiens
Manually annotated by BRENDA team
Mal, A.; Sturniolo, M.; Schiltz, R.L.; Ghosh, M.K.; Harter, M.L.
A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program
EMBO J.
20
1739-1753
2001
Homo sapiens
Manually annotated by BRENDA team
Fischle, W.; Emiliani, S.; Hendzel, M.J.; Nagase, T.; Nomura, N.; Voelter, W.; Verdin, E.
A new family of human histone deacetylases related to Saccharomyces cerevisiae HDA1p
J. Biol. Chem.
274
11713-11720
1999
Homo sapiens (P56524), Homo sapiens
Manually annotated by BRENDA team
Hu, E.; Chen, Z.; Fredrickson, T.; Zhu, Y.; Kirkpatrick, R.; Zhang, G.F.; Johanson, K.; Sung, C.M.; Liu, R.; Winkler, J.
Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor
J. Biol. Chem.
275
15254-15264
2000
Homo sapiens (Q9BY41), Homo sapiens
Manually annotated by BRENDA team
Fischle, W.; Dequiedt, F.; Fillion, M.; Hendzel, M.J.; Voelter, W.; Verdin, E.
Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo
J. Biol. Chem.
276
35826-35835
2001
Homo sapiens (Q8WUI4), Homo sapiens
Manually annotated by BRENDA team
Phiel, C.J.; Zhang, F.; Huang, E.Y.; Guenther, M.G.; Lazar, M.A.; Klein, P.S.
Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen
J. Biol. Chem.
276
36734-36741
2001
Homo sapiens
Manually annotated by BRENDA team
Pflum, M.K.H.; Tong, J.K.; Lane, W.S.; Schreiber, S.L.
Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation
J. Biol. Chem.
276
47733-47741
2001
Homo sapiens
Manually annotated by BRENDA team
Kao, H.Y.; Lee, C.H.; Komarov, A.; Han, C.C.; Evans, R.M.
Isolation and characterization of mammalian HDAC10, a novel histone deacetylase
J. Biol. Chem.
277
187-193
2002
Homo sapiens (Q969S8)
Manually annotated by BRENDA team
Gao, L.; Cueto, M.A.; Asselbergs, F.; Atadja, P.
Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family
J. Biol. Chem.
277
25748-25755
2002
Homo sapiens (Q96DB2), Homo sapiens
Manually annotated by BRENDA team
Guardiola, A.R.; Yao, T.P.
Molecular cloning and characterization of a novel histone deacetylase HDAC10
J. Biol. Chem.
277
3350-3356
2002
Homo sapiens (Q969S8)
Manually annotated by BRENDA team
Johnson, C.A.; White, D.A.; Lavender, J.S.; O'Neill, L.P.; Turner, B.M.
Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70
J. Biol. Chem.
277
9590-9597
2002
Homo sapiens
Manually annotated by BRENDA team
Klampfer, L.; Huang, J.; Swaby, L.A.; Augenlicht, L.
Requirement of histone deacetylase activity for signaling by STAT1
J. Biol. Chem.
279
30358-30368
2004
Homo sapiens
Manually annotated by BRENDA team
Suzuki, T.; Nagano, Y.; Kouketsu, A.; Matsuura, A.; Maruyama, S.; Kurotaki, M.; Nakagawa, H.; Miyata, N.
Novel Inhibitors of human histone deacetylases: design, synthesis, enzyme inhibition, and cancer cell growth inhibition of SAHA-based non-hydroxamates
J. Med. Chem.
48
1019-1032
2005
Homo sapiens (Q9BY41), Homo sapiens
Manually annotated by BRENDA team
Liu, T.; Kapustin, G.; Etzkorn, F.A.
Design and synthesis of a potent histone deacetylase inhibitor
J. Med. Chem.
50
2003-2006
2007
Homo sapiens
Manually annotated by BRENDA team
Han, A.; He, J.; Wu, Y.; Liu, J.O.; Chen, L.
Mechanism of recruitment of class II histone deacetylases by myocyte enhancer factor-2
J. Mol. Biol.
345
91-102
2004
Homo sapiens
Manually annotated by BRENDA team
Tong, J.J.; Liu, J.; Bertos, N.R.; Yang, X.J.
Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain
Nucleic Acids Res.
