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7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin + H2O
?
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin + H2O
?
acetylcadaverine + H2O
acetate + cadaverine
acetylputrescine + H2O
acetate + putrescine
diacetylspermidine + H2O
acetate + spermidine
-
81.9% activity of that of N8-acetylspermidine
-
?
N-(3-aminopropyl)acetamide + H2O
propane-1,3-diamine + acetate
very low activity
-
-
?
N-(8-aminooctyl)acetamide + H2O
octane-1,8-diamine + acetate
N-butylacetamide + H2O
butan-1-amine + acetate
N1,N8-diacetylspermidine + 2 H2O
2 acetate + spermidine
moderate activity
-
-
?
N1,N8-diacetylspermidine + H2O
2 acetate + spermidine
high activity
-
-
?
N1-acetylspermidine + H2O
acetate + spermidine
N1-acetylspermine + H2O
acetate + spermine
N1-acetylspermine + H2O
spermine + acetate
N8-acetylspermidine + H2O
acetate + spermidine
Nalpha,Nepsilon-diacetyl-L-lysinamide + H2O
?
low activity
-
-
?
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide + H2O
?
additional information
?
-
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin + H2O
?
very low activity
-
-
?
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin + H2O
?
low activity
-
-
?
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin + H2O
?
very low activity
-
-
?
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin + H2O
?
low activity
-
-
?
acetylcadaverine + H2O
acetate + cadaverine
high acitivity
-
-
?
acetylcadaverine + H2O
acetate + cadaverine
high acitivity
-
-
?
acetylcadaverine + H2O
acetate + cadaverine
-
-
-
-
?
acetylputrescine + H2O
acetate + putrescine
high acitivity
-
-
?
acetylputrescine + H2O
acetate + putrescine
high acitivity
-
-
?
acetylputrescine + H2O
acetate + putrescine
-
-
-
-
?
N-(8-aminooctyl)acetamide + H2O
octane-1,8-diamine + acetate
moderate to high activity
-
-
?
N-(8-aminooctyl)acetamide + H2O
octane-1,8-diamine + acetate
moderate activity
-
-
?
N-butylacetamide + H2O
butan-1-amine + acetate
very low activity
-
-
?
N-butylacetamide + H2O
butan-1-amine + acetate
low activity
-
-
?
N1-acetylspermidine + H2O
acetate + spermidine
very low activity
-
-
?
N1-acetylspermidine + H2O
acetate + spermidine
-
low activity
-
?
N1-acetylspermidine + H2O
acetate + spermidine
-
-
-
?
N1-acetylspermidine + H2O
acetate + spermidine
-
-
-
-
?
N1-acetylspermidine + H2O
acetate + spermidine
-
-
-
?
N1-acetylspermidine + H2O
acetate + spermidine
-
-
-
?
N1-acetylspermine + H2O
acetate + spermine
very low activity
-
-
?
N1-acetylspermine + H2O
acetate + spermine
low activity
-
-
?
N1-acetylspermine + H2O
acetate + spermine
-
-
-
-
?
N1-acetylspermine + H2O
spermine + acetate
-
-
-
?
N1-acetylspermine + H2O
spermine + acetate
-
-
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
-
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
best substrate
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
-
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
highest activity
-
?
N8-acetylspermidine + H2O
acetate + spermidine
best substrate
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
-
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
-
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
preferred substrate
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
involvement in cell growth and differentiation
-
?
N8-acetylspermidine + H2O
acetate + spermidine
-
involvement in controlling the levels of polyamines and acetylated polyamines in tissues
-
?
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide + H2O
?
low activity
-
-
?
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide + H2O
?
low activity
-
-
?
additional information
?
-
histone deacetylase 10 (HDAC10) from Danio rerio is a highly specific N8-acetylspermidine deacetylase. No activity with N1-acetylspermidine and N1-acetylspermine
-
-
?
additional information
?
-
-
histone deacetylase 10 (HDAC10) from Danio rerio is a highly specific N8-acetylspermidine deacetylase. No activity with N1-acetylspermidine and N1-acetylspermine
-
-
?
additional information
?
-
zebrafish HDAC10 complexed with a transition-state analogue inhibitor reveals that a glutamate gatekeeper and a sterically constricted active site confer specificity for N8-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. The N4 amino group of N8-acetylspermidine is recognized by a direct hydrogen bond with E117. No activity with TK(ac)PIW, AK(ac)P, GAK(ac), AK(ac), AK(ac)A, K(ac)NL, K(ac)NL, and GAK(ac)NLQ
-
-
?
additional information
?
