Information on EC 3.5.1.98 - histone deacetylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.5.1.98
-
RECOMMENDED NAME
GeneOntology No.
histone deacetylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
deacetylation
Q803C3
-
deacetylation
-
-
deacetylation
Q7K6A1
-
deacetylation
-
-
hydrolysis
-
-
hydrolysis
Q9Z2V5
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
class I histone deacetylase
-
-
class I histone deacetylase
Q7K6A1
-
class II histone deacetylase
-, P56524, Q13547, Q92769, Q9BY41
-
class IIa histone deacetylase
Q8WUI4
-
cytoplasmic deacetylase
-
-
HD1B
-
-
HD2
C1IC97, C1IC98
-
HD8
Q9BY41
-
HDA-1
Q7RY64
-
HDA-2
Q7SEL7
-
HDA-3
Q7SEB0
-
HDA-4
Q7S8C9
-
HDAC
P56524
-
HDAC
Q9BY41
-
HDAC
-
-
HDAC
Q2QWU2, Q5VP94, Q6YV04
-
HDAC 11
B2GUW3
-
HDAC1
-
class I histone deacetylase
HDAC1
Q2QWU2, Q5VP94, Q6YV04
-
HDAC10
-
-
HDAC10
Q2QWU2, Q5VP94, Q6YV04
-
HDAC2
Q92769
-
HDAC2
C1IC97, C1IC98
-
HDAC2
-
-
HDAC2
P70288
-
HDAC2
Q2QWU2, Q5VP94, Q6YV04
-
HDAC2-1
C1IC97
isoform
HDAC2-2
C1IC98
isoform
HDAC3
Q803C3
-
HDAC3
Q88895
-
HDAC3
Q2QWU2, Q5VP94, Q6YV04
-
HDAC4
-
-
HDAC4
-
class II histone deacetylase
HDAC4
P56524
-
HDAC5
-
-
HDAC6
-
class II histone deacetylase
HDAC6
Q94BN7
-
HDAC6
Q9UBN7
-
HDAC6
Q9Z2V5
-
HDAC6
Q2QWU2, Q5VP94, Q6YV04
-
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
Q8WUI4
-
HDAC8
Q9BY41
-
HDLP
O67135
-
histone deacetylase
P56524, Q13547, Q92769
-
histone deacetylase
Q9BY41
-
histone deacetylase
-
-
histone deacetylase
-
-
histone deacetylase 1
-
-
histone deacetylase 1
Q13547
-
histone deacetylase 10
-
a class IIb histone deacetylase
histone deacetylase 11
B2GUW3
-
histone deacetylase 2
-
-
histone deacetylase 2
Q92769
-
histone deacetylase 2
-
-
histone deacetylase 2
P70288
-
histone deacetylase 3
Q803C3
-
histone deacetylase 3
-
-
histone deacetylase 3
Q88895
-
histone deacetylase 4
-
-
histone deacetylase 6
-
-
histone deacetylase 6
Q94BN7
-
histone deacetylase 6
Q9Z2V5
-
histone deacetylase 7
-
-
histone deacetylase 7
Q8WUI4
-
histone deacetylase 8
-
-
histone deacetylase-1
Q13547
-
histone deacetylase-7
-
-
histone deacetylase-like protein
O67135
-
histone deacetylase1
Q13547
-
pfHDAC-1
Q7K6A1
-
RPD3
Q7SEB0
-
tubulin deacetylase
-
-
tubulin deacetylase
Q9Z2V5
-
CAS REGISTRY NUMBER
COMMENTARY
9076-57-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isoform AtHD1
Uniprot
Manually annotated by BRENDA team
isoform HdaA
-
-
Manually annotated by BRENDA team
isoform HdaA, major part of total histone deacetylase activity is due to HdaA
SwissProt
Manually annotated by BRENDA team
isoform HosB
SwissProt
Manually annotated by BRENDA team
isoform Hda-7, class II enzyme
-
-
Manually annotated by BRENDA team
isoform dHDAC1, i.e. dRPD3
-
-
Manually annotated by BRENDA team
isoform HDAC1
Swissprot
Manually annotated by BRENDA team
isoforms HD1 and HD2
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
histone deacetylase 8
SwissProt
Manually annotated by BRENDA team
isoform HDAC-A
SwissProt
Manually annotated by BRENDA team
isoform HDAC1
-
-
Manually annotated by BRENDA team
isoform HDAC10, class II enzyme
SwissProt
Manually annotated by BRENDA team
isoform HDAC10, enzyme is most similar to isoform HDAC6
SwissProt
Manually annotated by BRENDA team
isoform HDAC11
SwissProt
Manually annotated by BRENDA team
isoform HDAC4
SwissProt
Manually annotated by BRENDA team
isoform HDAC6, contains two potentially functional catalytic domains
SwissProt
Manually annotated by BRENDA team
isoform HDAC7, class II enzyme, and isoform HDAC3, class I enzyme
SwissProt
Manually annotated by BRENDA team
isoform HDAC8
SwissProt
Manually annotated by BRENDA team
isoform HDAC8, class I enzyme
SwissProt
Manually annotated by BRENDA team
isoform HDAC9, class II enzyme with several alternatively spliced isoforms
SwissProt
Manually annotated by BRENDA team
isoforms HDAC1 and HDAC2
-
-
Manually annotated by BRENDA team
isoforms HDAC1, HDAC3, HDAC8
SwissProt
Manually annotated by BRENDA team
patients with chronic obstructive pulmonary disease
-
-
Manually annotated by BRENDA team
histone deacetylase HD2 isoform 1; cultivars Caresse and Ippolytos
UniProt
Manually annotated by BRENDA team
histone deacetylase HD2 isoform 2; cultivars Caresse and Ippolytos
UniProt
Manually annotated by BRENDA team
isoform HDAC2
-
-
Manually annotated by BRENDA team
isoform HDAC3
-
-
Manually annotated by BRENDA team
isoform HDA-1
UniProt
Manually annotated by BRENDA team
isoform HDA-2
UniProt
Manually annotated by BRENDA team
isoform HDA-3
UniProt
Manually annotated by BRENDA team
isoform HDA-4
UniProt
Manually annotated by BRENDA team
variety Minghui63
-
-
Manually annotated by BRENDA team
variety Zhonghua11
UniProt
Manually annotated by BRENDA team
Wistar rat
UniProt
Manually annotated by BRENDA team
strain GK24
-
-
Manually annotated by BRENDA team
Thermus caldophilus GK24
strain GK24
-
-
Manually annotated by BRENDA team
isoforms HD1B-I, HD1B-II
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
alkylation (carbonylation) of conserved cysteine residues in HDAC1, -2 and -3 antagonizes their deacetylase activity and transcriptional co-repressor function
malfunction
-
down-regulation of HDAC gene HDA710 induces a semi-dwarf phenotype, down-regulation of HDAC gene HDA704 affects plant height and flag leaf development
malfunction
-
down-regulation of HDAC gene HDA710 induces a semi-dwarf phenotype, down-regulation of HDAC gene HDA704 affects plant height and flag leaf development
malfunction
-
HDAC inhibition improves DELTAF508 cystic fibrosis transmembrane conductance regulator stability and trafficking, silencing of HDAC2 and HDAC3 causes a 2.5fold and 1.5fold increase in DELTAF508 cystic fibrosis transmembrane conductance regulator mRNA, respectively, as well as an about 5fold increase in total DELTAF508 protein. Silencing of HDAC1 induces a 1.4fold stimulation of iodide efflux. In contrast, silencing of HDAC7 exhibits a 3.6fold stimulation of cAMP-mediated iodide efflux comparable to 30C efflux
malfunction
-
HDAC1 and HDAC2 with carboxy-terminal domains deleted, retain enzymatic activity but are unable to repress cartilage gene expression
malfunction
-
HDAC7 knockdown causes increased nuclear beta-catenin, decreased transcription of HDAC7, decreased expression of E2F2, cyclin-D1 and cyclin-E2, and increased retinoblastoma protein
malfunction
-
inhibition of histone deacetylase activity down-regulates urokinase plasminogen activator and matrix metalloproteinase-9 expression in gastric cancer
malfunction
-
inhibition of SIRT1 activity leads to a recovery from the intrinsic repressive activity of orphan nuclear receptor small heterodimer partner (SHP) but not of DAX1. Inhibition of SIRT1 significantly diminishes the repressive effect of SHP on liver receptor homolog 1 transactivity. Inhibition of SIRT1 activity significantly reverses SHP-mediated inhibition of bile-acid synthesis by liver receptor homolog 1 overexpression
malfunction
-
knockdown of HDAC1 can generate a remarkable defect in proliferation and also can significantly induce apoptosis and S-phase arrest in PaTu-8988 cells
malfunction
-
knockdown of HDAC10 significantly increases the mRNA expression levels of thioredoxin-interacting protein and induces release of cytochrome c and activated apoptotic signaling molecules through accumulation of reactive oxygen species in SNU-620 human gastric cancer cells
malfunction
-
short hairpin-RNA silencing of either HDAC2 or HDAC4 is sufficient to induce p21 expression
malfunction
-
suppression of HDAC3 reduces the migration and induces the expression of E-cadherin in ovarian cancer cells
malfunction
-
while brain development and adult stem cell fate are normal upon conditional deletion of HDAC2 or in mice lacking the catalytic activity of HDAC2, neurons derived from both zones of adult neurogenesis die at a specific maturation stage
metabolism
-
nitrative/oxidative stress reduce HDAC2 expression via nitration of distinct tyrosine residues. Peroxynitrite, hydrogen peroxide and cigarette smoke-conditioned medium reduce HDAC2 expression in A549 epithelial cells in vitro. This reduction is due to increased proteasomal degradation following ubiquitination rather than reduction of mRNA expression or stability
physiological function
-
regulator of cellular pathways like response to stress, protein folding, microtubule stability and cell migration
physiological function
-
ectopic overexpression of HDAC6 isotype increases the levels of phosphorylated epidermal growth factor receptor and phosphorylated AKT expression. HDAC6 plays an important role in the modulation of radiation response of epidermal growth factor receptor and human epidermal growth factor receptor 2-activated cells
physiological function
-
HDAC catalyze the removal of acetyl groups from core histones inducing local condensation of chromatin. Therefore, HDACs are generally considered repressors of transcription. Coiled-coil domain-containing protein 6 physically interacts with HDAC1 on the amphiregulin promoter. Coiled-coil domain-containing protein 6 requires HDAC1 activity to repress cAMP responsive element binding protein 1 target gene transcription
physiological function
-
HDAC1 and HDAC2 repress aggrecan and collagen 2(alpha1) expression but differ in their repression of collagen 9(alpha1), collagen 11(alpha1), dermatopontin, and cartilage oligomeric matrix protein. Carboxy-terminal domains of HDAC1 and HDAC2 are not required for enzymatic activity in vitro but are required for optimal deacetylation in vivo and repression of cartilage-specific gene expression
physiological function
-
HDAC1 enhances cell proliferation of ovarian cancer cells, the expression of HDAC1 and HDAC2 is correlated with the proliferation marker Ki-67 expression, and HDAC3 stimulates cell migration with downregulation of E-cadherin in ovarian carcinoma
physiological function
-
HDAC10 is involved in transcriptional downregulation of thioredoxin-interacting protein, leading to altered reactive oxygen species signaling in human gastric cancer cells
physiological function
-
HDAC2 and HDAC1 are required for glucocorticoid receptor-mediated gene activation. HDAC2, however, is regulated through a different mechanism from that of HDAC1. Acetylated HDAC1 can trans-regulate HDAC2 through heterodimerization. Both HDAC1 and HDAC2 are required for mouse mammary tumor virus transcription
physiological function
-
HDAC6 is necessary for protein aggregate formation and degradation
physiological function
-
HDAC6 mediates TGF-beta1-induced epithelial-mesenchymal transition in A-549 cells. Splicing variant HDAC6p114 is required for TGF-beta1-activated gene expression associated with epithelial-mesenchymal transition in A-549 cells
physiological function
-
HDAC7 overexpression has the ability to trump vascular endothelial growth factor signaling to inhibit endothelial cell proliferation, overexpression of HDAC7 leads to decreased nuclear beta-catenin and decreased activity of beta-catenin-dependent effectors and an associated inhibition of endothelial cell proliferation
physiological function
-
HDAC7 plays a central role in restoration of DELTAF508 cystic fibrosis transmembrane conductance regulator function
physiological function
-
HDACs regulate hepatocyte growth factor-induced urokinase plasminogen activator and matrix metalloproteinase-9 expression through a protein kinase C-dependent signal pathway in gastric cancer cells
physiological function
-
orphan nuclear receptor small heterodimer partner (SHP) interacts and co-localizes specifically with SIRT1 in vivo. SHP recruits SIRT1 on liver receptor homolog 1 target gene promoters and SIRT1 deacetylates template-dependent histone H3 and H4 to inhibit transcription of liver receptor homolog 1 target genes
physiological function
-
SIRT6 is a site-specific histone deacetylase that regulates chromatin structure. SIRT6 is implicated in fundamental biological processes in aging, including maintaining telomere integrity, fine-tuning aging-associated gene expression programs, preventing genomic instability, and maintaining metabolic homeostasis. The N-terminal extension of SIRT6 is critical for chromatin association and intrinsic catalytic activity
physiological function
-
the catalytic function of HDAC2 is required in adult but not embryonic neurogenesis. HDAC2 is critically required to silence progenitor transcripts during neuronal differentiation of adult generated neurons
physiological function
-
the HDAC gene HDA703 is involved in histone H4 acetylation in rice, HDAC gene HDA703 has a function during plant reproductive development and seed morphology, HDA702/HDAC1 and HDA710 play a similar but important role in root and vegetative growth
physiological function
-
the HDAC gene HDA703 is involved in histone H4 acetylation in rice, HDAC gene HDA703 has a function during plant reproductive development and seed morphology, HDA702/HDAC1 and HDA710 play a similar but important role in root and vegetative growth
physiological function
-
the HDAC1 overexpression plays an important role in tumorigenesis of pancreatic cancer
physiological function
-
activity of histone deacetylases influences splice site selection. Splicing of 700 genes in heLa cells is altered after HDAC inhibition. HDAC inhibition induces histone H4 acetylation and increases RNA Polymerase II processivity along an alternatively spliced element. In addition, HDAC inhibition reduces co-transcriptional association of the splicing regulator SRp40 with the target fibronectin exon. The depletion of HDAC1 has similar effect on fibronectin alternative splicing as global HDAC inhibition. This effect is reversed upon expression of mouse HDAC1 but not a catalytically inactive mutant
physiological function
-
embryos injected with mRNA encoding a dominant-negative form of histone deacetylase lacked expression of gene Nodal related, Nr1, and exhibit randomized sidedness of the heart and viscera at stage 45. Pharmacological blockade of HDACs implicates cleavage stages as the active period. Inhibition during these early stages is correlated with an absence of Nr1 expression at stage 21, high levels of heterotaxia at stage 45, and the deposition of the epigenetic marker H3K4me2 on the Nr1 gene. The known HDAC partner protein Mad3 is a 5HT-binding regulator. While Mad3 overexpression leads to an absence of Nr1 transcription and randomizes the left-right axis, a mutant form of Mad3 lacking 5HT binding sites is not able to induce heterotaxia
physiological function
-