30
1114-1123
2002
Homo sapiens (Q969S8), Homo sapiens
Manually annotated by BRENDA team
Vannini, A.; Volpari, C.; Filocamo, G.; Casavola, E.C.; Brunetti, M.; Renzoni, D.; Chakravarty, P.; Paolini, C.; De Francesco, R.; Gallinari, P.; Steinkuhler, C.; Di Marco, S.
Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor
Proc. Natl. Acad. Sci. USA
101
15064-15069
2004
Homo sapiens (Q9BY41), Homo sapiens
Manually annotated by BRENDA team
Guo, L.; Han, A.; Bates, D.L.; Cao, J.; Chen, L.
Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains
Proc. Natl. Acad. Sci. USA
104
4297-4302
2007
Homo sapiens (P56524), Homo sapiens
Manually annotated by BRENDA team
Hassig, C.A.; Tong, J.K.; Fleischer, T.C.; Owa, T.; Grable, P.G.; Ayer, D.E.; Schreiber, S.L.
A role for histone deacetylase activity in HDAC1-mediated transcriptional repression
Proc. Natl. Acad. Sci. USA
95
3519-3524
1998
Homo sapiens
Manually annotated by BRENDA team
Zhou, X.; Marks, P.A.; Rifkind, R.A.; Richon, V.M.
Cloning and characterization of a histone deacetylase, HDAC9
Proc. Natl. Acad. Sci. USA
98
10572-10577
2001
Homo sapiens (Q9UKV0), Homo sapiens
Manually annotated by BRENDA team
Geiger, R.C.; Kaufman, C.D.; Lam, A.P.; Budinger, G.R.; Dean, D.A.
Tubulin acetylation and histone deacetylase 6 activity in the lung under cyclic load
Am. J. Respir. Cell Mol. Biol.
40
76-82
2009
Homo sapiens, Mus musculus (Q9Z2V5), Mus musculus
Manually annotated by BRENDA team
Han, Y.; Jeong, H.M.; Jin, Y.H.; Kim, Y.J.; Jeong, H.G.; Yeo, C.Y.; Lee, K.Y.
Acetylation of histone deacetylase 6 by p300 attenuates its deacetylase activity
Biochem. Biophys. Res. Commun.
383
88-92
2009
Homo sapiens
Manually annotated by BRENDA team
Osoata, G.O.; Yamamura, S.; Ito, M.; Vuppusetty, C.; Adcock, I.M.; Barnes, P.J.; Ito, K.
Nitration of distinct tyrosine residues causes inactivation of histone deacetylase 2
Biochem. Biophys. Res. Commun.
384
366-371
2009
Homo sapiens, Homo sapiens (Q92769)
Manually annotated by BRENDA team
Dowling, D.P.; Gantt, S.L.; Gattis, S.G.; Fierke, C.A.; Christianson, D.W.
Structural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors
Biochemistry
47
13554-13563
2008
Homo sapiens (Q9BY41), Homo sapiens
Manually annotated by BRENDA team
Perrino, E.; Cappelletti, G.; Tazzari, V.; Giavini, E.; Del Soldato, P.; Sparatore, A.
New sulfurated derivatives of valproic acid with enhanced histone deacetylase inhibitory activity
Bioorg. Med. Chem. Lett.
18
1893-1897
2008
Homo sapiens
Manually annotated by BRENDA team
Mai, A.; Perrone, A.; Nebbioso, A.; Rotili, D.; Valente, S.; Tardugno, M.; Massa, S.; De Bellis, F.; Altucci, L.
Novel uracil-based 2-aminoanilide and 2-aminoanilide-like derivatives: histone deacetylase inhibition and in-cell activities
Bioorg. Med. Chem. Lett.
18
2530-2535
2008
Homo sapiens
Manually annotated by BRENDA team
Wang, H.; Yu, N.; Song, H.; Chen, D.; Zou, Y.; Deng, W.; Lye, P.L.; Chang, J.; Ng, M.; Sun, E.T.; Sangthongpitag, K.; Wang, X.; Wu, X.; Khng, H.H.; Fang, L.; Goh, S.K.; Ong, W.C.; Bonday, Z.; Stuenkel, W.; Poulsen, A.; Entzeroth, M.
N-Hydroxy-1,2-disubstituted-1H-benzimidazol-5-yl acrylamides as novel histone deacetylase inhibitors: Design, synthesis, SAR studies, and in vivo antitumor activity
Bioorg. Med. Chem. Lett.