-
-
zebrafish HDAC10 complexed with a transition-state analogue inhibitor reveals that a glutamate gatekeeper and a sterically constricted active site confer specificity for N8-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. The N4 amino group of N8-acetylspermidine is recognized by a direct hydrogen bond with E117. No activity with TK(ac)PIW, AK(ac)P, GAK(ac), AK(ac), AK(ac)A, K(ac)NL, K(ac)NL, and GAK(ac)NLQ
-
-
?
additional information
?
-
histone deacetylase 10 (HDAC10) from Homo sapiens is a highly specific N8-acetylspermidine deacetylase. No activity with N1-acetylspermidine and N1-acetylspermine
-
-
?
additional information
?
-
-
histone deacetylase 10 (HDAC10) from Homo sapiens is a highly specific N8-acetylspermidine deacetylase. No activity with N1-acetylspermidine and N1-acetylspermine
-
-
?
additional information
?
-
the conserved glutamate gatekeeper and a sterically constricted active site confer specificity for N8-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. Analysis of the intermolecular interactions of N8-acetylspermidine in the active site of hHDAC10 based on the structure of the Danio rerio enzyme-inhibitor crystal structure zHDAC10-AAT complex. No activity with N-(3-aminopropyl)acetamide, TK(ac)PIW, AK(ac)P, GAK(ac), AK(ac), K(ac)NL, K(ac)NL, and GAK(ac)NLQ
-
-
?
additional information
?
-
-
the conserved glutamate gatekeeper and a sterically constricted active site confer specificity for N8-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. Analysis of the intermolecular interactions of N8-acetylspermidine in the active site of hHDAC10 based on the structure of the Danio rerio enzyme-inhibitor crystal structure zHDAC10-AAT complex. No activity with N-(3-aminopropyl)acetamide, TK(ac)PIW, AK(ac)P, GAK(ac), AK(ac), K(ac)NL, K(ac)NL, and GAK(ac)NLQ
-
-
?
additional information
?
-
-
the bacterial enzyme from Mycoplana ramosa has broader substrate specificity in comparison with mammalian enzyme. Its substrates include both small and large acetylpolyamines such as acetylputrescine, acetylcadaverine, N1- and N8-acetylspermidine, and N1-acetylspermine
-
-
?
additional information
?
-
-
usage of the commercially available Fluor-de-Lys deacetylase fluorogenic substrate fir enzyme activity assays
-
-
?
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1,10-phenanthroline
-
Ki: 1.3 mM
1,5-Diaminopentane
-
cadaverine; Ki: 1.5 mM
1,6-diaminohexane
-
Ki: 1.5 mM
2,2'-dipyridyl
-
Ki: 1.9 mM
2-mercaptoethanol
-
slight inhibition at 1 mM
3-[(3-aminopropyl)amino]-N-hydroxyhexanamide
-
non-competitive inhibition, Ki: 1 nM
5-Aminovaleric acid
-
Ki: 4.1 mM
5-[(3-aminopropyl)amino]pentane-1-thiol
-
-
5-[(3-aminopropyl)amino]pentylboronic acid
-
-
6-aminohexanoic acid
-
Ki: 0.05 mM
6-[(3-aminopropyl)amino]-N-hydroxyhexanamide
-
-
6-[(3-aminopropyl)amino]hexanoic acid
7-[(3-aminopropyl)amino]-1,1,1-trifluoroheptan-2-one
7-[(3-aminopropyl)amino]-1-methoxyheptan-2-one
-
-
7-[(3-aminopropyl)amino]heptan-2-one
-
-
7-[N-(3-aminopropyl)amino]heptan-2-one
8-hydroxyquinoline
-
slight inhibition at 1 mM
acetylprocainamide
-
Ki: 1.9 mM
Acriflavin
-
strong inhibition at 1 mM
Cu2+
-
nearly complete inhibition at 1 mM
Diethylmalonate
-
Ki: 8 mM