HDAC9 gene knockdown produces dose-dependent gamma-globin gene silencing over an 80-320 nM range. Enforced expression of HDAC9 produces a dose-dependent 2.5fold increase in gammaglobin mRNA. HDAC9 binds in vivo in the upstream Ggamma-globin gene promoter region. Treatment of primary erythroid progenitors with HDAC9 siRNA results in 40 and 60% gamma-globin gene silencing in day 11 (early) and day 28 (late) progenitors, respectively. Enforced HDAC9 expression increases gamma-globin mRNA levels by 2.5fold with a simultaneous 7fold increase in fetal hemoglobin
physiological function
-
in liver, class IIa HDACs HDAC4, 5, and 7, are phosphorylated and excluded from the nucleus by AMPK family kinases. In response to the fasting hormone glucagon, these HDACs are rapidly dephosphorylated and translocated to the nucleus where they associate with the promoters of gluconeogenic enzymes such as G6Pase. In turn, HDAC4/5 recruit HDAC3, which results in the acute transcriptional induction of these genes via deacetylation and activation of FOXO family transcription factors. Loss of class IIa HDACs in murine liver results in inhibition of FOXO target genes and lowers blood glucose, resulting in increased glycogen storage
physiological function
-
Lysine-specific demethylase 1 has a repressive role in proinflammatory cytokine expression such as IL1alpha, IL1b,eta IL6 and IL8 and classical complement components. HDAC1 and lysine-specific demethylase 1 synergistically regulate these inflammatory-related genes
physiological function
Q7RY64, Q7S8C9, Q7SEB0, Q7SEL7
mutation of HDA-1 by repeat-induced point mutation causes partial loss of DNA methylation. The site-specific loss of DNA methylation in hda-1 correlates with loss of H3 lysine 9 trimethylation and increased H3 acetylation. In addition, an increase in H2B acetylation is observed by two-dimensional gel electrophoresis of histones of the hda-1 mutant
physiological function
-
role for Clr6 in transcriptional regulation of amino acid permease gene per1. When ammonia is used as the nitrogen source, low levels of per1 are transcribed and histones in the coding and surrounding regions of per1 are acetylated. In the presence of proline, histones at per1 are deacetylated in a Clr6-dependent manner
physiological function
-
simultaneous treatment with IFNalpha2 and inhibitor trichostatin A, as well as combined HDAC1/HDAC2 silencing, restores STAT3-dependent reporter gene and endogenous gene expression, strongly suggesting that HDAC1 and HDAC2 are directly involved in repressing IFNalpha2-activated STAT3. In contrast, HDAC1 and HDAC2 activities are required for ISGF3-dependent gene expression. HDAC1 and HDAC2 differentially modulate STAT activity in response to IFNalpha2, while they are required for the induction of ISGF3-responsive genes, they impair the transcription of STAT3-dependent genes
physiological function
-
Sir2 is involved in protection against Hog1-induced cell death and can suppress Hog1-induced reactive oxygen species accumulation. Therefore, cell death seems to be dictated by the balance of reactive oxygen species induced by Hog1 and the protective effect of Sir2. Prolonged activation of stress-activated protein kinase leads to cell death, by causing accumulation of reactive oxygen species. Mutations of the SCF-CDC4 ubiquitin ligase complex suppress cell death by preventing the degradation of Msn2 and Msn4 transcription factors. Accumulation of transcription factors Msn2 and Msn4 leads to the induction of PNC1, which is an activator of the Sir2 histone acetylase
physiological function
-
Sirt1 inhibits T cell activation by suppressing the transcription of Bcl2-associated factor 1, Bclaf1, a protein required for T cell activation. Sirt1-null T cells have increased acetylation of the histone 3 lysine 56 residue, H3K56, at the bclaf1 promoter, as well as increasing Bclaf1 transcription. Sirt1 binds to bclaf1 promoter upon T cell receptor/CD28 stimulation by forming a complex with histone acetyltransferase p300 and NF-kappaB transcription factor Rel-A. The recruitment of Sirt1, but not p300, requires Rel-A. Knockdown of Bclaf1 suppresses the hyperactivation observed in Sirt1-/- T cells. Therefore, Sirt1 negatively regulates T cell activation via H3K56 deacetylation at the promoter region to inhibit transcription of Bclaf1
physiological function
Q7RY64, Q7S8C9, Q7SEB0, Q7SEL7
the hda-2 mutation does not affect DNA methylation at any region tested, and the deletion and repeat-induced point mutation alleles give identical results
physiological function
Q7RY64, Q7S8C9, Q7SEB0, Q7SEL7
the hda-3 mutation leads to global increases in histones H3 and H4 acetylation levels and to partial loss of DNA methylation
physiological function
Q7RY64, Q7S8C9, Q7SEB0, Q7SEL7
the hda-4 mutation leads to global increases in histones H3 and H4 acetylation levels
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AC-Arg-Gly-Lys(AC)-4-amino-7-methylcoumarin + H2O
?
show the reaction diagram
-
substrate activity assay
-
-
?
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-Leu-Gly-Lys(Ac)-7-amido-4-methylcoumarin + H2O
Ac-Leu-Gly-Lys-7-amido-4-methylcoumarin + acetate
show the reaction diagram
Q7K6A1
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
Fluor de Lys + H2O
?
show the reaction diagram
-
-
-
-
?
Fluor de Lys + H2O
?
show the reaction diagram
O67135
-
-
-
?
Fluor de Lys H4-AcK16 + H2O
?
show the reaction diagram
-
-
-
-
?
Fluor de Lys HDAC substrate + H2O
?
show the reaction diagram
-
-
-
-
?
Fluor de Lys HDAC substrate + H2O
?
show the reaction diagram
Q8WUI4
commercially available kit
-
-
?
Fluor de Lys HDAC8 substrate + H2O
?
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 H1 + H2O
acetate + histone H1
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-histone H3 + H2O
acetate + histone H3
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-histone H3 + H2O
acetate + histone H3
show the reaction diagram
-
-
individual lysine residues in the H3 tail are deacetylated at similar rates
-
?
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-histone H4 + H2O
acetate + histone H4
show the reaction diagram
Q2QWU2, Q5VP94, Q6YV04
-
-
-
?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
show the reaction diagram
-
-
rate of deacetylation is not uniform. H4 K5 is deacetylated first, followed by K8, K12 and K16. The specificity of deacetylation and the histone-binding preference of transcriptional co-repressors N-CoR/SMRT match each other, rate of deacetylation by isoform HDAC3 is not uniform. H4 K5 is deacetylated first, followed by K8, K12 and K16. The specificity of deacetylation and the histone-binding preference of transcriptional co-repressors N-CoR/SMRT match each other
-
?
N-acetyl-lysine-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, transcrition factor MyoD
-
-
?
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 H2A-H2B dimer + H2O
histone H3-H4 dimer + acetate
show the reaction diagram
P56517
-
-
-
?
N6-lysine acetylated histone H2A-H2B dimer + H2O
histone H3-H4 dimer + acetate
show the reaction diagram
-
isoform HD2, slightly preferred substrate
-
-
?
N6-lysine acetylated histone H3 + H2O
histone H3 + acetate
show the reaction diagram
Q9BY41
-
-
-
?
N6-lysine acetylated histone H3 + H2O
histone H3 + acetate
show the reaction diagram
-
-
-
-
?
N6-lysine acetylated histone H3-H4 tetramer + H2O
histone H3-H4 tetramer + acetate
show the reaction diagram
P56517
preferred substrate
-
-
?
N6-lysine acetylated histone H3-H4 tetramer + H2O
histone H3-H4 tetramer + acetate
show the reaction diagram
-
isoform HD1, preferred substrate
-
-
?
N6-lysine acetylated histone H4 + H2O
histone H4 + acetate
show the reaction diagram
Q9BY41
-
-
-
?
N6-lysine acetylated histone H4 + H2O
histone H4 + acetate
show the reaction diagram
-
substrate of isoforms HDAC1, HDAC2, HDAC. HDAC3 preferentially cleeaves lysines 5 and 12 of H4. H4 tails in purified mononucleosomes are deacetylated by isoforms HDAC1 and HDAC3 only in presence of ATP
-
-
?
N6-lysine acetylated histone H4 peptide + H2O
histone H4 peptide + acetate
show the reaction diagram
Q9BY41
peptide of N-terminal 20 amino acids
-
-
?
N6-lysine-acetylated histone H4 peptide + H2O
acetate + histone H4 peptide
show the reaction diagram
Q96DB2
-
-
-
?
RHK(acetyl)K(acetyl)-fluorophore + H2O
RHKK-fluorophore + acetate
show the reaction diagram
-
i.e. Fluor de Lys, fluorogenic substrate
-
-
?
RHK(acetyl)K(acetyl)-fluorophore + H2O
RHKK-fluorophore + acetate
show the reaction diagram
Q9BY41
i.e. Fluor de Lys, fluorogenic substrate
-
-
?
RHK(acetyl)K(acetyl)-fluorophore + H2O
RHKK-fluorophore + acetate
show the reaction diagram
Q9UBN7
i.e. Fluor de Lys, fluorogenic substrate
-
-
?
tert-butyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Lys-7-amido-4-methylcoumarin + acetate
show the reaction diagram
-
-
-
-
?
Fluor de Lys HDAC8 substrate + H2O
?
show the reaction diagram
-
commercially available kit
-
-
?
additional information
?
-
-
conserved mechanism of histone deacetylase repression of some secondary metabolite gene clusters
-
-
-
additional information
?
-
-
histone deacetylases regulate the expression of HoxA9, which acts as a master switch to regulate the expression of prototypical endothelial-committed genes such as endothelial nitric oxide synthase, VE-cadherin, VEGF-R2, and mediates the shear stress-induced maturation of endothelial cells
-
-
-
additional information
?
-
-
isoform HDAC4 is an essential regulator of myofibroblastic differentiation
-
-
-
additional information
?
-
-
isoforms HDAC1 and HDAC2 are associated in vivo, complex is able to deacetylate all four core histones in vitro
-
-
-
additional information
?
-
-
Gal4-dHDAC1, consisting of the N-terminal 147 amino acid residues of the yeast Gal4 protein fused to the N terminus of full-length dHDAC1 protein, but not dHDAC1, is able to repress transcription in vitro. Transcriptional repression is blocked by the enzyme inhibitor FR901228
-
-
-
additional information
?
-
Q969S8
isoform HDAC10 represses transcription independent of its deacetylase activity
-
-
-
additional information
?
-
Q9UKV0
isoforms HDAC9 and HDAC9a both contain the histone deacetylase catalytic domain, possess histone deacetylase activity, and also repress myocyte enhancer-binding factor-2 mediated transcription
-
-
-
additional information
?
-
B2GUW3
acetylation of histone core proteins is regulated by HDAC, H3K9-K14 deacetylation is mediated, at least in part, by HDAC 11
-
-
-
additional information
?
-
-
deacetylation of tubulin
-
-
-
additional information
?
-
Q9Z2V5
deacetylation of tubulin
-
-
-
additional information
?
-
-
HDAC6 deacetylases tubulins, best noted substrate is beta-tubulin
-
-
-
additional information
?
-
-
HDACs catalyse the removal of acetyl groups from e-N-acetylated lysine residues of various protein substrates
-
-
-
additional information
?
-
Q8WUI4
HDACs catalyze the deacetylation of lysine residues in the N-terminal tails of core histones, in addition non-histone proteins may also serve as substrates
-
-
-
additional information
?
-
-
histone deacetylase proteins catalyze the removal of acetyl groups from acetylated lysines on histone substrates
-
-
-
additional information
?
-
-
histone deacetylases catalyse the removal of the N-acetyl lysine residues from the histone tails, they also deacetylate a growing number of non-histone proteins
-
-
-
additional information
?
-
Q13547
histone deacetylases catalyze the removal of acetyl groups from histones, leading to chromatin condensation and transcriptional repression
-
-
-
additional information
?
-
-
the acetylation status of lysine residues in nucleosomal proteins is tightly controlled by two counteracting enzyme families, the histone acetyl transferases and the histone deacetylases, HDACs
-
-
-
additional information
?
-
-
Fluor de Lys HDAC substrate, commercially available kit
-
-
-
additional information
?
-
-
HDAC7 binds directly to beta-catenin in the cytoplasm of endothelial cells
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
?
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 H1 + H2O
acetate + histone H1
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-histone H3 + H2O
acetate + histone H3
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
show the reaction diagram
Q2QWU2, Q5VP94, Q6YV04
-
-
-
?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
show the reaction diagram
-
-
-
-
?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
show the reaction diagram
-
-
rate of deacetylation is not uniform. H4 K5 is deacetylated first, followed by K8, K12 and K16. The specificity of deacetylation and the histone-binding preference of transcriptional co-repressors N-CoR/SMRT match each other
-
?
N-acetyl-lysine-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
-
-
?
alpha-tubulin + H2O
acetate + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
conserved mechanism of histone deacetylase repression of some secondary metabolite gene clusters
-
-
-
additional information
?
-
-
histone deacetylases regulate the expression of HoxA9, which acts as a master switch to regulate the expression of prototypical endothelial-committed genes such as endothelial nitric oxide synthase, VE-cadherin, VEGF-R2, and mediates the shear stress-induced maturation of endothelial cells
-
-
-
additional information
?
-
-
isoform HDAC4 is an essential regulator of myofibroblastic differentiation
-
-
-
additional information
?
-
-
isoforms HDAC1 and HDAC2 are associated in vivo, complex is able to deacetylate all four core histones in vitro
-
-
-
additional information
?
-
B2GUW3
acetylation of histone core proteins is regulated by HDAC, H3K9-K14 deacetylation is mediated, at least in part, by HDAC 11
-
-
-
additional information
?
-
-
deacetylation of tubulin
-
-
-
additional information
?
-
Q9Z2V5
deacetylation of tubulin
-
-
-
additional information
?
-
-
HDAC6 deacetylases tubulins, best noted substrate is beta-tubulin
-
-
-
additional information
?
-
-
HDACs catalyse the removal of acetyl groups from e-N-acetylated lysine residues of various protein substrates
-
-
-
additional information
?
-
Q8WUI4
HDACs catalyze the deacetylation of lysine residues in the N-terminal tails of core histones, in addition non-histone proteins may also serve as substrates
-
-
-
additional information
?
-
-
histone deacetylase proteins catalyze the removal of acetyl groups from acetylated lysines on histone substrates
-
-
-
additional information
?
-
-
histone deacetylases catalyse the removal of the N-acetyl lysine residues from the histone tails, they also deacetylate a growing number of non-histone proteins
-
-
-
additional information
?
-
Q13547
histone deacetylases catalyze the removal of acetyl groups from histones, leading to chromatin condensation and transcriptional repression
-
-
-
additional information
?