19
1403-1408
2009
Homo sapiens
Manually annotated by BRENDA team
Chen, P.C.; Patil, V.; Guerrant, W.; Green, P.; Oyelere, A.K.
Synthesis and structure-activity relationship of histone deacetylase (HDAC) inhibitors with triazole-linked cap group
Bioorg. Med. Chem.
16
4839-4853
2008
Homo sapiens
Manually annotated by BRENDA team
Balasubramanian, S.; Verner, E.; Buggy, J.J.
Isoform-specific histone deacetylase inhibitors: The next step?
Cancer Lett.
280
211-221
2009
Homo sapiens
Manually annotated by BRENDA team
Jung, J.C.; Moon, H.I.; Oh, S.
Synthesis, structural characterization and biological evaluation of N-protected cyclopropylethylcarbamates as potential histone deacetylase inhibitor
Chem. Biol. Drug Des.
72
592-595
2008
Homo sapiens
Manually annotated by BRENDA team
Nian, H.; Delage, B.; Ho, E.; Dashwood, R.H.
Modulation of histone deacetylase activity by dietary isothiocyanates and allyl sulfides: studies with sulforaphane and garlic organosulfur compounds
Environ. Mol. Mutagen.
50
213-221
2009
Homo sapiens (Q9BY41), Homo sapiens
Manually annotated by BRENDA team
Xiong, S.D.; Yu, K.; Liu, X.H.; Yin, L.H.; Kirschenbaum, A.; Yao, S.; Narla, G.; Difeo, A.; Wu, J.B.; Yuan, Y.; Ho, S.M.; Lam, Y.W.; Levine, A.C.
Ribosome-inactivating proteins isolated from dietary bitter melon induce apoptosis and inhibit histone deacetylase-1 selectively in premalignant and malignant prostate cancer cells
Int. J. Cancer
125
774-782
2009
Homo sapiens (Q13547)
Manually annotated by BRENDA team
Montero, A.; Beierle, J.M.; Olsen, C.A.; Ghadiri, M.R.
Design, synthesis, biological evaluation, and structural characterization of potent histone deacetylase inhibitors based on cyclic alpha/beta-tetrapeptide architectures
J. Am. Chem. Soc.
131
3033-3041
2009
Homo sapiens
Manually annotated by BRENDA team
Schuetz, A.; Min, J.; Allali-Hassani, A.; Schapira, M.; Shuen, M.; Loppnau, P.; Mazitschek, R.; Kwiatkowski, N.P.; Lewis, T.A.; Maglathin, R.L.; McLean, T.H.; Bochkarev, A.; Plotnikov, A.N.; Vedadi, M.; Arrowsmith, C.H.
Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity
J. Biol. Chem.
283
11355-11363
2008
Homo sapiens (Q8WUI4), Homo sapiens
Manually annotated by BRENDA team
Jones, P.; Altamura, S.; De Francesco, R.; Paz, O.G.; Kinzel, O.; Mesiti, G.; Monteagudo, E.; Pescatore, G.; Rowley, M.; Verdirame, M.; Steinkuehler, C.
A novel series of potent and selective ketone histone deacetylase inhibitors with antitumor activity in vivo
J. Med. Chem.
51
2350-2353
2008
Homo sapiens
Manually annotated by BRENDA team
Weerasinghe, S.V.; Estiu, G.; Wiest, O.; Pflum, M.K.
Residues in the 11 A channel of histone deacetylase 1 promote catalytic activity: implications for designing isoform-selective histone deacetylase inhibitors
J. Med. Chem.
51
5542-5551
2008
Homo sapiens (Q13547)
Manually annotated by BRENDA team
Wang, J.C.; Chen, C.; Dumlao, T.; Naik, S.; Chang, T.; Xiao, Y.Y.; Sominsky, I.; Burton, J.
Enhanced histone deacetylase enzyme activity in primary myelofibrosis
Leuk. Lymphoma
49
2321-2327
2008
Homo sapiens
Manually annotated by BRENDA team
Duong, V.; Bret, C.; Altucci, L.; Mai, A.; Duraffourd, C.; Loubersac, J.; Harmand, P.O.; Bonnet, S.; Valente, S.; Maudelonde, T.; Cavailles, V.; Boulle, N.