diisopropyl fluorophosphate
-
weak inhibition, Ki: 33 mM
echothiopate
-
non-competitive inhibition, Ki: 0.4 mM, i.e.ammonium, (2-mercaptoethyl)trimethyl-, S-ester with O,O-diethyl phosphorothioate
Fe2+
-
strong inhibition at 1 mM
iodoacetamide
-
slight inhibition at 1 mM
N',N''-bis(tert-butoxycarbonyl)-6-[(3-aminopropyl)amino]-N-hydroxyhexanamide
-
-
N',N''-bis(tert-butoxycarbonyl)-6-[(3-aminopropyl)amino]-N-methoxy-N-methylhexanamide
-
-
N,N'-bis(tert-butoxycarbonyl)-5-[(3-aminopropyl)amino]pentan-1-ol
-
-
N,N'-bis(tert-butoxycarbonyl)-5-[(3-aminopropyl)amino]pentane-1-thiol
-
-
N,N'-bis(tert-butoxycarbonyl)-6-[(3-aminopropyl)amino]hexanal
-
-
N,N'-bis(tert-butoxycarbonyl)-6-[(3-aminopropyl)amino]hexanoic acid
-
-
N,N'-bis(tert-butoxycarbonyl)-7-[(3-aminopropyl)amino]-1,1,1-trifluoroheptan-2-ol
-
-
N,N'-bis(tert-butoxycarbonyl)-7-[(3-aminopropyl)amino]-1,1,1-trifluoroheptan-2-one
-
-
N,N'-bis(tert-butoxycarbonyl)-7-[(3-aminopropyl)amino]-1-bromoheptan-2-ol
-
-
N,N'-bis(tert-butoxycarbonyl)-7-[(3-aminopropyl)amino]-1-bromoheptan-2-one
-
-
N,N'-bis(tert-butoxycarbonyl)-7-[(3-aminopropyl)amino]-1-methoxyheptan-2-ol
-
-
N,N'-bis(tert-butoxycarbonyl)-7-[(3-aminopropyl)amino]-1-methoxyheptan-2-one
-
-
N,N'-bis(tert-butoxycarbonyl)-7-[(3-aminopropyl)amino]heptan-2-one
-
-
N-acetylputrescine
-
Ki: 0.8 mM
N-ethylmaleimide
-
Ki: 0.86 mM
N1,N3-bis(tert-butoxycarbonyl)-N1-(5-bromopentyl)propane-1,3-diamine
-
-
N1,N3-bis(tert-butoxycarbonyl)-N1-(hept-6-enyl)propane-1,3-diamine
-
-
N1,N3-bis(tert-butoxycarbonyl)-N1-(pent-4-enyl)propane-1,3-diamine
-
-
N1,N3-bis(tert-butoxycarbonyl)-N1-[5-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)pentyl]propane-1,3-diamine
-
-
N1,N3-bis(tert-butoxycarbonyl)-N1-[5-(methylsulfonyl)pentyl]propane-1,3-diamine
-
-
N1,N3-bis(tert-butoxycarbonyl)-N1-[5-(methylthio)pentyl]propane-1,3-diamine
-
-
N1,N3-bis(tert-butoxycarbonyl)-N1-[5-(oxiran-2-yl)pentyl]propane-1,3-diamine
-
-
N1-(hept-6-enyl)propane-1,3-diamine
-
-
N1-(pent-4-enyl)propane-1,3-diamine
-
-
N1-[5-(methylsulfonyl)pentyl]propane-1,3-diamine
-
-
N8-Acetylspermidine
-
stimulation of cell growth due to inhibition of N8-acetylspremidine deacetylase, maximum cell growth stimulation above 1 mM
NaN3
-
slight inhibition at 1 mM
p-chloromercuribenzoic acid
Pargyline
-
slight inhibition at 1 mM
Quinacrine
-
strong inhibition at 1 mM
S-{5-[(3-aminopropyl)amino]pentyl} thioacetate
-
-
S-{7-[(3-aminopropyl)amino]-2-oxoheptyl} ethanethioate
-
-
S-{N,N'-bis(tert-butoxycarbonyl)-5-[(3-aminopropyl)amino]pentyl} thioacetate
-
-
S-{N,N'-bis(tert-butoxycarbonyl)-7-[(3-aminopropyl)amino]-2-oxoheptyl}thioacetate
-
-
Semicarbazide
-
slight inhibition at 1 mM
sodium butyrate
-
weak inhibition, Ki: 38.5 mM
additional information
-
design, synthesis, and evaluation of N8-acetylspermidine analogues bearing different zinc binding groups as potential inhibitors of the enzyme, overview. Most of the synthesized compounds exhibit modest potency, with IC50 values in the mid-micromolar range, but compounds bearing hydroxamate or trifluoromethylketone zinc binding groups exhibit enhanced inhibitory potency in the mid-nanomolar range. Three compounds exhibit very poor inhibitory potency against th enzyme, 6-[(3-aminopropyl)amino]hexanoic acid, S-{5-[(3-aminopropyl)amino]pentyl} thioacetate, and N1-[5-(methylsulfonyl)pentyl]propane-1,3-diamine dihydrochloride