-
-
the acetylation status of lysine residues in nucleosomal proteins is tightly controlled by two counteracting enzyme families, the histone acetyl transferases and the histone deacetylases, HDACs
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
additional information
-
deacetylation by isoform dHDAC1 does not require any additional cofactors
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
ratio of kcat to KM value in presence of metal ion in decreasing order: Co(II), Fe(II), Zn(II), Ni(II)
Co2+
-
-
Fe2+
-
ratio of kcat to KM value in presence of metal ion in decreasing order: Co(II), Fe(II), Zn(II), Ni(II). Fe(II) bound to enzyme is readily oxidized to Fe(III) upon exposure to oxygen
Fe2+
-
-
K+
Q9BY41
presence of two potassium ions in the structure of isoform HDAC8, one of which interacts with the key catalytic residues. Direct role of potassium in fold stabilization
K+
-
K+ bound to monovalent cation site 2 enhances catalytic activity of HDAC8 45fold with maximal deacetylase activity observed at 10 mM KCl. K+ is the predominant monovalent cation bound to HDAC8 in vivo, K+ binding to site 1 enhances the affinity of HDAC8 for suberoylanilide hydroxamic acid
Mg2+
-
Zn2+, Mg2+, or Mn2+ is required. Zn2+ is the most efficient
Na+
-
Na+ binds more weakly to both monovalent cation sites and activates HDAC8 to a lesser extent than K+
Ni2+
-
ratio of kcat to KM value in presence of metal ion in decreasing order: Co(II), Fe(II), Zn(II), Ni(II)
Zinc
-
enzyme active site consists of a tubular pocket, a zinc-binding site and two D-H charge-relay systems
Zn2+
-
Zn2+, Mg2+, or Mn2+ is required. Zn2+ is the most efficient
Zn2+
-
ratio of kcat to KM value in presence of metal ion in decreasing order: Co(II), Fe(II), Zn(II), Ni(II)
Mn2+
-
Zn2+, Mg2+, or Mn2+ is required. Zn2+ is the most efficient
additional information
-
the identity of the catalytic metal ion influences both the Michaelis-Menten constant and the affinity of inhibitor suberoylanilide hydroxamic acid, with Fe(II) and Co(II) giving KM values 5fold lower than that of Zn(II). Apo-enzyme has a low residual level of activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(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
Q8WUI4
-
(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
-
-
(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
Q94BN7
-
(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
Q94BN7
-
(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
Q94BN7
-
(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
Q94BN7
-
(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
Q94BN7
-
(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
Q94BN7
-
(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
Q94BN7
-
(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
Q94BN7
-
(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]
Q94BN7
-
(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
Q94BN7
-
(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)-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
-
-
1,10-phenanthroline
P56517
10 mM, 66% inhibition
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
2,3-dihydrobenzoic acid
-
98% residual activity at 0.5 mM
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-benzoylbenzoic acid
-
and hydroxamate analogs
3-benzoylpropanoic acid
-
and hydroxamate analogs
3-hydroxycinnamic acid
-
96% residual activity at 0.5 mM
3-morpholinosydonomine
-
i.e. SIN-1. The expression of wild-type, Y153A and Y146A HDAC2 mutants is reduced following 4 h treatment with 250 microM SIN-1. The expression of the Y253A HDAC2 mutant is not reduced by SIN-1
-
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-thioxo-3H-1,2-dithiol-5-yl)phenyl 2-propylpentanoate
-
-
4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide
-
M344
4-benzoylbutyric acid
-
and hydroxamate analogs
4-benzoylbutyric hydroxamic acid
-
-
4-hydroxy-2-nonenal
-
maximal inhibition of recombinant HDAC3 in complex with CoR1 is 70%
4-Phenylbutyric acid
-
and hydroxamate analogs
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
-
-
5-phenylvaleric acid
-
and hydroxamate analogs
5-phenylvaleric hydroxamic acid
-
-
6-mercapto-N-phenylhexanamide
-
-
6-[(1-(mercaptomethyl)vinyl)amino]-N-phenylhexanamide
-
-
6-[(2E)-2-[(2-bromo-4-hydroxy-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
Q7K6A1
-
6-[(2E)-2-[(2-bromo-4-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
Q7K6A1
-
6-[(2E)-2-[(2-bromo-5-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
Q7K6A1
-
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
O67135
simultaneous and efficient interactions of compound with both the enzyme surface and the tubular binding pocket, through proper selection of its arm groups, are critical for potential antagonist activity
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-[(2E)-2-[(2-bromo-4-hydroxy-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
7-[(2E)-2-[(2-bromo-5-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
7-[(2E)-2-[(2-bromo-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
7-[(2E)-2-[(2-bromophenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
7-[(2E)-2-[(2-bromopyridin-3-yl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
7-[(2E)-2-[(2-chlorophenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
7-[(2E)-2-[(6-bromo-1,3-benzodioxol-5-yl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
7-[(2E)-2-[[4-(dimethylamino)-2-hydroxyphenyl]methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
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
8-[(2E)-2-[(2,5-dihydroxyphenyl)methylidene]hydrazino]-N-hydroxy-8-oxooctanamide
Q7K6A1
-
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
-
natural inhibitor
apicidin A
-
-
azumamide E
-
-
Baclofen
-
98% residual activity at 0.5 mM
belinostat
-
PXD101
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
-
non-competitive
Butyrate
-
inhibition of histone deacetylase activity, resulting in prevention of interferon gamma-induced Janus kinase 1 activation, STAT1 phosphorylation, its nuclear translocation, and STAT1-dependent gene activation
Butyrate
-
inhibition of histone deacetylases, results in down-regulation of HoxA9 expression
Butyrate
-
class I-selective HDAC inhibitor
Butyric acid
-
-
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
EDTA
-
1 mM, 30 min, complete loss of activity. Zn2+, Mg2+, Mn2+ may restore activity
entinostat
-
MS-275
ferulic acid
-
80% residual activity at 0.5 mM
FK-228
-
natural inhibitor
FOXP
-
FOXP3 specifically inhibits binding of histone deacetylase 2 and 4 to the site and increases local histone H3 acetylation
-
FR901228
-
Gal4-dHDAC1, consisting of the N-terminal 147 amino acid residues of the yeast Gal4 protein fused to the N terminus of full-length dHDAC1 protein, but not dHDAC1, is able to repress transcription in vitro. Transcriptional repression is blocked by the enzyme inhibitor FR901228
gamma-aminobutyric acid
-
-
HC-toxin
-
cyclic peptide inhibitor from Cochliobolus carbonum. Histone deacetylase in crude extracts of Alternaria brassicola is relatively insensitive to inhibition, such as enzyme from Cochliobolus carbonum. Comparison of sensitivity in various Cochliobolus carbonum strains and in several other fungi
HC-toxin
Q8X1S4
cyclic peptide inhibitor from Cochliobolus carbonum. Histone deacetylase in crude extracts of Cochliobolus carbonum is relatively insensitive to inhibition. Comparison of sensitivity in various Cochliobolus carbonum strains and in several other fungi. Resistance genetically cosegregates with toxin production
HC-toxin
-
cyclic peptide inhibitor from Cochliobolus carbonum. Histone deacetylase in crude extracts of Diheterospora chlamydosporia is relatively insensitive to inhibition, such as enzyme from Cochliobolus carbonum. Comparison of sensitivity in various Cochliobolus carbonum strains and in several other fungi
HDAC1 siRNA
-
-
-
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
-
broad-spectrum or pan-HDAC inhibitor
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
LAQ824
-
enzyme inhibition results in altered Toll-like receptor 4-dependent activation and function of macrophages and dendritic cells. Pan-HDAC inhibition modulates only a limited set of genes involved in distinct arms of immune responses, specifically dendritic cell-controlled T helper 1 effector, but not T helper 2 effector cell activation and migration. It also inhibits dendritic cell-mediated monocyte, but not neutrophil chemotaxis
LAQ824
Q8WUI4
-
LAQ824
-
pan-HDAC inhibitor
largazole
-
-
largazole
Q94BN7
FK228; FK228; FK228; FK228
LBH-589
-
panobinostat, broad-spectrum or pan-HDAC inhibitor
LBH589
Q8WUI4
-
LBH589
-
pan-histone deacetylase inhibitor
Mandelic acid
-
85% residual activity at 0.5 mM
MC1568
P56524
specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs
MC1575
P56524
specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs; specificity for class II HDACs
MCP30
-
30 kDa protein isolated from bitter melon seeds, Momordica charantia, contains two highly related type I ribosome-inactivating proteins, alpha- and beta-momorcharin
-
methyl (3R,6R,9R)-9-(acetylamino)-6-[6-(hydroxyamino)-6-oxohexyl]-5,8-dioxo-4,7-diazabicyclo[9.3.1]pentadeca-1(15),11,13-triene-3-carboxylate
-
tight binding competitive inhibition
methyl N-[(2S)-2-[(N-acetyl-L-alanyl)amino]-7-(hydroxyamino)-7-oxoheptanoyl]-L-phenylalaninate
-
-
MGCD-0103
-
mocetinostat dihydrobromide, class I-selective HDAC inhibitor
MS-275
-
inhibition of histone deacetylases, results in down-regulation of HoxA9 expression
MS-275
-
SNDX-275, entinostat, class I-selective HDAC inhibitor
MS-275
-
inhibition of HDAC1 leads to a significant increase of global acetylation of residues K9 and K14 on histone H3, which is a feature of active transcription, and a significant induction of proinflammatory cytokine expression. Genomic DNA corresponding to the IL1beta and IL6 promoter is significantly enriched upon HDAC 1 inhibition
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-aminopyrimidin-5-yl)-5-[(6-oxo-4-phenyl-1,6-dihydropyrimidin-2-yl)sulfanyl]pentanamide
-
-
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-[1-methyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]cyclopropanecarboxamide
-
-
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
Q9BY41
-
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-5-(4-phenyl-1H-1,2,3-triazol-1-yl)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-7-(4-phenyl-1H-1,2,3-triazol-1-yl)heptanamide
-
-
N-hydroxy-7-[(2E)-2-[(2-hydroxynaphthalen-1-yl)methylidene]hydrazino]-7-oxoheptanamide
Q7K6A1
-
N-hydroxy-7-[(2E)-2-[(3-hydroxyphenyl)methylidene]hydrazino]-7-oxoheptanamide
Q7K6A1
-
N-hydroxy-7-[(2E)-2-[[4-(1H-imidazol-1-yl)phenyl]methylidene]hydrazino]-7-oxoheptanamide
Q7K6A1
-
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-8-oxo-8-[(2E)-2-[(2,4,6-trihydroxyphenyl)methylidene]hydrazino]octanamide
Q7K6A1
-
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
Q94BN7
-
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
Q94BN7
-
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
-
-
NaCl
P56517
inhibitory in sodium phosphate/citric acid buffer, 50% inhibition at 100 mM
NVP-LAQ824
-
-
oxamflatin
Q8WUI4
-
p300
-
p300 can inactivate HDAC6 by acetylation
-
panobinostat
-
LBH-589
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
-
belinostat, broad-spectrum or pan-HDAC inhibitor
pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
Q9BY41
i.e. MS27-275
romidepsin
-
FK-228, FR901228, depsipeptide, class I-selective HDAC inhibitor
romidepsin
-
FK228
S-(2-hydroxyethyl) methanesulfonothioate
-
-
S-nitrosocysteine
Q9BY41
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
Q9BY41
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
-
-
-
shRNA
Q9Z2V5
-
-
siRNA
B2GUW3
-
-
SK7041
-
i.e. 4-dimethylamino-N-[4-(2-hydroxylcarbamoyl-vinyl)benzyl] benzamide
sodium butyrate
-
-
sodium butyrate
-
-
sodium butyrate
-
pan-HDAC inhibitor
sodium phenylbutyrate
-
-
sorbic acid
-
91% residual activity at 0.5 mM
spiruchostatin
-
-
splitomicin
Q7K6A1
-
suberoyl anilide hydroxamic acid
-
-
suberoylanilide hydroxamic acid
-
inhibition of histone deacetylase activity, resulting in prevention of interferon gamma-induced Janus kinase 1 activation, STAT1 phosphorylation, its nuclear translocation, and STAT1-dependent gene activation
suberoylanilide hydroxamic acid
-
SAHA, vorinostat, zolinza, broad-spectrum or pan-HDAC inhibitor
suberoylanilide hydroxamic acid
-
SAHA, synthetic inhibitor
suberoylanilide hydroxamic acid
-
SAHA
suberoylanilide hydroxamic acid
-
SAHA, vorinostat
suberoylanilide hydroxamic acid
Q7K6A1
SAHA
suberoylanilide hydroxamic acid
-
SAHA
suberoylanilide hydroxamic acid
P56524
SAHA; SAHA; SAHA; SAHA; SAHA
suberoylanilide hydroxamic acid
-
pan-HDAC inhibitor
suberoylanilide hydroxamic acid
-
i.e. SAHA, antiproliferative activities against MDA-MB-231 and K562 cell lines, IC50 0.00132 and 0.00169 microM, respectively
sulforaphane
-
at 0.015 mM, 40, 30 and 40% inhibition of histone deacetylase activities in BPH-1, LnCaP and PC-3 prostate epithelial cells, resp. Inhibition is accompanied by a 50-100% increase in acetylated histones. BPH-1 cells treated with inhibitor show enhanced interaction of acetylated histone H4 with the promoter region of the P21 gene and the bax gene
sulforaphane
-
SFN, found in broccoli sprouts
tartaric acid
-
90% residual activity at 0.5 mM
trapoxin A
-
-
trapoxin B
-
natural inhibitor
trapoxin B
-
-
trichostatin A
-
-
trichostatin A
-
inhibition of histone deacetylase activity, resulting in prevention of interferon gamma-induced Janus kinase 1 activation, STAT1 phosphorylation, its nuclear translocation, and STAT1-dependent gene activation
trichostatin A
-
inhibition of histone deacetylases, results in down-regulation of HoxA9 expression
trichostatin A
Q7Z8L7, Q7Z8L9
-
trichostatin A
-
natural inhibitor
trichostatin A
Q803C3
-
trichostatin A
B2GUW3
-
trichostatin A
-
TSA
trichostatin A
Q7K6A1
TSA
trichostatin A
-
TSA
trichostatin A
P56524
TSA; TSA; TSA; TSA; TSA
trichostatin-A
-
specific HDAC inhibitor
trichostatin-A
Q2QWU2, Q5VP94, Q6YV04
specific HDAC inhibitor; specific HDAC inhibitor; specific HDAC inhibitor
troglitazone
-
-
tubacin
-
HDAC6-selective inhibitor
tubacin
Q8WUI4
-
Valeric acid
-
83% residual activity at 0.5 mM
Valproate
-
class I-selective HDAC inhibitor
Valproic acid
-