Specific activity of class II histone deacetylases in human breast cancer cells
Mol. Cancer Res.
6
1908-1919
2008
Homo sapiens, Homo sapiens (P56524), Homo sapiens (Q13547), Homo sapiens (Q92769), Homo sapiens (Q9BY41)
Manually annotated by BRENDA team
Ray, S.; Lee, C.; Hou, T.; Boldogh, I.; Brasier, A.R.
Requirement of histone deacetylase1 (HDAC1) in signal transducer and activator of transcription 3 (STAT3) nucleocytoplasmic distribution
Nucleic Acids Res.
36
4510-4520
2008
Homo sapiens (Q13547), Homo sapiens
Manually annotated by BRENDA team
Bowers, A.A.; West, N.; Newkirk, T.L.; Troutman-Youngman, A.E.; Schreiber, S.L.; Wiest, O.; Bradner, J.E.; Williams, R.M.
Synthesis and histone deacetylase inhibitory activity of largazole analogs: alteration of the zinc-binding domain and macrocyclic scaffold
Org. Lett.
11
1301-1304
2009
Homo sapiens, Homo sapiens (Q13547), Homo sapiens (Q92769), Homo sapiens (Q9UBN7)
Manually annotated by BRENDA team
Ishii, S.; Kurasawa, Y.; Wong, J.; Yu-Lee, L.Y.
Histone deacetylase 3 localizes to the mitotic spindle and is required for kinetochore-microtubule attachment
Proc. Natl. Acad. Sci. USA
105
4179-4184
2008
Homo sapiens
Manually annotated by BRENDA team
Zhou, J.; Vos, C.C.; Gjyrezi, A.; Yoshida, M.; Khuri, F.R.; Tamanoi, F.; Giannakakou, P.
The protein farnesyltransferase regulates HDAC6 activity in a microtubule-dependent manner
J. Biol. Chem.
284
9648-9655
2009
Homo sapiens
Manually annotated by BRENDA team
Kawabata, T.; Nishida, K.; Takasugi, K.; Ogawa, H.; Sada, K.; Kadota, Y.; Inagaki, J.; Hirohata, S.; Ninomiya, Y.; Makino, H.
Increased activity and expression of histone deacetylase 1 in relation to tumor necrosis factor-alpha in synovial tissue of rheumatoid arthritis
Arthritis Res. Ther.
12
R133
2010
Homo sapiens
Manually annotated by BRENDA team
Zhuang, Y.; Nguyen, H.T.; Lasky, J.A.; Cao, S.; Li, C.; Hu, J.; Guo, X.; Burow, M.E.; Shan, B.
Requirement of a novel splicing variant of human histone deacetylase 6 for TGF-beta1-mediated gene activation
Biochem. Biophys. Res. Commun.
392
608-613
2010
Homo sapiens
Manually annotated by BRENDA team
Chetan, B.; Bunha, M.; Jagrat, M.; Sinha, B.N.; Saiko, P.; Graser, G.; Szekeres, T.; Raman, G.; Rajendran, P.; Moorthy, D.; Basu, A.; Jayaprakash, V.
Design, synthesis and anticancer activity of piperazine hydroxamates and their histone deacetylase (HDAC) inhibitory activity
Bioorg. Med. Chem. Lett.
20
3906-3910
2010
Homo sapiens (Q9BY41), Homo sapiens
Manually annotated by BRENDA team
Bora-Tatar, G.; Dayangac-Erden, D.; Demir, A.S.; Dalkara, S.; Yelekci, K.; Erdem-Yurter, H.
Molecular modifications on carboxylic acid derivatives as potent histone deacetylase inhibitors: Activity and docking studies
Bioorg. Med. Chem.
17
5219-5228
2009
Homo sapiens (Q9BY41), Homo sapiens
Manually annotated by BRENDA team
Zhang, Y.; Feng, J.; Liu, C.; Zhang, L.; Jiao, J.; Fang, H.; Su, L.; Zhang, X.; Zhang, J.; Li, M.; Wang, B.; Xu, W.
Design, synthesis and preliminary activity assay of 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid derivatives as novel histone deacetylases (HDACs) inhibitors
Bioorg. Med. Chem.
18
1761-1772
2010
Homo sapiens (Q9BY41)
Manually annotated by BRENDA team
Davies, G.F.; Ross, A.R.; Arnason, T.G.; Juurlink, B.H.; Harkness, T.A.