-
1,4-diaminobutane
-
competitive inhibition, Ki: 0.25 mM; putrescine
1,4-diaminobutane
-
Ki: 1.45 mM; putrescine
1,4-diaminobutane
-
competitive inhibition, Ki: 0.25 mM
6-[(3-aminopropyl)amino]hexanoic acid
-
-
6-[(3-aminopropyl)amino]hexanoic acid
-
Ki: 0.011 mM
7-[(3-aminopropyl)amino]-1,1,1-trifluoroheptan-2-one
AAT, binds as a tetrahedral gem-diolate to both APAH (acetylpolyamine amidohydrolase, EC 3.5.1.62) and HDAC10, thereby mimicking the tetrahedral intermediate and its flanking transition states in catalysis
7-[(3-aminopropyl)amino]-1,1,1-trifluoroheptan-2-one
AAT, enzyme-bound structure analysis, overview. This inhibitor binds as a transition state analogue
7-[(3-aminopropyl)amino]-1,1,1-trifluoroheptan-2-one
AAT, binds as a tetrahedral gem-diolate to both APAH (acetylpolyamine amidohydrolase, EC 3.5.1.62) and HDAC10, thereby mimicking the tetrahedral intermediate and its flanking transition states in catalysis
7-[(3-aminopropyl)amino]-1,1,1-trifluoroheptan-2-one
AAT, the inhibitor binds as a transition state analogue
7-[(3-aminopropyl)amino]-1,1,1-trifluoroheptan-2-one
-
-
7-[N-(3-aminopropyl)amino]heptan-2-one
-
stimulation of cell growth due to inhibition of N8-acetylspermidine deacetylase, maximum cell growth stimulation at 0.1 mM
7-[N-(3-aminopropyl)amino]heptan-2-one
-
induction of neurite outgrowth at 0.001 to 0.0001 mM due to inhibition of N8-acetylspermidine deacetylase, involvement in differentiation of PC 12 cells
dithiothreitol
-
remarkable inhibition at 1 mM
dithiothreitol
-
inhibition above 3 mM
EDTA
-
Ki: 3.5 mM
EDTA
-
inhibition above 2.5 mM
N1-acetylspermidine
-
Ki: 1.37 mM
N1-acetylspermidine
-
Ki: 0.16 mM, competitive inhibition
p-chloromercuribenzoic acid
-
complete inhibition at 1 mM
p-chloromercuribenzoic acid
-
Ki: 0.15 mM
spermidine
-
competitive inhibition, Ki: 0.055 mM
spermidine
-
competitive inhibition, Ki: 0.055 mM
spermine
-
competitive inhibition, Ki: 0.036 mM
spermine
-
competitive inhibition, Ki: 0.036 mM
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Adenocarcinoma of Lung
HDAC10 Regulates Cancer Stem-Like Cell Properties in KRAS-Driven Lung Adenocarcinoma.
Adrenal Cortex Neoplasms
Comprehensive DNA methylation analysis of benign and malignant adrenocortical tumors.
Carcinogenesis
HDAC10 expression is associated with DNA mismatch repair gene and is a predictor of good prognosis in colon carcinoma.
Carcinogenesis
HDAC10 Regulates Cancer Stem-Like Cell Properties in KRAS-Driven Lung Adenocarcinoma.
Carcinogenesis
Histone deacetylase 10 exerts anti-tumor effects on cervical cancer via a novel microRNA-223/TXNIP/Wnt/?-catenin pathway.
Carcinogenesis
Histone deacetylase 10 exerts antitumor effects on cervical cancer via a novel microRNA-223/TXNIP/Wnt/?-catenin pathway.
Carcinoma
HDAC10 as a potential therapeutic target in ovarian cancer.
Carcinoma
HDAC10 expression is associated with DNA mismatch repair gene and is a predictor of good prognosis in colon carcinoma.
Carcinoma
HDAC10 Is Positively Associated With PD-L1 Expression and Poor Prognosis in Patients With NSCLC.