treatment causes hyperacetylation of histones in cultured cells and activates transcription from diverse exogenous and endogenous promoters
Valproic acid
Q803C3
-
Valproic acid
-
Depakene, Convulex
Valproic acid
-
-
vorinostat
-
SAHA
[4-[(E)-[[6-(hydroxyamino)-6-oxohexanoyl]hydrazono]methyl]phenyl]boronic acid
Q7K6A1
-
MGCD-0103
-
-
additional information
-
in phosphate buffer, the presence of NaCl is inhibitory
-
additional information
Q969S8
isoform HDAC10 is resistant to inhibitors trapoxin B and sodium butyrate
-
additional information
Q7Z8L7, Q7Z8L9
enzyme is part of a high molecular weight complex insensitive to trichostatin A
-
additional information
-
when A-549 cells are stretched for 24 h cytoplasmic HDAC activity is decreased
-
additional information
-
nitration of distinct tyrosine residues
-
additional information
-
HDAC is not inhibited by isovaleric acid, L-valine, sodium lactate, succinic acid, citric acid, benzylic acid, hippuric acid, antranilic acid (2-aminobenzoic acid), alpha-hydroxyacetonaphthone, and kojic acid
-
additional information
-
methylselenocysteine and selenomethionine have little or no inhibitory activity up to 2 mM
-
additional information
-
the CDK-related kinase 3-associated HDAC activities are sensitive to the class I/II HDAC inhibitor trichostatin A and to the sirtuin inhibitor nicotinamide
-
additional information
-
3-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid shows no inhibition of HDAC1 at 0.01 mM, 2,2,2-trifluoro-1-[5-(pyridin-2-yl)thiophen-2-yl]ethanone is inactive against HDAC6, 2,2,2-trifluoro-1-[5-(1H-indol-5-yl)thiophen-2-yl]ethanone is essentially inactive against HDAC1 and 4
-
additional information
-
HDAC10 is not inhibited by SK7068, MS275, and oxamflatin
-
additional information
-
nitrative/oxidative stress reduce HDAC2 expression via nitration of distinct tyrosine residues. Peroxynitrite, hydrogen peroxide and cigarette smoke-conditioned medium reduce HDAC2 expression in A549 epithelial cells in vitro. This reduction is due to increased proteasomal degradation following ubiquitination rather than reduction of mRNA expression or stability
-
additional information
-
presence of 5-6 carbon units between the Zn2+ binding group and the 1,3,4-thiadiazole ring is optimal for inhibitory potency
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
N-(cyclohexylcarbamothioyl)benzamide
-
10 microM, 5.6fold activation of HDAC8. No activation of other HDAC isoenzymes
N-(phenylcarbamothioyl)benzamide
-
10 microM, 12fold activation of HDAC8. No activation of other HDAC isoenzymes
N-[(3,5-dimethoxyphenyl)carbamothioyl]benzamide
-
10 microM, 8.4fold activation of HDAC8. No activation of other HDAC isoenzymes
heat shock protein 70
P70288
Hsp70
-
additional information
-
in Tris/HCl buffer, optimum concentration of NaCl is 50 mM for isoforms HD1 and HD2 and 100 mM for the nuclear matrix form
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00244
-
Ac-DQK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC3
0.01646
-
Ac-DQK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC6
0.00228
-
Ac-FEK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC6
0.0046
-
Ac-FEK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC3
0.0117
-
Ac-FEK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1
0.0353
-
Ac-FEK(acetyl)-7-amido-4-methylcoumarin
-
isoform FB188 HDAH
0.0359
-
Ac-FEK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC8
0.0043
-
Ac-GGK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC6
0.01
-
Ac-GGK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC3
0.0138
-
Ac-GGK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1
0.0391
-
Ac-GGK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC8
0.0877
-
Ac-GGK(acetyl)-7-amido-4-methylcoumarin
-
isoform FB188 HDAH
0.0123
-
Ac-GS(PO3)K(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC6
0.0276
-
Ac-GS(PO3)K(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC3
0.046
-
Ac-GS(PO3)K(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1
0.0489
-
Ac-GS(PO3)K(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC8
0.0666
-
Ac-GS(PO3)K(acetyl)-7-amido-4-methylcoumarin
-
isoform FB188 HDAH
0.00405
-
Ac-GSK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC3
0.0108
-
Ac-GSK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC8
0.011
-
Ac-GSK(acetyl)-7-amido-4-methylcoumarin
-
isoform FB188 HDAH
0.0133
-
Ac-GSK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1
0.0241
-
Ac-GSK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC6
0.00069
-
Ac-IHK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1
0.00625
-
Ac-IHK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC6
0.0091
-
Ac-IHK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC8
0.0148
-
Ac-IHK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC3
0.108
-
Ac-IHK(acetyl)-7-amido-4-methylcoumarin
-
isoform FB188 HDAH
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
-
Ac-KYK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC8
0.0056
-
Ac-KYK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1
0.00745
-
Ac-KYK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC3
0.107
-
Ac-KYK(acetyl)-7-amido-4-methylcoumarin
-
isoform FB188 HDAH
0.03
-
Ac-Leu-Gly-Lys(Ac)-7-amido-4-methylcoumarin
Q7K6A1
apparent KM
0.00303
-
Ac-LIK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1
0.0069
-
Ac-LYK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC3
0.0294
-
Ac-LYK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1
0.03
-
Ac-LYK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC6
0.01
-
Ac-PFK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC8
0.0119
-
Ac-VLK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC3
0.015
-
Ac-VLK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1
0.0221
-
Ac-VLK(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC6
0.078
-
benzyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC1, 37C, pH not specified in the publication
-
0.099
-
benzyloxycarbonyl-L-Lys(acetyl)-7-amido-4-methylcoumarin
-
isoform HDAC6, 37C, pH not specified in the publication
-
0.03
-
benzyloxycarbonyl-L-Lys(trifluoroacetyl)-7-amido-4-methylcoumarin
-
isoform HDAC8, 37C, pH not specified in the publication
-
0.061
-
benzyloxycarbonyl-L-Lys(trifluoroacetyl)-7-amido-4-methylcoumarin
-
isoform HDAC7, 37C, pH not specified in the publication
-
0.000015
-
Fluor de Lys
Q9UBN7
mt H611A, pH 7.2, 23C
-
0.0024
-
Fluor de Lys
Q9UBN7
catalytic domain II, pH 7.2, 23C
-
0.0033
-
Fluor de Lys
Q9UBN7
wild-type, pH 7.2, 23C
-
0.0038
-
Fluor de Lys
Q9UBN7
mutant H216A, pH 7.2, 23C
-
0.013
-
Fluor de Lys HDAC substrate
Q8WUI4
mutant H843Y
-
0.016
-
Fluor de Lys HDAC substrate
Q8WUI4
mutant H843A; mutant H843F
-
0.017
-
Fluor de Lys HDAC substrate
Q8WUI4
wild type enzyme
-
0.066
-
Fluor de Lys HDAC substrate
-
mutant F150A
-
0.088
-
Fluor de Lys HDAC substrate
-
wild type
-
0.14
-
Fluor de Lys HDAC8 substrate
-
Co2+-D101E mutant
-
0.16
-
Fluor de Lys HDAC8 substrate
-
Co2+-wild type
-
0.23
-
Fluor de Lys HDAC8 substrate
-
presence of activator N-(phenylcarbamothioyl)benzamide, pH not specified in the publication, temperature not specified in the publication
-
0.744
-
Fluor de Lys HDAC8 substrate
-
pH not specified in the publication, temperature not specified in the publication
-
1
-
Fluor de Lys HDAC8 substrate
-
Co2+-D101A mutant, larger than 1.00; Co2+-D101L mutant, larger than 1.00; Co2+-D101N mutant, larger than 1.00; Co2+-H143A mutant, larger than 1.00
-
0.16
-
RHK(acetyl)K(acetyl)-fluorophore
-
presence of Co(II), 25C. pH 8.0
0.21
-
RHK(acetyl)K(acetyl)-fluorophore
-
presence of Fe(II), 25C. pH 8.0
1.1
-
RHK(acetyl)K(acetyl)-fluorophore
-
presence of Zn(II), 25C. pH 8.0
1.1
-
Fluor de Lys HDAC8 substrate
-
Zn2+-wild type
-
additional information
-
additional information
-
Km value according to commercial HDAC Fluorescent Activity Assay Kit is 0.143 mM
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.19
-
Ac-Leu-Gly-Lys(Ac)-7-amido-4-methylcoumarin
Q7K6A1
-
0.0019
-
Fluor de Lys
Q9UBN7
mt H611A, pH 7.2, 23C
-
0.037
-
Fluor de Lys
Q9UBN7
catalytic domain II, pH 7.2, 23C
-
0.27
-
Fluor de Lys
Q9UBN7
mutant H216A, pH 7.2, 23C
-
0.29
-
Fluor de Lys
Q9UBN7
wild-type, pH 7.2, 23C
-
0.0002
-
Fluor de Lys HDAC substrate
Q8WUI4
wild type enzyme
-
0.017
-
Fluor de Lys HDAC substrate
Q8WUI4
mutant H843F
-
0.018
-
Fluor de Lys HDAC substrate
Q8WUI4
mutant H843A
-
1.1
-
Fluor de Lys HDAC substrate
Q8WUI4
mutant H843Y
-
0.007
-
Fluor de Lys HDAC8 substrate
-
pH not specified in the publication, temperature not specified in the publication
-
0.036
-
Fluor de Lys HDAC8 substrate
-
presence of activator N-(phenylcarbamothioyl)benzamide, pH not specified in the publication, temperature not specified in the publication
-
0.15
-
Fluor de Lys HDAC8 substrate
-
Co2+-D101E mutant
-
0.9
-
Fluor de Lys HDAC8 substrate
-
Zn2+-wild type
-
1.2
-
Fluor de Lys HDAC8 substrate
-
Co2+-wild type
-
0.48
-
RHK(acetyl)K(acetyl)-fluorophore
-
presence of Fe(II), 25C. pH 8.0
0.9
-
RHK(acetyl)K(acetyl)-fluorophore
-
presence of Zn(II), 25C. pH 8.0
1.2
-
RHK(acetyl)K(acetyl)-fluorophore
-
presence of Co(II), 25C. pH 8.0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0007
-
(2E)-N-hydroxy-3-naphthalen-1-ylprop-2-enamide
-
HDAC8 inhibition
0.0033
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid (3,4-dimethylphenyl)-amide hydroxyamide
-
isoform HDAC7, 37C, pH not specified in the publication
0.0088
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid (3,4-dimethylphenyl)-amide hydroxyamide
-
isoform HDAC1, 37C, pH not specified in the publication
0.014
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid (3,4-dimethylphenyl)-amide hydroxyamide
-
isoform HDAC8, 37C, pH not specified in the publication
0.024
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid (3,4-dimethylphenyl)-amide hydroxyamide
-
isoform HDAC6, 37C, pH not specified in the publication
0.0053
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid biphenyl-2-ylamide hydroxyamide
-
isoform HDAC8, 37C, pH not specified in the publication
0.0092
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid biphenyl-2-ylamide hydroxyamide
-
isoform HDAC6, 37C, pH not specified in the publication
0.014
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid biphenyl-2-ylamide hydroxyamide
-
isoform HDAC7, 37C, pH not specified in the publication
0.049
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid biphenyl-2-ylamide hydroxyamide
-
isoform HDAC1, 37C, pH not specified in the publication
0.0014
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide (4-phenylthiazol-2-yl)amide
-
isoform HDAC7, 37C, pH not specified in the publication
0.0015
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide (4-phenylthiazol-2-yl)amide
-
isoform HDAC8, 37C, pH not specified in the publication
0.0026
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide (4-phenylthiazol-2-yl)amide
-
isoform HDAC1, 37C, pH not specified in the publication
0.0054
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide (4-phenylthiazol-2-yl)amide
-
isoform HDAC6, 37C, pH not specified in the publication
0.011
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenyl-amide
-
isoform HDAC6, 37C, pH not specified in the publication; isoform HDAC7, 37C, pH not specified in the publication
0.017
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenyl-amide
-
isoform HDAC8, 37C, pH not specified in the publication
0.029
-
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenyl-amide
-
isoform HDAC1, 37C, pH not specified in the publication
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
-
N-hydroxy-1-methyl-indole-6-carboxamide
-
HDAC8 inhibition
0.0085
-
N-hydroxy-1-methyl-indole-6-carboxamide
-
HDAC1 inhibition
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
-
suberoylanilide hydroxamic acid
-
presence of Co(II), 25C. pH 8.0
0.00013
-
suberoylanilide hydroxamic acid
-
presence of Fe(II), 25C. pH 8.0
0.00025
-
suberoylanilide hydroxamic acid
-
presence of Zn(II), 25C. pH 8.0
0.000504
-
trichostatin A
-
pH and temperature not specified in the publication
0.564
-
Valproic acid
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00088
-
(2E)-3-[1,2-bis(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
0.00041
-
(2E)-3-[1-benzyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
0.0012
-
(2E)-3-[1-benzyl-2-(2-phenylethyl)-1H-benzimidazol-6-yl]-N-hydroxyprop-2-enamide
-
-
0.00022
-
(2E)-3-[1-ethyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
0.000052
-
(2E)-3-[1-[2-(diethylamino)ethyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
0.000041
-
(2E)-3-[1-[3-(dimethylamino)-2,2-dimethylpropyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
0.00019
-
(2E)-3-[1-[3-(dimethylamino)propyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
0.00016
-
(2E)-3-[1-[4-(dimethylamino)butyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
0.0032
-
(2E)-3-[2-cyclohexyl-1-(3-hydroxypropyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
0.00017
-
(2E)-3-[2-[(benzyloxy)methyl]-1-(3-hydroxypropyl)-1H-benzimidazol-5-yl]-N-hydroxyprop-2-enamide
-
-
0.000045
-
(2E)-3-[4-([[2-(3a,7a-dihydro-1H-indol-3-yl)ethyl](2-hydroxyethyl)amino]methyl)phenyl]-N-hydroxyprop-2-enamide
-
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
-
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
-
-
0.0011
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.0017
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(1-methylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.0001
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-methylpropyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00017
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00008
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-phenylpropyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00053
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-octyl-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.0019
-
(2E)-N-hydroxy-3-[1-(3-hydroxypropyl)-2-thiophen-3-yl-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00021
-
(2E)-N-hydroxy-3-[1-(3-methoxypropyl)-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00025
-
(2E)-N-hydroxy-3-[1-(3-morpholin-4-ylpropyl)-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00026
-
(2E)-N-hydroxy-3-[1-methyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00016
-
(2E)-N-hydroxy-3-[1-[3-(1H-imidazol-1-yl)propyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.0002
-