Troglitazone inhibits histone deacetylase activity in breast cancer cells
Cancer Lett.
288
236-250
2010
Homo sapiens
Manually annotated by BRENDA team
Liu, R.; Wang, L.; Chen, G.; Katoh, H.; Chen, C.; Liu, Y.; Zheng, P.
FOXP3 up-regulates p21 expression by site-specific inhibition of histone deacetylase 2/histone deacetylase 4 association to the locus
Cancer Res.
69
2252-2259
2009
Homo sapiens
Manually annotated by BRENDA team
Nian, H.; Bisson, W.H.; Dashwood, W.M.; Pinto, J.T.; Dashwood, R.H.
Alpha-keto acid metabolites of organoselenium compounds inhibit histone deacetylase activity in human colon cancer cells
Carcinogenesis
30
1416-1423
2009
Homo sapiens (Q9BY41), Homo sapiens
Manually annotated by BRENDA team
Hui, S.; Brunt, K.; Husain, M.
Temporal and spatial regulation of histone deacetylase-7 and beta-catenin in endothelial cells
Circ. Res.
106
1180-1183
2010
Homo sapiens
Manually annotated by BRENDA team
Fiesel, F.C.; Voigt, A.; Weber, S.S.; Van den Haute, C.; Waldenmaier, A.; Goerner, K.; Walter, M.; Anderson, M.L.; Kern, J.V.; Rasse, T.M.; Schmidt, T.; Springer, W.; Kirchner, R.; Bonin, M.; Neumann, M.; Baekelandt, V.; Alunni-Fabbroni, M.; Schulz, J.B.; Kahle, P.J.
Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6
EMBO J.
29
209-221
2010
Homo sapiens
Manually annotated by BRENDA team
Hong, S.; Derfoul, A.; Pereira-Mouries, L.; Hall, D.J.
A novel domain in histone deacetylase 1 and 2 mediates repression of cartilage-specific genes in human chondrocytes
FASEB J.
23
3539-3552
2009
Homo sapiens
Manually annotated by BRENDA team
Hayashi, A.; Horiuchi, A.; Kikuchi, N.; Hayashi, T.; Fuseya, C.; Suzuki, A.; Konishi, I.; Shiozawa, T.
Type-specific roles of histone deacetylase (HDAC) overexpression in ovarian carcinoma: HDAC1 enhances cell proliferation and HDAC3 stimulates cell migration with downregulation of E-cadherin
Int. J. Cancer
127
1332-1346
2010
Homo sapiens
Manually annotated by BRENDA team
Luo, Y.; Jian, W.; Stavreva, D.; Fu, X.; Hager, G.; Bungert, J.; Huang, S.; Qiu, Y.
Trans-regulation of histone deacetylase activities through acetylation
J. Biol. Chem.
284
34901-34910
2009
Homo sapiens
Manually annotated by BRENDA team
Doyle, K.; Fitzpatrick, F.A.
Redox signaling, alkylation (carbonylation) of conserved cysteines inactivates class I histone deacetylases 1, 2, and 3 and antagonizes their transcriptional repressor function
J. Biol. Chem.
285
17417-17424
2010
Homo sapiens
Manually annotated by BRENDA team
Gantt, S.L.; Joseph, C.G.; Fierke, C.A.
Activation and inhibition of histone deacetylase 8 by monovalent cations
J. Biol. Chem.
285
6036-6043
2010
Homo sapiens
Manually annotated by BRENDA team
Ontoria, J.M.; Altamura, S.; Di Marco, A.; Ferrigno, F.; Laufer, R.; Muraglia, E.; Palumbi, M.C.; Rowley, M.; Scarpelli, R.; Schultz-Fademrecht, C.; Serafini, S.; Steinkuehler, C.; Jones, P.
Identification of novel, selective, and stable inhibitors of class II histone deacetylases. Validation studies of the inhibition of the enzymatic activity of HDAC4 by small molecules as a novel approach for cancer therapy
J. Med. Chem.
52
6782-6789
2009
Homo sapiens
Manually annotated by BRENDA team
Lee, K.H.; Choi, E.Y.; Kim, M.K.; Kim, K.O.; Jang, B.I.; Kim, S.W.; Kim, S.W.; Song, S.K.; Kim, J.R.
Inhibition of histone deacetylase activity down-regulates urokinase plasminogen activator and matrix metalloproteinase-9 expression in gastric cancer
Mol. Cell. Biochem.
343
163-171
2010
Homo sapiens
Manually annotated by BRENDA team
Lee, J.; Jeong, E.; Choi, M.; Kim, S.; Park, J.; Song, S.; Park, J.; Bang, Y.; Kim, T.
Inhibition of histone deacetylase 10 induces thioredoxin-interacting protein and causes accumulation of reactive oxygen species in SNU-620 human gastric cancer cells
Mol. Cells
30
107-112
2010
Homo sapiens
Manually annotated by BRENDA team
Hutt, D.M.; Herman, D.; Rodrigues, A.P.; Noel, S.; Pilewski, J.M.; Matteson, J.; Hoch, B.; Kellner, W.; Kelly, J.W.; Schmidt, A.; Thomas, P.J.; Matsumura, Y.; Skach, W.R.; Gentzsch, M.; Riordan, J.R.; Sorscher, E.J.; Okiyoneda, T.; Yates, J.R.; Lukacs, G.L.; Frizzell, R.A.; Manning, G.; Gottesfeld, J.M.; Balc, B.a.l.c.h.
Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis
Nat. Chem. Biol.
6
25-33
2010
Homo sapiens
Manually annotated by BRENDA team
Leone, V.; Mansueto, G.; Pierantoni, G.M.; Tornincasa, M.; Merolla, F.; Cerrato, A.; Santoro, M.; Grieco, M.; Scaloni, A.; Celetti, A.; Fusco, A.
CCDC6 represses CREB1 activity by recruiting histone deacetylase 1 and protein phosphatase 1
Oncogene
29
4341-4351
2010
Homo sapiens
Manually annotated by BRENDA team
Gao, D.J.; Xu, M.; Zhang, Y.Q.; Du, Y.Q.; Gao, J.; Gong, Y.F.; Man, X.H.; Wu, H.Y.; Jin, J.; Xu, G.M.; Li, Z.S.
Upregulated histone deacetylase 1 expression in pancreatic ductal adenocarcinoma and specific siRNA inhibits the growth of cancer cells
Pancreas
39
994-1001
2010
Homo sapiens
Manually annotated by BRENDA team
Kim, I.A.; No, M.; Lee, J.M.; Shin, J.H.; Oh, J.S.; Choi, E.J.; Kim, I.H.; Atadja, P.; Bernhard, E.J.
Epigenetic modulation of radiation response in human cancer cells with activated EGFR or HER-2 signaling: potential role of histone deacetylase 6
Radiother. Oncol.
92
125-132
2009
Homo sapiens
Manually annotated by BRENDA team
Janzer, A.; Lim, S.; Fronhoffs, F.; Niazy, N.; Buettner, R.; Kirfel, J.
Lysine-specific demethylase 1 (LSD1) and histone deacetylase 1 (HDAC1) synergistically repress proinflammatory cytokines and classical complement pathway components
Biochem. Biophys. Res. Commun.
421
665-670
2012
Homo sapiens
Manually annotated by BRENDA team
Shultz, M.; Fan, J.; Chen, C.; Cho, Y.S.; Davis, N.; Bickford, S.; Buteau, K.; Cao, X.; Holmqvist, M.; Hsu, M.; Jiang, L.; Liu, G.; Lu, Q.; Patel, C.; Suresh, J.R.; Selvaraj, M.; Urban, L.; Wang, P.; Yan-Neale, Y.; Whitehead, L.; Zhang, H.; Zhou, L.; Atadja, P.
The design, synthesis and structure-activity relationships of novel isoindoline-based histone deacetylase inhibitors
Bioorg. Med. Chem. Lett.
21
4909-4912
2011
Homo sapiens
Manually annotated by BRENDA team
Singh, R.K.; Mandal, T.; Balsubramanian, N.; Viaene, T.; Leedahl, T.; Sule, N.; Cook, G.; Srivastava, D.K.
Histone deacetylase activators: N-acetylthioureas serve as highly potent and isozyme selective activators for human histone deacetylase-8 on a fluorescent substrate
Bioorg. Med. Chem. Lett.
21
5920-5923
2011
Homo sapiens
Manually annotated by BRENDA team
Guan, P.; Sun, F.; Hou, X.; Wang, F.; Yi, F.; Xu, W.; Fang, H.