(2E)-N-hydroxy-3-[1-[3-(2-oxopyrrolidin-1-yl)propyl]-2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.000026
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(2-piperidin-1-ylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.000035
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(2-pyrrolidin-1-ylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.000047
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(3,4,5-trimethoxybenzyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00031
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(3-pyrrolidin-1-ylpropyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00025
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(pyridin-2-ylmethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00017
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-propyl-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00017
-
(2E)-N-hydroxy-3-[2-(2-phenylethyl)-1H-benzimidazol-5-yl]prop-2-enamide
-
-
0.00093
-
(2E)-N-hydroxy-3-[2-[(4-methoxyphenyl)sulfonyl]-2,3-dihydro-1H-isoindol-5-yl]prop-2-enamide
-
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
-
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
-
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
-
isoform HDAC1, pH not specified in the publication, temperature not specified in the publication
0.00002
-
(2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide
Q8WUI4
mutant H843Y
0.0043
-
(2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide
Q8WUI4
wild type
4
-
(2S)-2-(acetylamino)-3-[3-[(2S)-2-[[(2S)-2-ammonio-7-(hydroxyamino)-7-oxoheptanoyl]amino]-3-methoxy-3-oxopropyl]phenyl]propanoate
-
isoform HDAC1
8.1
-
(2S)-2-(acetylamino)-3-[3-[(2S)-2-[[(2S)-2-ammonio-7-(hydroxyamino)-7-oxoheptanoyl]amino]-3-methoxy-3-oxopropyl]phenyl]propanoate
-
HeLa cell nuclear extract
0.00014
-
(2S)-8-oxo-2-[(3-piperidin-1-ylpropanoyl)amino]-N-quinolin-3-ylnonanamide
-
HDAC1
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
Q94BN7
-
0.00058
-
(3S,15R,20aS)-15-methyl-3-[(1E)-4-sulfanylbut-1-en-1-yl]-3,4,6,7,14,15,18,19,20,20a-decahydro-1H,5H,16H-11,8:15,12-di(azeno)pyrrolo[2,1-c][1,8,12,4,15]oxadithiadiazacyclooctadecine-1,5,16-trione
Q94BN7
-
0.0008
-
(3S,15R,20aS)-15-methyl-3-[(1E)-4-sulfanylbut-1-en-1-yl]-3,4,6,7,14,15,18,19,20,20a-decahydro-1H,5H,16H-11,8:15,12-di(azeno)pyrrolo[2,1-c][1,8,12,4,15]oxadithiadiazacyclooctadecine-1,5,16-trione
Q94BN7
-
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
Q94BN7
-
0.0003
-
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
-
HDAC1
0.0004
-
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
-
HDAC10; HDAC2; HDAC9
0.0015
-
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
-
HDAC3
0.0028
-
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
-
HDAC5
0.01
-
(3S,6S,10S,14S)-3-(1H-indol-3-ylmethyl)-10-methyl-14-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,11-tetraazacyclotetradecane-2,5,8,12-tetrone
-
HDAC4, larger than 0.010; HDAC6, larger than 0.010; HDAC7, larger than 0.010; HDAC8, larger than 0.010
0.000025
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC9
0.000028
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC10
0.00004
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC2
0.00005
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC1
0.00006
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC5
0.00055
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC3
0.002
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC8
0.01
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9,10-dimethyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC4, larger than 0.010; HDAC6, larger than 0.010; HDAC7, larger than 0.010
0.00002
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC10
0.00003
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC2; HDAC9
0.000035
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC1
0.00007
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC5
0.00015
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC3
0.0022
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC8
0.01
-
(3S,6S,9S,13S)-3-(1H-indol-3-ylmethyl)-9-methyl-13-(2-methylpropyl)-6-(6-oxooctyl)-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetrone
-
HDAC4, larger than 0.010; HDAC6, larger than 0.010; HDAC7, larger than 0.010
0.000012
-
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
-
HDAC1
0.000015
-
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
-
HDAC10
0.000022
-
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
-
HDAC9
0.00004
-
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
-
HDAC2
0.00005
-
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
-
HDAC5
0.00028
-
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
-
HDAC3
0.0015
-
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
-
HDAC8
0.01
-
(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-3-(6-oxooctyl)decahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecine-1,4,7,11(8H)-tetrone
-
HDAC4, larger than 0.010; HDAC6, larger than 0.010; HDAC7, larger than 0.010
0.00027
-
(4E)-N-(2-aminophenyl)-5-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]pent-4-enamide
Q94BN7
-
0.0041
-
(4E)-N-(2-aminophenyl)-5-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]pent-4-enamide
Q94BN7
;
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
Q94BN7
larger than 0.030
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
Q94BN7
larger than 0.030; larger than 0.030; larger than 0.030; larger than 0.030
0.014
-
(5E)-N-(2-aminophenyl)-6-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]hex-5-enamide
Q94BN7
-
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
Q94BN7
-
0.029
-
(5E)-N-(2-aminophenyl)-6-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]hex-5-enamide
Q94BN7
-
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
Q94BN7
larger than 0.030
0.0000012
-
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Q94BN7
-
0.0000034
-
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Q94BN7
-
0.0000035
-
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Q94BN7
-
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
Q94BN7
-
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
Q94BN7
-
0.00000086
-
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3-thia-7,14,20,21-tetraazatricyclo[14.3.1.1-2,5]henicosa-1(20),2(21),16,18-tetraene-6,9,13-trione
Q94BN7
-
0.0000011
-
(5R,8S,11S)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3-thia-7,14,20,21-tetraazatricyclo[14.3.1.1-2,5]henicosa-1(20),2(21),16,18-tetraene-6,9,13-trione
Q94BN7
-
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
Q94BN7
-
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
Q94BN7
-
0.0000038
-
(5R,8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Q94BN7
-
0.0000048
-
(5R,8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Q94BN7
-
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
Q94BN7
-
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
Q94BN7
-
0.0019
-
(5S,8R,11R)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Q94BN7
-
0.0022
-
(5S,8R,11R)-5-methyl-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
Q94BN7
-
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
Q94BN7
-
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]
Q94BN7
-
0.0000015
-
(5S,8S,11S,5'S,8'S,11'S)-11,11'-[disulfanediyldi(1E)but-1-ene-4,1-diyl]bis[5-methyl-8-(1-methylethyl)-3,10,17-trioxa-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione]
Q94BN7
-
0.0000017
-
(5S,8S,11S,5'S,8'S,11'S)-11,11'-[disulfanediyldi(1E)but-1-ene-4,1-diyl]bis[5-methyl-8-(1-methylethyl)-3,10,17-trioxa-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-triene-6,9,13-trione]
Q94BN7
-
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]
Q94BN7
-
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
Q94BN7
-
0.000085
-
(8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),4,16(19)-tetraene-6,9,13-trione
Q94BN7
-
0.00012
-
(8S,11S)-8-(1-methylethyl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),4,16(19)-tetraene-6,9,13-trione
Q94BN7
-
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
Q94BN7
larger than 0.030
0.000035
-
(E)-3-[3-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]phenyl]-N-hydroxyacrylamide
-
recombinant HDAC3, pH not specified in the publication, temperature not specified in the publication
0.000047
-
(E)-3-[3-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]phenyl]-N-hydroxyacrylamide
-
recombinant HDAC1, pH not specified in the publication, temperature not specified in the publication
0.000066
-
(E)-3-[3-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]phenyl]-N-hydroxyacrylamide
-
recombinant HDAC6, pH not specified in the publication, temperature not specified in the publication
0.000086
-
(E)-3-[3-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]phenyl]-N-hydroxyacrylamide
-
recombinant HDAC8, pH not specified in the publication, temperature not specified in the publication
0.00016
-
(E)-N1-hydroxy-N5-(5-styryl-1,3,4-thiadiazol-2-yl)glutaramide
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37C, pH not specified in the publication
0.00557
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-(4-methoxyphenyl)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00106
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-(naphthalen-1-yl)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00362
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-m-tolyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00413
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-o-tolyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00382
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-p-tolyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00354
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-pentyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00407
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-phenethyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00821
-
(S)-7-(2-(hydroxyamino)-2-oxoethoxy)-N-phenyl-1,2,3,4-tetrahydroisoquinoline-3-carboxamide hydrochloride
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.05
-
(S)-benzyl 3-(biphenyl-4-ylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
IC50 above 0.05 mM, in 15 mM Tris-HCl, pH 8.0, at 37C
0.00058
-
(S)-benzyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenethylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.05
-
(S)-benzyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
IC50 above 0.05 mM, in 15 mM Tris-HCl, pH 8.0, at 37C
0.00339
-
(S)-N-(2,4-dimethylphenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00334
-
(S)-N-(3-chloro-4-fluorophenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.0032
-
(S)-N-(3-chlorophenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00323
-
(S)-N-(4-fluorophenyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00221
-
(S)-N-(biphenyl-4-yl)-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.0051
-
(S)-N-benzyl-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide hydrochloride
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00577
-
(S)-N-hexyl-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.01217
-
(S)-N-tert -butyl-7-(2-(hydroxyamino)-2-oxoethoxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00378
-
(S)-tert-butyl 3-(2,4-dimethylphenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00155
-
(S)-tert-butyl 3-(3-chloro-4-fluorophenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00117
-
(S)-tert-butyl 3-(3-chlorophenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00256
-
(S)-tert-butyl 3-(4-fluorophenylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00341
-
(S)-tert-butyl 3-(benzylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00198
-
(S)-tert-butyl 3-(biphenyl-4-ylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00442
-
(S)-tert-butyl 3-(hexylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00458
-
(S)-tert-butyl 3-(tert-butylcarbamoyl)-7-(2-(hydroxyamino)-2-oxoethoxy)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.001
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(4-methoxyphenylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00177
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(mtolylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00425
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(naphthalen-1-ylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.004
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(o-tolylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00165
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(p-tolylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00302
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(pentylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00267
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenethylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.00129
-
(S)-tert-butyl 7-(2-(hydroxyamino)-2-oxoethoxy)-3-(phenylcarbamoyl)-3,4-dihydroisoquinoline-2(1H)-carboxylate
-
in 15 mM Tris-HCl, pH 8.0, at 37C
0.000055
-
1-methyl-N-[(1S)-7-oxo-1-[(4-phenyl-1,3-thiazol-2-yl)carbamoyl]octyl]piperidine-2-carboxamide
-
HDAC1
0.000037
-
1-[5-(2,3-dihydro-1,4-benzodioxin-6-yl)thiophen-2-yl]-2,2,2-trifluoroethanone
-
HDAC6, pH and temperature not specified in the publication
0.01
-
1-[5-(2,3-dihydro-1,4-benzodioxin-6-yl)thiophen-2-yl]-2,2,2-trifluoroethanone
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication; IC50 above 0.01 mM, HDAC4, pH and temperature not specified in the publication
0.000029
-
1-[5-(4-acetylphenyl)thiophen-2-yl]-2,2,2-trifluoroethanone
-
HDAC6, pH and temperature not specified in the publication
0.01
-
1-[5-(4-acetylphenyl)thiophen-2-yl]-2,2,2-trifluoroethanone
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication
0.072
-
1-[5-(4-acetylphenyl)thiophen-2-yl]-2,2,2-trifluoroethanone
-
HDAC4, pH and temperature not specified in the publication
0.098
-
15-deoxy-DELTA12,14-prostaglandin J2-biotin
-
recombinant HDAC3 in complex with CoR1, pH and temperature not specified in the publication
0.00013
-
2,2,2-trifluoro-1-(2-phenyl-1,3-thiazol-5-yl)ethanone
-
HDAC4, pH and temperature not specified in the publication
0.00021
-
2,2,2-trifluoro-1-(2-phenyl-1,3-thiazol-5-yl)ethanone
-
HDAC6 pH and temperature not specified in the publication
0.0037
-
2,2,2-trifluoro-1-(2-phenyl-1,3-thiazol-5-yl)ethanone
-
HDAC1, pH and temperature not specified in the publication
0.0019
-