Design, synthesis and preliminary bioactivity studies of 1,3,4-thiadiazole hydroxamic acid derivatives as novel histone deacetylase inhibitors
Bioorg. Med. Chem.
20
3865-3872
2012
Homo sapiens
Manually annotated by BRENDA team
Henkes, L.M.; Haus, P.; Jaeger, F.; Ludwig, J.; Meyer-Almes, F.J.
Synthesis and biochemical analysis of 2,2,3,3,4,4,5,5,6,6,7,7-dodecafluoro-N-hydroxy-octanediamides as inhibitors of human histone deacetylases
Bioorg. Med. Chem.
20
985-995
2012
Homo sapiens
Manually annotated by BRENDA team
Feng, J.H.; Jing, F.B.; Fang, H.; Gu, L.C.; Xu, W.F.
Expression, purification, and S-nitrosylation of recombinant histone deacetylase 8 in Escherichia coli
Biosci. Trends
5
17-22
2011
Homo sapiens (Q9BY41), Homo sapiens
Manually annotated by BRENDA team
Terracciano, S.; Chini, M.G.; Riccio, R.; Bruno, I.; Bifulco, G.
Design, synthesis, and biological activity of hydroxamic tertiary amines as histone deacetylase inhibitors
ChemMedChem
7
694-702
2012
Homo sapiens, Aquifex aeolicus (O67135)
Manually annotated by BRENDA team
Icardi, L.; Lievens, S.; Mori, R.; Piessevaux, J.; De Cauwer, L.; De Bosscher, K.; Tavernier, J.
Opposed regulation of type I IFN-induced STAT3 and ISGF3 transcriptional activities by histone deacetylases (HDACS) 1 and 2
FASEB J.
26
240-249
2012
Homo sapiens
Manually annotated by BRENDA team
Muralidhar, S.A.; Ramakrishnan, V.; Kalra, I.S.; Li, W.; Pace, B.S.
Histone deacetylase 9 activates gamma-globin gene expression in primary erythroid cells
J. Biol. Chem.
286
2343-2353
2011
Homo sapiens
Manually annotated by BRENDA team
Chen, Y.; Huang, P.; Ai, W.; Li, X.; Guo, W.; Zhang, J.; Yang, J.
Histone deacetylase activity is decreased in peripheral blood monocytes in patients with COPD
J. Inflamm.
9
10
2012
Homo sapiens
Manually annotated by BRENDA team
Mahboobi, S.; Sellmer, A.; Winkler, M.; Eichhorn, E.; Pongratz, H.; Ciossek, T.; Baer, T.; Maier, T.; Beckers, T.
Novel chimeric histone deacetylase inhibitors: a series of lapatinib hybrides as potent inhibitors of epidermal growth factor receptor (EGFR), human epidermal growth factor receptor 2 (HER2), and histone deacetylase activity
J. Med. Chem.
53
8546-8555
2010
Homo sapiens
Manually annotated by BRENDA team
Hnilicova, J.; Hozeifi, S.; Duskova, E.; Icha, J.; Tomankova, T.; Stanek, D.
Histone deacetylase activity modulates alternative splicing
PLoS ONE
6
e16727
2011
Homo sapiens
Manually annotated by BRENDA team
Meyners, C.; Baud, M.G.; Fuchter, M.J.; Meyer-Almes, F.J.
Kinetic method for the large-scale analysis of the binding mechanism of histone deacetylase inhibitors
Anal. Biochem.
460
39-46
2014
Homo sapiens (Q13547), Homo sapiens (Q9BY41), Homo sapiens (Q9UBN7), Homo sapiens, Alcaligenes sp. (Q70I53), Alcaligenes sp. DSM 11172 (Q70I53)
Manually annotated by BRENDA team
Wong, J.C.; Tang, G.; Wu, X.; Liang, C.; Zhang, Z.; Guo, L.; Peng, Z.; Zhang, W.; Lin, X.; Wang, Z.; Mei, J.; Chen, J.; Pan, S.; Zhang, N.; Liu, Y.; Zhou, M.; Feng, L.; Zhao, W.; Li, S.; Zhang, C.; Zhang, M.; Rong, Y.; Jin, T.G.; Zhang, X.; Ren, S.; Ji, Y.; Zhao, R.; She, J.; Ren, Y.; Xu, C.; Chen, D.; Cai, J.; Shan, S.