2,2,2-trifluoro-1-(4-phenylthiophen-2-yl)ethanone
-
HDAC6, pH and temperature not specified in the publication
0.0032
-
2,2,2-trifluoro-1-(4-phenylthiophen-2-yl)ethanone
-
HDAC4, pH and temperature not specified in the publication
0.01
-
2,2,2-trifluoro-1-(4-phenylthiophen-2-yl)ethanone
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication
0.00017
-
2,2,2-trifluoro-1-(5-phenylthiophen-2-yl)ethanone
-
HDAC6, pH and temperature not specified in the publication
0.0028
-
2,2,2-trifluoro-1-(5-phenylthiophen-2-yl)ethanone
-
HDAC4, pH and temperature not specified in the publication
0.02
-
2,2,2-trifluoro-1-(5-phenylthiophen-2-yl)ethanone
-
IC50 above 0.02 mM, HDAC1, pH and temperature not specified in the publication
0.000024
-
2,2,2-trifluoro-1-(5-[3-[(methylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
HDAC4, pH and temperature not specified in the publication
0.00023
-
2,2,2-trifluoro-1-(5-[3-[(methylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
HDAC6, pH and temperature not specified in the publication
0.0027
-
2,2,2-trifluoro-1-(5-[3-[(methylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
HDAC1, pH and temperature not specified in the publication
0.00003
-
2,2,2-trifluoro-1-(5-[3-[(propylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
HDAC4, pH and temperature not specified in the publication
0.00024
-
2,2,2-trifluoro-1-(5-[3-[(propylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
HDAC6, pH and temperature not specified in the publication
0.0022
-
2,2,2-trifluoro-1-(5-[3-[(propylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
HDAC1, pH and temperature not specified in the publication
0.000035
-
2,2,2-trifluoro-1-(5-[3-[(thiophen-2-ylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
HDAC4, pH and temperature not specified in the publication
0.00052
-
2,2,2-trifluoro-1-(5-[3-[(thiophen-2-ylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
HDAC6, pH and temperature not specified in the publication
0.0039
-
2,2,2-trifluoro-1-(5-[3-[(thiophen-2-ylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl]thiophen-2-yl)ethanone
-
HDAC1, pH and temperature not specified in the publication
0.005
-
2,2,2-trifluoro-1-[5-(1H-indol-5-yl)thiophen-2-yl]ethanone
-
IC50 above 0.005 mM, HDAC6, pH and temperature not specified in the publication
0.01
-
2,2,2-trifluoro-1-[5-(1H-indol-5-yl)thiophen-2-yl]ethanone
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication; IC50 above 0.01 mM, HDAC4, pH and temperature not specified in the publication
0.0063
-
2,2,2-trifluoro-1-[5-(2-methoxyphenyl)thiophen-2-yl]ethanone
-
HDAC6, pH and temperature not specified in the publication
0.01
-
2,2,2-trifluoro-1-[5-(2-methoxyphenyl)thiophen-2-yl]ethanone
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication; IC50 above 0.01 mM, HDAC4, pH and temperature not specified in the publication
0.0031
-
2,2,2-trifluoro-1-[5-(3-methoxyphenyl)thiophen-2-yl]ethanone
-
HDAC6, pH and temperature not specified in the publication
0.0038
-
2,2,2-trifluoro-1-[5-(3-methoxyphenyl)thiophen-2-yl]ethanone
-
HDAC4, pH and temperature not specified in the publication
0.01
-
2,2,2-trifluoro-1-[5-(3-methoxyphenyl)thiophen-2-yl]ethanone
-
IC50 above 0.01 mM, HDAC1, pH and temperature not specified in the publication
0.00006
-
2,2,2-trifluoro-1-[5-(3-[[(4-fluorobenzyl)sulfonyl]methyl]-1,2,4-oxadiazol-5-yl)thiophen-2-yl]ethanone
-
HDAC4, pH and temperature not specified in the publication
0.0007
-
2,2,2-trifluoro-1-[5-(3-[[(4-fluorobenzyl)sulfonyl]methyl]-1,2,4-oxadiazol-5-yl)thiophen-2-yl]ethanone
-
HDAC6, pH and temperature not specified in the publication
0.0066
-
2,2,2-trifluoro-1-[5-(3-[[(4-fluorobenzyl)sulfonyl]methyl]-1,2,4-oxadiazol-5-yl)thiophen-2-yl]ethanone
-
HDAC1, pH and temperature not specified in the publication
0.00011
-
2,2,2-trifluoro-1-[5-(4-methoxyphenyl)thiophen-2-yl]ethanone
-
HDAC4, pH and temperature not specified in the publication
0.001
-
2,2,2-trifluoro-1-[5-(4-methoxyphenyl)thiophen-2-yl]ethanone
-
IC50 above 0.001 mM, HDAC1, pH and temperature not specified in the publication; IC50 above 0.001 mM, HDAC6, pH and temperature not specified in the publication
0.00054
-
2,2,2-trifluoro-1-[5-(pyridin-2-yl)thiophen-2-yl]ethanone
-
HDAC4, pH and temperature not specified in the publication
0.001
-
2,2,2-trifluoro-1-[5-(pyridin-2-yl)thiophen-2-yl]ethanone
-
IC50 above 0.001 mM, HDAC1, pH and temperature not specified in the publication; IC50 above 0.001 mM, HDAC6, pH and temperature not specified in the publication
0.000015
-
2,2,2-trifluoro-1-[5-(quinoxalin-6-yl)thiophen-2-yl]ethanone
-
HDAC6, pH and temperature not specified in the publication
0.00016
-
2,2,2-trifluoro-1-[5-(quinoxalin-6-yl)thiophen-2-yl]ethanone
-
HDAC4, pH and temperature not specified in the publication
0.00091
-
2,2,2-trifluoro-1-[5-(quinoxalin-6-yl)thiophen-2-yl]ethanone
-
HDAC1, pH and temperature not specified in the publication
0.000026
-
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide
-
HDAC1
0.000048
-
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide
-
HDAC3
0.000059
-
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide
-
HDAC2
0.01
-
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide
-
HDAC5, larger than 0.010; HDAC7, larger than 0.010
0.000059
-
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
-
HDAC1
0.00011
-
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
-
HDAC2
0.00012
-
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
-
HDAC3
0.00034
-
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
-
HDAC6
0.005
-
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
-
HDAC8, larger than 0.005
0.01
-
2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide
-
HDAC5, larger than 0.010; HDAC7, larger than 0.010
0.198
-
2-[(methylsulfonyl)sulfanyl]ethanaminium bromide
-
-
0.0096
-
2-[(methylsulfonyl)sulfanyl]ethyl 2-propylpentanoate
-
-
0.00007
-
3-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
-
HDAC6, pH and temperature not specified in the publication
0.00031
-
3-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
-
HDAC4, pH and temperature not specified in the publication
0.0128
-
3-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
-
HDAC1, pH and temperature not specified in the publication
0.0023
-
3-[5-[(1E)-3-(hydroxyamino)-3-oxoprop-1-en-1-yl]-2-(2-phenylethyl)-1H-benzimidazol-1-yl]propanoic acid
-
-
0.00023
-
3-[5-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]furan-2-yl]-N-hydroxy-acrylamide
-
recombinant HDAC8, pH not specified in the publication, temperature not specified in the publication
0.00061
-
3-[5-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]furan-2-yl]-N-hydroxy-acrylamide
-
recombinant HDAC3, pH not specified in the publication, temperature not specified in the publication
0.00063
-
3-[5-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]furan-2-yl]-N-hydroxy-acrylamide
-
recombinant HDAC1, pH not specified in the publication, temperature not specified in the publication
0.0063
-
3-[5-[4-(3-chloro-4-(3-fluorobenzyloxy)phenylamino)quinazolin-6-yl]furan-2-yl]-N-hydroxy-acrylamide
-
recombinant HDAC6, pH not specified in the publication, temperature not specified in the publication
0.0564
-
4-(3-thioxo-3H-1,2-dithiol-5-yl)phenyl 2-propylpentanoate
-
-
0.133
-
4-benzoylbutyric hydroxamic acid
-
-
0.14
-
4-hydroxy-2-nonenal
-
recombinant HDAC3 in complex with CoR1, pH and temperature not specified in the publication
0.000027
-
4-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
-
HDAC6, pH and temperature not specified in the publication
0.0025
-
4-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
-
HDAC1, pH and temperature not specified in the publication
0.074
-
4-[5-(trifluoroacetyl)thiophen-2-yl]benzoic acid
-
HDAC4, pH and temperature not specified in the publication
0.000041
-
4-[5-(trifluoroacetyl)thiophen-2-yl]benzonitrile
-
HDAC6, pH and temperature not specified in the publication
0.00016
-
4-[5-(trifluoroacetyl)thiophen-2-yl]benzonitrile
-
HDAC4, pH and temperature not specified in the publication
0.0027
-
4-[5-(trifluoroacetyl)thiophen-2-yl]benzonitrile
-
HDAC1, pH and temperature not specified in the publication
0.04316
-
4-[[(2E)-2-(4-chlorobenzylidene)hydrazinyl]carbonothioyl]-N-hydroxypiperazine-1-carboxamide
-
pH and temperature not specified in the publication
0.00045
-
5-(4-hydroxyphenyl)-3H-1,2-dithiol-3-thione
-
ADTOH
0.005
-
5-phenylvaleric hydroxamic acid
-
-
0.00037
-
6-mercapto-N-phenylhexanamide
-
37C
0.00039
-
6-[(1-(mercaptomethyl)vinyl)amino]-N-phenylhexanamide
-
37C
0.000059
-
6-[(2E)-2-[(2-bromo-4-hydroxy-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
Q7K6A1
-
0.000106
-
6-[(2E)-2-[(2-bromo-4-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
Q7K6A1
-
0.000089
-
6-[(2E)-2-[(2-bromo-5-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-6-oxohexanamide
Q7K6A1
-
0.0001
-
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
-
HDAC1
0.0002
-
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
-
HDAC2
0.00028
-
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
-
HDAC10
0.00055
-
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
-
HDAC9
0.0006
-
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
-
HDAC3
0.0007
-
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
-
HDAC5
0.0023
-
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
-
HDAC6; HDAC8
0.01
-
6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanoic acid
-
HDAC4, larger than 0.010; HDAC7, larger than 0.010
0.00007
-
6-[(9H-fluoren-3-ylmethyl)(3-phenoxybenzyl)amino]-N-hydroxyhexanamide
-
HDAC activity in HeLa nuclear cell extracts, 25C, pH 8.0
0.00017
-
6-[(biphenyl-4-ylmethyl)[4-[(4-bromobenzyl)oxy]benzyl]amino]-N-hydroxyhexanamide
-
HDAC activity in HeLa nuclear cell extracts, 25C, pH 8.0
0.0003159
-
6-[4-(2,6-dimethoxyphenyl)-1H-1,2,3-triazol-1-yl]-N-hydroxyhexanamide
-
-
0.0001626
-
6-[4-(biphenyl-2-yl)-1H-1,2,3-triazol-1-yl]-N-hydroxyhexanamide
-
-
0.0000019
-
6-[4-(biphenyl-3-yl)-1H-1,2,3-triazol-1-yl]-N-hydroxyhexanamide
-
-
0.0000524
-
6-[4-(biphenyl-4-yl)-1H-1,2,3-triazol-1-yl]-N-hydroxyhexanamide
-
-
0.00018
-
6-[[4-[(4-bromobenzyl)oxy]benzyl](9H-fluoren-3-ylmethyl)amino]-N-hydroxyhexanamide
-
HDAC activity in HeLa nuclear cell extracts, 25C, pH 8.0
0.0000043
-
6-{4-[4-(dimethylamino)phenyl]-1H-1,2,3-triazol-1-yl}-N-hydroxyhexanamide
-
-
0.00017
-
7-mercapto-N-(2-phenyl-1,3-thiazol-5-yl)heptanamide
-
37C
0.00021
-
7-mercapto-N-(3-phenoxyphenyl)heptanamide
-
37C
0.00021
-
7-mercapto-N-phenylheptanamide
-
37C
0.00011
-
7-mercapto-N-pyridin-3-ylheptanamide
-
37C
0.000072
-
7-mercapto-N-quinolin-3-ylheptanamide
-
37C
0.000059
-
7-[(2E)-2-[(2-bromo-4-hydroxy-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
0.000049
-
7-[(2E)-2-[(2-bromo-5-hydroxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
0.000022
-
7-[(2E)-2-[(2-bromo-5-methoxyphenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
0.000037
-
7-[(2E)-2-[(2-bromophenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
0.000036
-
7-[(2E)-2-[(2-bromopyridin-3-yl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
0.00009
-
7-[(2E)-2-[(2-chlorophenyl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
0.00002
-
7-[(2E)-2-[(6-bromo-1,3-benzodioxol-5-yl)methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
0.000037
-
7-[(2E)-2-[[4-(dimethylamino)-2-hydroxyphenyl]methylidene]hydrazino]-N-hydroxy-7-oxoheptanamide
Q7K6A1
-
0.0000054
-
7-[4-(biphenyl-3-yl)-1H-1,2,3-triazol-1-yl]-N-hydroxyheptanamide
-
-
0.0001061
-
7-{4-[4-(dimethylamino)phenyl]-1H-1,2,3-triazol-1-yl}-N-hydroxyheptanamide
-
-
0.00011
-
8-[(2E)-2-[(2,5-dihydroxyphenyl)methylidene]hydrazino]-N-hydroxy-8-oxooctanamide
Q7K6A1
-
0.0000007
-
apicidin
Q9BY41
isoform HDAC3
0.000001
-
apicidin
Q7K6A1
-
0.000002
-
apicidin
Q9BY41
isoform HDAC1
0.000015
-
apicidin
-
HDAC9
0.000018
-
apicidin
-
HDAC1
0.00003
-
apicidin
-
HDAC10
0.000035
-
apicidin
-
HDAC2
0.000044
-
apicidin
-
HDAC1
0.00008
-
apicidin
-
HDAC5
0.0001
-
apicidin
-
HDAC3
0.00075
-
apicidin
-
HDAC8
0.001
-
apicidin
Q9BY41
isoform HDAC8
0.01
-
apicidin
-
HDAC4, larger than 0.010; HDAC6, larger than 0.010; HDAC7, larger than 0.010
0.02
-
beta-methylselenopyruvate
-
HDAC8, at 37C, pH not specified in the publication
0.021
-
Butyrate
-
isoform HD2
0.045
-
Butyrate
-
isoform HD1
0.08
-
Butyrate
-
nuclear matrix form of enzyme
0.35
-
Butyrate
-
pH 8.0
2.54
-
caffeic acid
-
pH and temperature not specified in the publication
0.375
-
chlorogenic acid
-
pH and temperature not specified in the publication
0.115
-
curcumin
-
pH and temperature not specified in the publication
0.0036
-
LAQ824
Q8WUI4
mutant H843Y
0.553
-
LAQ824
Q8WUI4
wild type
0.0000018
-
LBH-589
Q7K6A1
-
0.00013
-
LBH589
Q8WUI4
mutant H843Y
0.0154
-
LBH589
Q8WUI4
wild type
0.000046
-
methyl (3R,6R,9R)-9-(acetylamino)-6-[6-(hydroxyamino)-6-oxohexyl]-5,8-dioxo-4,7-diazabicyclo[9.3.1]pentadeca-1(15),11,13-triene-3-carboxylate
-
HeLa cell nuclear extract
0.000057
-
methyl (3R,6R,9R)-9-(acetylamino)-6-[6-(hydroxyamino)-6-oxohexyl]-5,8-dioxo-4,7-diazabicyclo[9.3.1]pentadeca-1(15),11,13-triene-3-carboxylate
-
isoform HDAC1
0.231
-
methyl (3R,6R,9R)-9-(acetylamino)-6-[6-(hydroxyamino)-6-oxohexyl]-5,8-dioxo-4,7-diazabicyclo[9.3.1]pentadeca-1(15),11,13-triene-3-carboxylate
-
isoform HDAC8
0.000167
-
methyl N-[(2S)-2-[(N-acetyl-L-alanyl)amino]-7-(hydroxyamino)-7-oxoheptanoyl]-L-phenylalaninate
-
HeLa cell nuclear extract
0.000174
-
methyl N-[(2S)-2-[(N-acetyl-L-alanyl)amino]-7-(hydroxyamino)-7-oxoheptanoyl]-L-phenylalaninate
-
isoform HDAC1
0.000045
-
MS-275
Q94BN7
-
0.00012
-
MS-275
-
HDAC1
0.00013
-
MS-275
Q94BN7
-
0.00017
-
MS-275
Q94BN7
-
0.00025
-
MS-275
-
HDAC2
0.0004
-
MS-275
-
HDAC3
0.00094
-
MS-275
Q7K6A1
-
0.01
-
MS-275
-
HDAC5, larger than 0.010; HDAC6, larger than 0.010; HDAC7, larger than 0.010; HDAC8, larger than 0.010
0.03
-
MS-275
Q94BN7
larger than 0.030
0.000079
-
N-(6-mercaptohexyl)-1-benzofuran-2-carboxamide
-
37C
0.0001
-
N-(6-mercaptohexyl)-1H-indole-2-carboxamide
-
37C
0.000085
-
N-(6-mercaptohexyl)-2-naphthamide
-
37C
0.00036
-
N-(6-mercaptohexyl)benzamide
-
37C
0.000075
-
N-biphenyl-3-yl-7-mercaptoheptanamide
-
37C
0.0033
-
N-hydroxy-1-(3-hydroxypropyl)-2-(2-phenylethyl)-1H-benzimidazole-5-carboxamide
-
-
0.0013
-
N-hydroxy-2-[1-methyl-2-(2-phenylethyl)-1H-benzimidazol-5-yl]cyclopropanecarboxamide
-
-
0.01
-
N-hydroxy-3-[1-(3-hydroxypropyl)-2-(2-methylpropyl)-1H-benzimidazol-5-yl]propanamide
-
larger than 0.010
0.00017
-
N-hydroxy-3-[2-(2-phenylethyl)-1-(3,4,5-trimethoxybenzyl)-1H-benzimidazol-5-yl]propanamide
-
-
0.00002
-
N-hydroxy-3-[2-[(2-methyl-1H-indol-3-yl)acetyl]-2,3-dihydro-1H-isoindol-5-yl]propanamide
-
isoform HDAC1, pH not specified in the publication, temperature not specified in the publication
0.000044
-
N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
Q9BY41
isoform HDAC3
0.000086
-
N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
Q9BY41
isoform HDAC1
0.000175
-
N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
Q9BY41
isoform HDAC8
0.03367
-
N-hydroxy-4-[[(2E)-2-(2-hydroxybenzylidene)hydrazinyl]carbonothioyl]piperazine-1-carboxamide
-
pH and temperature not specified in the publication
0.00011
-
N-hydroxy-5-(4-phenyl-1H-1,2,3-triazol-1-yl)pentanamide
-
-
0.0000142
-
N-hydroxy-6-(4-phenyl-1H-1,2,3-triazol-1-yl)hexanamide
-
-
0.0000002
-
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
-
HDAC10
0.0000006
-
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
-
HDAC9
0.0000015
-
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
-
HDAC1
0.0000025
-
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
-
HDAC5
0.000005
-
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
-
HDAC2
0.000025
-
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
-
HDAC3
0.00003
-
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
-
HDAC6
0.00012
-
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
-
HDAC8
0.01
-
N-hydroxy-6-[(2S,5S,8S,11S)-8-(1H-indol-3-ylmethyl)-2-methyl-11-(2-methylpropyl)-3,6,9,13-tetraoxo-1,4,7,10-tetraazacyclotridecan-5-yl]hexanamide
-
HDAC4, larger than 0.010; HDAC7, larger than 0.010
0.0000006
-
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
-
HDAC1
0.0000035
-
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
-
HDAC2
0.000035
-
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
-
HDAC3; HDAC6
0.00018
-
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
-
HDAC8
0.01
-
N-hydroxy-6-[(3S,6S,9S,15aS)-6-(1H-indol-3-ylmethyl)-9-(2-methylpropyl)-1,4,7,11-tetraoxotetradecahydro-1H-pyrrolo[1,2-a][1,4,7,10]tetraazacyclotridecin-3-yl]hexanamide
-
HDAC4, larger than 0.010; HDAC7, larger than 0.010
0.000076
-
N-hydroxy-6-[4-(2-methoxyphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
0.0000139
-
N-hydroxy-6-[4-(3-methoxyphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
0.0000174
-
N-hydroxy-6-[4-(3-methylphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
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
-
-
0.0000434
-
N-hydroxy-6-[4-(4-methylphenyl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
0.0000018
-
N-hydroxy-6-[4-(6-methoxynaphthalen-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
0.0000676
-
N-hydroxy-6-[4-(pyridin-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
0.0002872
-
N-hydroxy-6-[4-(pyridin-3-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
0.0001125
-
N-hydroxy-6-[4-(pyridin-4-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
0.0000021
-
N-hydroxy-6-[4-(quinolin-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
0.0001515
-
N-hydroxy-6-[4-(quinolin-7-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
0.0000317
-
N-hydroxy-6-[4-(thiophen-2-yl)-1H-1,2,3-triazol-1-yl]hexanamide
-
-
0.0000023
-
N-hydroxy-6-{4-[4-(pyridin-4-yl)phenyl]-1H-1,2,3-triazol-1-yl}hexanamide
-
-
0.0000096
-
N-hydroxy-7-(4-phenyl-1H-1,2,3-triazol-1-yl)heptanamide
-
-
0.000041
-
N-hydroxy-7-[(2E)-2-[(2-hydroxynaphthalen-1-yl)methylidene]hydrazino]-7-oxoheptanamide
Q7K6A1
-
0.000059
-
N-hydroxy-7-[(2E)-2-[(3-hydroxyphenyl)methylidene]hydrazino]-7-oxoheptanamide
Q7K6A1
-
0.000015
-
N-hydroxy-7-[(2E)-2-[[4-(1H-imidazol-1-yl)phenyl]methylidene]hydrazino]-7-oxoheptanamide
Q7K6A1
-
0.0000153
-
N-hydroxy-7-[4-(6-methoxynaphthalen-2-yl)-1H-1,2,3-triazol-1-yl]heptanamide
-
-
0.0000239
-
N-hydroxy-7-[4-(pyridin-2-yl)-1H-1,2,3-triazol-1-yl]heptanamide
-
-
0.0000166
-
N-hydroxy-7-{4-[4-(pyridin-4-yl)phenyl]-1H-1,2,3-triazol-1-yl}heptanamide
-
-
0.000043
-
N-hydroxy-8-oxo-8-[(2E)-2-[(2,4,6-trihydroxyphenyl)methylidene]hydrazino]octanamide
Q7K6A1
-
0.000089
-
N-methyl-N-(quinoxalin-6-ylmethyl)-5-(trifluoroacetyl)thiophene-2-carboxamide
-
HDAC6, pH and temperature not specified in the publication
0.000098
-
N-methyl-N-(quinoxalin-6-ylmethyl)-5-(trifluoroacetyl)thiophene-2-carboxamide
-
HDAC4, pH and temperature not specified in the publication
0.00058
-
N-methyl-N-(quinoxalin-6-ylmethyl)-5-(trifluoroacetyl)thiophene-2-carboxamide
-
HDAC1, pH and temperature not specified in the publication
0.00067
-
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
-
HDAC1
0.00088
-
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
-
HDAC2
0.00097
-
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
-
HDAC6
0.001
-
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
-
HDAC3
0.01
-
N-[(1S)-1-(6-chloro-1H-benzimidazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide
-
HDAC5, larger than 0.010; HDAC7, larger than 0.010; HDAC8, larger than 0.010
0.00067
-
N-[(2E)-3-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]prop-2-en-1-yl]-2-sulfanylacetamide
Q94BN7
-
0.0007
-
N-[(2E)-3-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]prop-2-en-1-yl]-2-sulfanylacetamide
Q94BN7
-
0.00096
-
N-[(2E)-3-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]prop-2-en-1-yl]-2-sulfanylacetamide
Q94BN7
-
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
Q94BN7
-
0.00024
-
N-[(3E)-4-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]but-3-en-1-yl]-2-sulfanylacetamide
Q94BN7
-
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
Q94BN7
-
0.0015
-
N-[(3E)-4-[(5R,8S,11S)-5-methyl-8-(1-methylethyl)-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1-2,5]icosa-1(18),2(20),16(19)-trien-11-yl]but-3-en-1-yl]-2-sulfanylacetamide
Q94BN7
-
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
Q94BN7
-
0.00022
-
N1-(5-benzyl-1,3,4-thiadiazol-2-yl)-N7-hydroxyheptanediamide
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37C, pH not specified in the publication
0.00026
-
N1-(5-benzyl-1,3,4-thiadiazol-2-yl)-N8-hydroxyoctanediamide
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37C, pH not specified in the publication
0.000089
-
N1-hydroxy-N7-(5-phenyl-1,3,4-thiadiazol-2-yl)heptanediamide
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37C, pH not specified in the publication
0.00027
-
N1-hydroxy-N8-(5-phenyl-1,3,4-thiadiazol-2-yl)octanediamide
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37C, pH not specified in the publication
0.00034
-
N1-methyl-2-oxo-N9-phenylnonanediamide
-
37C
0.0026
-
oxamflatin
Q8WUI4
mutant H843Y
0.098
-
oxamflatin
Q8WUI4
wild type
0.000185
-
pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
Q9BY41
isoform HDAC1
0.000201
-
pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
Q9BY41
isoform HDAC3
0.01
-
pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
Q9BY41
isoform HDAC8
0.102
-
S-(2-hydroxyethyl) methanesulfonothioate
-
-
0.0175
-
S-[2-[(2-propylpentanoyl)amino]ethyl]methanesulfonothioate
-
-
0.013
-
sodium butyrate
-
recombinant HDAC3 in complex with CoR1, pH and temperature not specified in the publication
0.01
-
splitomicin
Q7K6A1
larger than 0.01
0.00001
-
suberoylanilide hydroxamic acid
Q94BN7
-
0.000013
-
suberoylanilide hydroxamic acid
Q94BN7
-
0.000017
-
suberoylanilide hydroxamic acid
Q94BN7
-
0.000026
-
suberoylanilide hydroxamic acid
Q94BN7
-
0.000059
-
suberoylanilide hydroxamic acid
Q7K6A1
-
0.000065
-
suberoylanilide hydroxamic acid
-
-
0.000106
-
suberoylanilide hydroxamic acid
Q9BY41
isoform HDAC3
0.00011
-
suberoylanilide hydroxamic acid
-
HeLa cell nuclear extract
0.000112
-
suberoylanilide hydroxamic acid
-
isoform HDAC1
0.000119
-
suberoylanilide hydroxamic acid
Q9BY41
isoform HDAC1
0.00015
-
suberoylanilide hydroxamic acid
-
HDAC from HeLa cell nucleus extracts, mainly including HDAC1 and HDAC2, 37C, pH not specified in the publication
0.00027
-
suberoylanilide hydroxamic acid
-
isoform HDAC8
0.00028
-
suberoylanilide hydroxamic acid
-
37C
0.0003
-
suberoylanilide hydroxamic acid
Q8WUI4
mutant H843Y
0.004
-
suberoylanilide hydroxamic acid
Q9BY41
isoform HDAC8
0.113
-
suberoylanilide hydroxamic acid
Q8WUI4
wild type
0.0000006
-
trichostatin A
Q9BY41
isoform HDAC3
0.0000006
-
trichostatin A
Q7K6A1
-
0.0000015
-
trichostatin A
Q9BY41
isoform HDAC1
0.000003
-
trichostatin A
-
pH 8.0
0.000005
-
trichostatin A
-
-
0.000022
-
trichostatin A
-
HDAC activity in HeLa nuclear cell extracts, 25C, pH 8.0
0.00004
-
trichostatin A
-
isoform HDAC8
0.00004
-
trichostatin A
Q8WUI4
mutant H843Y
0.000041
-
trichostatin A
-
HeLa cell nuclear extract
0.00006
-
trichostatin A
-
isoform HDAC1
0.0003
-
trichostatin A
Q8WUI4
wild type
0.00049
-
trichostatin A
Q9BY41
isoform HDAC8
0.008
-
trichostatin A
-
recombinant HDAC3 in complex with CoR1, pH and temperature not specified in the publication
0.0008
-
tubacin
Q8WUI4
mutant H843Y
0.225
-
tubacin
Q8WUI4
wild type
0.4
-
Valproic acid
-
isoform HDAC1, pH 8.0, 37C
0.995
-
Valproic acid
-
-
0.00003
-
vorinostat
-
HDAC1
0.000043
-
vorinostat
-
HDAC6
0.000057
-
vorinostat
-
HDAC3
0.000082
-
vorinostat
-
HDAC2
0.0017
-
vorinostat
-
HDAC8
0.01
-
vorinostat
-
HDAC7, larger than 0.010
0.000045
-
[4-[(E)-[[6-(hydroxyamino)-6-oxohexanoyl]hydrazono]methyl]phenyl]boronic acid
Q7K6A1
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7
-
isoform HD2
7
7.5
-
nuclear matrix form of enzyme
7.5
-
-
isoform HD1
7.5
-
P56517
-
8
-
-
activity assay
8.1
-
-
activity assay
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
activity assay at room temperature
25
-
-
in vitro tubulin deacetylation assay
25
-
-
activity assay
30
-
-
activity assay
37
-
-
activity assay
37
-
Q803C3
activity assay
37
-
-
activity assay
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.3
-
P56517
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
prostate epithelial cell
Manually annotated by BRENDA team
-
atlas on distribution of eleven histone deacetylase isoforms in the brain
Manually annotated by BRENDA team
Q9UKV0
high-level expression
Manually annotated by BRENDA team
Q9ZTP8
expression levels of enzyme isoforms differ during early embryo germination
Manually annotated by BRENDA team
-
primary erythroid progenitor cell
Manually annotated by BRENDA team
-
immature flower
Manually annotated by BRENDA team
Q7K6A1
expressed in gametocytes and mature blood stages of the malaria parasite life cycle
Manually annotated by BRENDA team
-
nuclear extract rich in histine deacetylase activity
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
first leaves of seedlings
Manually annotated by BRENDA team
-
in liver, class IIa HDACs HDAC4, 5, and 7, are phosphorylated and excluded from the nucleus by AMPK family kinases. In response to the fasting hormone glucagon, these HDACs are rapidly dephosphorylated and translocated to the nucleus where they associate with the promoters of gluconeogenic enzymes such as G6Pase. In turn, HDAC4/5 recruit HDAC3, which results in the acute transcriptional induction of these genes via deacetylation and activation of FOXO family transcription factors. Loss of class IIa HDACs in murine liver results in inhibition of FOXO target genes and lowers blood glucose, resulting in increased glycogen storage
Manually annotated by BRENDA team
-
prostate epithelial cell
Manually annotated by BRENDA team
-
body-wall muscle cell
Manually annotated by BRENDA team
-
prostate epithelial cell
Manually annotated by BRENDA team
P56524
prominent expression
Manually annotated by BRENDA team
Q9UKV0
high-level expression
Manually annotated by BRENDA team
P56524
highest expression observed
Manually annotated by BRENDA team
P56524
prominent expression
Manually annotated by BRENDA team
P56524
prominent expression
Manually annotated by BRENDA team
additional information
P56524
expression in all tisuues tested
Manually annotated by BRENDA team
additional information
-
isoform HDAC10 is expressed in most of the cancer cells examined
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enrichment of enzyme is cytoplasm is not sensitive to leptomycin B
Manually annotated by BRENDA team
Q8WUI4
shuttling of isoform HDAC7 between cytoplasm and nucleus. Catalytic activity of HDAC7 requires interaction with isoform HDAC3 in the nucleus
Manually annotated by BRENDA team
-
depending on phosphorylation status
Manually annotated by BRENDA team
P56524
part of multiprotein complex in the nucleus
Manually annotated by BRENDA team
Q8WUI4
predominant localization of isoform HDAC7, which shuttles between cytoplasm and nucleus. Catalytic activity of HDAC7 requires interaction with isoform HDAC3 in the nucleus
Manually annotated by BRENDA team
O22446
presumably localized to euchromatic regions
Manually annotated by BRENDA team
-
depending on phosphorylation status
Manually annotated by BRENDA team
-
mitotic spindle
Manually annotated by BRENDA team
-
cytoplasmic expression of HDAC1, 2 and 3 is significantly increased in carcinomas compared with benign tumors
Manually annotated by BRENDA team
additional information
O22446
isoform AtHD1 is excluded from the nucleolus
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
51000
-
Q7K6A1
-
55000
-
-
isoform HD1, gel filtration
60000
-
Q9ZTP8
gel filtration, enzyme complex including Rbap protein
65000
-
-
determined by SDS-PAGE and Western Blot analysis
72000
-
P56517
gel filtration
114000
-
-
truncated isoform of the HDAC6p114 protein, SDS-PAGE
120000
-
Q9ZTP8
gel filtration, enzyme complex including Rbap protein
131000
-
-
HDAC6p131, major isoform of histone deacetlyase 6, SDS-PAGE
220000
-
-
isoform HD2, gel filtration
220000
-
P56524
sucrose gradient
400000
500000
Q7Z8L7, Q7Z8L9
gel filtration, enzyme is part of a high molecular weight complex
400000
-
-
enzyme complex solubilized from nuclear matrix, gel filtration
500000
-
Q9ZTP8
gel filtration, enzyme complex including Rbap protein
600000
-
P56524
gel filtration
600000
-
Q7Z8L7, Q7Z8L9
gel filtration, enzyme is part of a high molecular weight complex insensitive to trichostatin A
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 42000, SDS-PAGE
?
Q969S8
x * 70000, SDS-PAGE
?
P56524
x * 105000, calculated, x * 119000, SDS-PAGE of FLAG-tagged protein
?
Q7Z8L7, Q7Z8L9
x * 120000, SDS-PAGE and calculated
?
Q96DB2
x * 39000, calculated
?
-
x * 42188, calculated
?
Q9BY41
x * 45240, calculated
?
-
x * 90000, SDS-PAGE and calculated
?
Q7Z8L7, Q7Z8L9
x * 98000, SDS-PAGE and calculated
?