Pharmacokinetic optimization of class-selective histone deacetylase inhibitors and identification of associated candidate predictive biomarkers of hepatocellular carcinoma tumor response
J. Med. Chem.
55
8903-8925
2012
Mus musculus (O09106), Mus musculus, Homo sapiens (Q13547)
Manually annotated by BRENDA team
Kim, B.; Pithadia, A.S.; Fierke, C.A.
Kinetics and thermodynamics of metal-binding to histone deacetylase 8
Protein Sci.
24
354-365
2015
Homo sapiens (Q9BY41)
Manually annotated by BRENDA team
Castaneda, C.A.; Lopez, J.E.; Joseph, C.G.; Scholle, M.D.; Mrksich, M.; Fierke, C.A.
Active site metal identity alters histone deacetylase 8 substrate selectivity a potential novel regulatory mechanism
Biochemistry
56
5663-5670
2017
Homo sapiens (Q9BY41)
Manually annotated by BRENDA team
Wagner, F.F.; Weiwer, M.; Steinbacher, S.; Schomburg, A.; Reinemer, P.; Gale, J.P.; Campbell, A.J.; Fisher, S.L.; Zhao, W.N.; Reis, S.A.; Hennig, K.M.; Thomas, M.; Mueller, P.; Jefson, M.R.; Fass, D.M.; Haggarty, S.J.; Zhang, Y.L.; Holson, E.B.
Kinetic and structural insights into the binding of histone deacetylase 1 and 2 (HDAC1, 2) inhibitors
Bioorg. Med. Chem.
24
4008-4015
2016
Homo sapiens (O15379), Homo sapiens (Q13547), Homo sapiens (Q92769)
Manually annotated by BRENDA team
Stefan, A.; Calonghi, N.; Schipani, F.; Dal Piaz, F.; Sartor, G.; Hochkoeppler, A.
Purification of active recombinant human histone deacetylase 1 (HDAC1) overexpressed in Escherichia coli
Biotechnol. Lett.
40
1355-1363
2018
Homo sapiens (Q13547), Homo sapiens
Manually annotated by BRENDA team
Kasler, H.G.; Lee, I.S.; Lim, H.W.; Verdin, E.
Histone deacetylase 7 mediates tissue-specific autoimmunity via control of innate effector function in invariant natural killer T cells
eLife
7
e32109
2018
Mus musculus (Q8C2B3), Homo sapiens (Q8WUI4), Homo sapiens, Mus musculus C57BL/6 (Q8C2B3)
Manually annotated by BRENDA team
Yang, Z.; Shen, M.; Tang, M.; Zhang, W.; Cui, X.; Zhang, Z.; Pei, H.; Li, Y.; Hu, M.; Bai, P.; Chen, L.
Discovery of 1,2,4-oxadiazole-containing hydroxamic acid derivatives as histone deacetylase inhibitors potential application in cancer therapy
Eur. J. Med. Chem.
178
116-130
2019
Homo sapiens (Q13547), Homo sapiens (Q9UBN7), Homo sapiens
Manually annotated by BRENDA team
Kutil, Z.; Skultetyova, L.; Rauh, D.; Meleshin, M.; Snajdr, I.; Novakova, Z.; Mikesova, J.; Pavlicek, J.; Hadzima, M.; Baranova, P.; Havlinova, B.; Majer, P.; Schutkowski, M.; Barinka, C.
The unraveling of substrate specificity of histone deacetylase 6 domains using acetylome peptide microarrays and peptide libraries
FASEB J.
33
4035-4045
2019
Homo sapiens (Q9UBN7), Homo sapiens
Manually annotated by BRENDA team
Buckwalter, J.M.; Chan, W.; Shuman, L.; Wildermuth, T.; Ellis-Mohl, J.; Walter, V.; Warrick, J.I.; Wu, X.R.; Kaag, M.; Raman, J.D.; DeGraff, D.J.
Characterization of histone deacetylase expression within in vitro and in vivo bladder cancer model systems
Int. J. Mol. Sci.
20
E2599
2019
Homo sapiens (P56524), Homo sapiens (Q8WUI4), Homo sapiens (Q9UKV0), Homo sapiens
Manually annotated by BRENDA team