Thermus caldophilus GK24
-
x * 42188, calculated
-
monomer
P56517
1 * 66000, SDS-PAGE, 1 * 54938, calculated
additional information
-
class II histone deacetylases bind myocyte enhancer factor-2
additional information
-
enzyme contains an amino-terminal catalytic domain and a carboxyl pseudo-repeat that shares significant homology with its catalytic domain
additional information
Q9ZTP8
enzyme copurifies as a complex with a protein related to the retinoblastoma-associated protein, Rbap46
additional information
-
enzyme has a bipartite modular structure consisting of a N-terminal putative deacetylase domain and a C-terminal leucine-rich domain. Isoform HDAC10 interacts with enzyme isoform HDAC3, but not with HDAC4 or HDAC6
additional information
-
enzyme interacts directly with transcription factor MEF-2
additional information
Q8WUI4
histone deacetylase activity of isoform HDAC7 maps to a C-terminal domain and is dependent on interaction with isoform HDAC3 in the nucleus. Cytoplasmic HDAC7 that is not bound to HDAC3 is inactive. Transcriptional corepressors SMRT and N-CoR may serve as critical mediators of interaction between HDAC7 and HDAC3
additional information
-
in undifferentiatied muscle cells, isoform HDAC1 associates with transcription factor MyoD resulting in silencing of MyoD-dependent transcription of endogenous p21 as well as muscle-specific genes
additional information
-
isoform HD2 dissociates into HD1 when treated with 1.6 M NaCl or applied to a Q-Sepharose column. The active form of enzyme is a high-molecular-mass complex associated with proteins that are components of the nuclear matrix
additional information
Q96DB2
isoform HDAC11 interacts with isoform HDAC6
additional information
-
isoforms HDAC1 and HDAC2 are associated in vivo, complex is able to deacetylate all four core histones in vitro
additional information
-
isoforms HDAC1, HDAC2, HDAC3 co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
isoform HDAC1 is phosphorylated at S423 and S421. Loss of phosphorylation reduces the enzyme acivity and complex formation
acetylation
-
HDAC, but not HDAC2 is acetylated by p300
additional information
Q969S8
sequence contains a potential N-glycosylation site at D616, 3 putative protein kinase C phosphorylation sites, and several putative casein kinase phosphorylation sites
additional information
Q9BY41
sequence includes a potential N-glycosylation site at N136, a cAMP-dependent kinase phosphorylation site at S39, and two potential casein kinase II phosphorylation sites
additional information
-
cyclopentenone prostaglandins covalently alkylate (carbonylate) class I HDAC1, -2, and -3
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
free enzyme and in complexes with inhibitors trichostatin A and suberoylanilide hydroxamic acid. Active site consists of a tubular pocket, a zinc-binding site and two D-H charge-relay systems
-
modeling studies using inhibitor 6-[(9H-fluoren-3-ylmethyl)(3-phenoxybenzyl)amino]-N-hydroxyhexanamide and histone deacetylase-like protein, PDB ID: 1C3R. Inhibitor fills the equivalent space at the protein surface and occupies the catalytic binding site, coordinating the fundamental zinc ion
O67135
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
Q9BY41
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
P56524
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
Q8WUI4
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Co(2+)-HDAC8 is stable in the presence of oxygen
-
712485
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by affinity chromatography on a 5-ml HiTrap Chelating column charged with Ni2+ and by anion exchange chromatography on a Source 30Q column
Q8WUI4
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
-
using a mono Q HR5-5 column
-
via affinity chromatography using irreversible inhibitor trapoxin
-
cytoplasmic lysates are prepared
Q9Z2V5
using an engineered HPC4 epitope tag at the C-terminus
Q7K6A1
recombinant protein
-
enzyme copurifies as a complex with a protein related to the retinoblastoma-associated protein, Rbap46
Q9ZTP8
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
transient and stable expression of green fluorescent protein-tagged enzyme in onion cells and roots, seeds and leaves of Arabidopsis. For control of enzymic activity, expression in bacterial cells. Expression in insect cells does not result in catalytically active enzyme
O22446
His-tagged expression in Escherichia coli; His-tagged expression in Escherichia coli
Q7Z8L7, Q7Z8L9
expression in Escherichia coli, GST fusion protein
-
full lengtht cDNAs for hdac1 and hdac3 are cloned into the pGEM-T easy vector and confirmed by sequencing, for functional analysis the genes are subcloned into the vector pCS2
Q803C3
expression in Sf9 cells of full-length protein and of Gal4-dHDAC1, consisting of the N-terminal 147 amino acid residues of the yeast Gal4 protein fused to the N terminus of full-length dHDAC1 protein
-
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
Q96DB2
expression in 293T, HeLa and Neuro2A cells
-
expression in baculoviral system, His-tagged protein
Q9UBN7
expression in Escherichia coli
-
expression in HEK-293 cells and Escherichia coli
Q9BY41
expression in HeLa and Sf9 cells, FLAG-tagged protein
-
expression in SV40 T-Ag Jurkat cells
-
expression in U2OS and 293T cells
Q969S8
expression of FLAG-tagged enzyme in T-Ag Jurkat cells
-
expression of FLAG-tagged protein in 293 cells
P56524
expression with FLAG-tag in HEK-293 cells
-
FLAG-tagged HDAC1 deletion mutants, aa 1-482, 1-140 and 141-482, are constructed in pcDNA3 FLAG expression plasmid
-
FLAG-tagged protein, expression in C2 or 10T1/2 cells
-
full-length HDAC1 with COOH-terminal His tag is expressed using baculovirus expression system; full-length HDAC2 with COOH-terminal His tag is expressed using baculovirus expression system; full-length HDAC3 with COOH-terminal His tag is expressed using baculovirus expression system; full-length HDAC4 with COOH-terminal His tag is expressed using baculovirus expression system; full-length HDAC8 with COOH-terminal His tag is expressed using baculovirus expression system
P56524
HDAC1 mutants are cloned into pBJ5HDAC1-F
-
isoform HDAC1
-
isoform HDAC8, expression in Escherichia coli
Q9BY41
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 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
Q8WUI4
isoform HDAC3, expression in NIH 3T3 fibroblasts
-
stable expression in MCF-7 cell
-
into the pAc5.1 expression vector for expression in S2 insect cells
Q7K6A1
overexpression in Escherichia coli as glutathione S-transferase fusion protein
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
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
-
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
-
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
-
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
-
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
-
isoform HDAC2-2 transcript levels decline 6 h after abscisic acid treatment and show no significant difference in 24 h after abscisic acid treatment
C1IC97, C1IC98
isoform HDAC2-1 is significantly induced at 6 and 24 h after spraying of seedlings with 0.1 mM jasmonic acid, isoform HDAC2-1 shows a marked induction at 24 h after 0.1 mM abscisic acid treatment, isoform HDAC2-1 transcript levels show an increase upon treatment with 0.1 mM salicylic acid after 24 h
C1IC97, C1IC98
no conclusions can be drawn for isoform HDAC2-2 after 0.1 mM salicylic acid treatment as transcripts levels increase both in treated and untreated plants at 6 and 24 h, but with no significant differences between them
C1IC97, C1IC98
mutations of the SCF-CDC4 ubiquitin ligase complex suppress cell death by preventing the degradation of Msn2 and Msn4 transcription factors. Accumulation of transcription factors Msn2 and Msn4 leads to the induction of PNC1, which is an activator of the Sir2 histone acetylase
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C261S
-
the single mutant forms about 70% less covalent adduct with 5-deoxy-DELTA12,14-prostaglandin J2-biotin compared to the wild type enzyme
C261S/C273S
-
the double mutant shows about 95% less alkylation by 0.005 mM 5-deoxy-DELTA12,14-prostaglandin J2-biotin compared to the wild type enzyme
C273S
-
the single mutant forms about 70% less covalent adduct with 5-deoxy-DELTA12,14-prostaglandin J2-biotin compared to the wild type enzyme
D101A
-
mutant, confirms that the strictly conserved side chain of D101 is crucial for the function of the L2 loop
D101E
-
mutant, confirms that the strictly conserved side chain of D101 is crucial for the function of the L2 loop
D101L
-
mutant, confirms that the strictly conserved side chain of D101 is crucial for the function of the L2 loop
D101N
-
mutant, confirms that the strictly conserved side chain of D101 is crucial for the function of the L2 loop
D174N
-
isoform HDAC1 mutant, about 5% of wild-type activity, reduced ability to bind a trapoxin-affinity matrix and decreased interaction with proteins RbAp48 and mSin3A
D174N/D176N
-
isoform HDAC1 mutant, about 3% of wild-type activity, reduced ability to bind a trapoxin-affinity matrix and decreased interaction with proteins RbAp48 and mSin3A
D176A
-
the mutation increases the K1/2 for potassium inhibition by more than 40fold
D176N
-
isoform HDAC1 mutant, about 3% of wild-type activity, reduced ability to bind a trapoxin-affinity matrix and decreased interaction with proteins RbAp48 and mSin3A
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
H135A
Q969S8
loss of catalytic activity
H141A
-
isoform HDAC1 mutant, about 20% of wild-type activity, reduced ability to bind a trapoxin-affinity matrix
H141A
-
not able to deacetylate MyoD transcription factor or to repress MyoD-mediated transcription in vivo
H141A
-
mutated channel residue, 20% deacetylase activity
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
Q9UBN7
mutation in the first catalytic domain of enzyme, slight decrease in catalytic rate
H28A
-
mutated channel residue, 20% deacetylase activity
H611A
Q9UBN7
mutation in second catalytic domain of enzyme, more than 5000fold decrease in catalytic rate
H843A
Q8WUI4
mutant, constructed to assess the role of the active site His-843
H843F
Q8WUI4
mutant, constructed to assess the role of the active site His-843
H843Y
Q8WUI4
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
P29A
-
mutated channel residue, 18% deacetylase activity
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
-
mutant, constructed for identification of tyrosine residues responsible for HDAC2 degradation
Y146A
-
in presence of peroxynitrite, activity is reduced by 32%. In presence of 3-morpholinosydonomine, activity is reduced similar to wild-type
Y153A
-
mutant, constructed for identification of tyrosine residues responsible for HDAC2 degradation
Y153A
-
in presence of 3-morpholinosydonomine, activity is reduced similar to wild-type. In presence of peroxynitrite, activity is abolished
Y204A
-
mutated channel residue, 40% deacetylase activity
Y253A
-
mutant, constructed for identification of tyrosine residues responsible for HDAC2 degradation
Y253A
-
Y253 is at least partly responsible for the proteasomal degradation of HDAC2 under nitrative stress. Activity is not reduced in presence of 3-morpholinosydonomine
additional information
-
deletion of enzyme gene hdaA causes transcriptional activation of two telomere-proximal gene clusters and subsequent increased levels of the corresponding molecules, but not of a telomere-distal cluster
additional information
-
knock-down by RNAi does not result in muscle function or developmental defects
L271A
-
mutated channel residue, 12% deacetylase activity
additional information
-
deletion of casein kinase 2 consensus sequence resulting in loss of phosphorylation reduces the enzyme activity and complex formation. Deletion of the highly charged C-terminal region decreases catalytic activity to 22% of wild-type and protein associations
additional information
Q9UBN7
enzyme contains two potentially functional catalytic domains. Expression of first domain alone does not result in catalytic activity. The catalytic domain II alone shows only a modest decrease in substrate binding and product formation rate compared to wild-type
additional information
Q9BY41
knock-down of isoform HDAC8 expression by RNAi inhibits growth of human lung, colon, and cervical cancer cell lines
additional information
-
silencing of enzyme isoforms HDAC, HDAC6, and HDAC8 expression impairs transforming growth factor beta1-induced expression of smooth muscle alpha-actin. HDAC4 silencing is most efficient and also prevents transforming growth factor beta1-mediated morphological changes. Forced down-regulation of HDAC4 stimulates the expression of 5-TG-3-interacting factor and TGIF2 homeoproteins
additional information
-
silencing of isoforms HDAC1, HDAC2, HDAC3 by RNAi markedly decreases interferon gamma-driven gene activation. Overexpression of the enzymes enhances STAT1-driven transcriptional activity
additional information
-
complex of HDAC6-microtubule directly bind to alpha subunit of FTase
Y298H
-
deacetylase-dead mutant
additional information
-
knock-down of isoform HDAC2 expression by small hairpin RNA inhibits cellular proliferation in a dose-dependent manner, which is also partly p53-dependent and induces cellular senescence. Knock-down enhances p53-dependent trans-repression and trans-activation of a subset of target genes. Enhancement is due to increased p53-DNA binding activity
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
general inhibition of histone deacetylases alters the balance of T helper 1 and T helper 2 effector cell activation and migration
medicine
-
inhibitors of histone deacetylase activity sensitize colon cancer cells to interferon gamma-induced apoptosis through cooperative negative regulation of the Bcl-x expression
medicine
Q9BY41
knock-down of isoform HDAC8 expression by RNAi inhibits growth of human lung, colon, and cervical cancer cell lines
medicine
-
a representative compound, (2E)-N-hydroxy-3-[2-(2-phenylethyl)-1-(2-pyrrolidin-1-ylethyl)-1H-benzimidazol-5-yl]prop-2-enamide, SB639, has demonstrated antitumor activity in a colon cancer xenograft model
medicine
-
because of their fundamental role in gene expression, histone deacetylase proteins are promising targets for cancer treatment
medicine
-
class I and II HDACs are generally considered valuable therapeutic targets for the treatment of leukemia and solid tumors
medicine
-
HDAC inhibition is a clinically validated therapeutic strategy for cancer treatment
medicine
-
HDAC inhibitors are a promising class of anticancer agents
medicine
-
HDAC inhibitors have attracted a great deal of interest as drug targets
medicine
-
HDAC inhibitors have attracted a great deal of interest as drug targets in recent years
medicine
-
HDAC inhibitors in food may help reverse aberrant patterns of histone changes in cancer cells
medicine
-
HDAC inhibitors offer a promising strategy for cancer therapy
medicine
-
HDACs are the most relevant, tractible cancer targets
medicine
-
histone deacetylase activities are elevated in patients with primary myelofibrosis
medicine
-
inhibition of HDAC activity has emerged as a promising approach for reversing the anomalous epigenetic states associated with cancer and other chronic diseases
medicine
-
type I ribosome-inactivating proteins derived from plants are HDAC inhibitors that can be utilized in the prevention and treatment of prostate cancer
medicine
-
histone deacetylase 1 is a gene therapy target in pancreatic ductal adenocarcinoma
medicine
-
compared with healthy non-smokers, HDAC activity in the peripheral blood mononuclear cells of patients with chronic obstructive pulmonary disease is decreased by 40%. In patients with chronic obstructive pulmonary disease, HDAC activity is negatively correlated to smoke intensity. In chronic obstructive pulmonary disease patients who have smoked for more than 40 pack-years, HDAC activity in peripheral blood mononuclear cells is 40% lower than that in chronic obstructive pulmonary disease patients who have smoked fewer than 40 pack-years. Serum CXCL8 levels in patients with chronic obstructive pulmonary disease are significantly higher than that in controls and are negatively correlated to HDAC activities
medicine
-
HDAC2 is nitrated under nitrative/oxidative stress and in the peripheral lung tissues of smokers and patients with chronic obstructive pulmonary disease
medicine
P70288
it is proposed that induction of Hsp70 and subsequent activation of HDAC2 are important triggering signals of cardiac hypertrophy
medicine
-
loss of class IIa HDACs in murine liver results in inhibition of FOXO target genes and lowers blood glucose, resulting in increased glycogen storage. Suppression of class IIa HDACs in mouse models of type 2 diabetes ameliorates hyperglycemia, suggesting that inhibitors of class I/II HDACs may be potential therapeutics for metabolic syndrome
medicine
-
application of HDAC inhibitors in cancer cell lines and mouse model systems leads to interruption of the cell cycle, differentiation and apoptosis, clinical studies have shown tumor repression and improvement of patient symptoms without significant side effects