Carcinoma
Histone Deacetylase (HDAC) 10 Suppresses Cervical Cancer Metastasis through Inhibition of Matrix Metalloproteinase (MMP) 2 and 9 Expression.
Carcinoma
Histone deacetylase 10 suppresses proliferation and invasion by inhibiting the phosphorylation of ?-catenin and serves as an independent prognostic factor for human clear cell renal cell carcinoma.
Carcinoma, Hepatocellular
Growth attenuation is associated with histone deacetylase 10-induced autophagy in the liver.
Carcinoma, Renal Cell
Histone deacetylase 10 suppresses proliferation and invasion by inhibiting the phosphorylation of ?-catenin and serves as an independent prognostic factor for human clear cell renal cell carcinoma.
Carcinoma, Squamous Cell
Histone Deacetylase (HDAC) 10 Suppresses Cervical Cancer Metastasis through Inhibition of Matrix Metalloproteinase (MMP) 2 and 9 Expression.
Colitis
HDAC10 deletion promotes Foxp3+ T-regulatory cell function.
Colonic Neoplasms
HDAC10 expression is associated with DNA mismatch repair gene and is a predictor of good prognosis in colon carcinoma.
Kidney Neoplasms
DDX39B Predicts Poor Survival and Associated with Clinical Benefit of Anti-PD-L1 Therapy in ccRCC.
Leukemia, Lymphocytic, Chronic, B-Cell
Expression and Function of Histone Deacetylase 10 (HDAC10) in B Cell Malignancies.
Lung Neoplasms
4-hydroxyphenylpyruvate dioxygenase promotes lung cancer growth via pentose phosphate pathway (PPP) flux mediated by LKB1-AMPK/HDAC10/G6PD axis.
Lung Neoplasms
HDAC10 Is Positively Associated With PD-L1 Expression and Poor Prognosis in Patients With NSCLC.
Lung Neoplasms
HDAC10 promotes lung cancer proliferation via AKT phosphorylation.
Lung Neoplasms
HDAC10 Regulates Cancer Stem-Like Cell Properties in KRAS-Driven Lung Adenocarcinoma.
Lymphatic Metastasis
Histone Deacetylase (HDAC) 10 Suppresses Cervical Cancer Metastasis through Inhibition of Matrix Metalloproteinase (MMP) 2 and 9 Expression.
Lymphoma
Expression and Function of Histone Deacetylase 10 (HDAC10) in B Cell Malignancies.
Lymphoma, Mantle-Cell
Expression and Function of Histone Deacetylase 10 (HDAC10) in B Cell Malignancies.
Malnutrition
Growth attenuation is associated with histone deacetylase 10-induced autophagy in the liver.
Neoplasm Metastasis
Histone Deacetylase (HDAC) 10 Suppresses Cervical Cancer Metastasis through Inhibition of Matrix Metalloproteinase (MMP) 2 and 9 Expression.
Neoplasm Metastasis
Histone deacetylase 10 exerts anti-tumor effects on cervical cancer via a novel microRNA-223/TXNIP/Wnt/?-catenin pathway.
Neoplasm Metastasis
Histone deacetylase 10 exerts antitumor effects on cervical cancer via a novel microRNA-223/TXNIP/Wnt/?-catenin pathway.
Neoplasm Metastasis
Histone deacetylase 10 suppresses proliferation and invasion by inhibiting the phosphorylation of ?-catenin and serves as an independent prognostic factor for human clear cell renal cell carcinoma.
Neoplasm Metastasis
Suppression of lung cancer cell invasion and metastasis by connexin43 involves the secretion of follistatin-like 1 mediated via histone acetylation.
Neoplasms
4-hydroxyphenylpyruvate dioxygenase promotes lung cancer growth via pentose phosphate pathway (PPP) flux mediated by LKB1-AMPK/HDAC10/G6PD axis.
Neoplasms
Binding of N8-Acetylspermidine Analogues to Histone Deacetylase 10 Reveals Molecular Strategies for Blocking Polyamine Deacetylation.
Neoplasms
Decreased expression of histone deacetylase 10 predicts poor prognosis of gastric cancer patients.
Neoplasms
Expression and Function of Histone Deacetylase 10 (HDAC10) in B Cell Malignancies.
Neoplasms
HDAC10 as a potential therapeutic target in ovarian cancer.
Neoplasms
HDAC10 expression is associated with DNA mismatch repair gene and is a predictor of good prognosis in colon carcinoma.
Neoplasms
HDAC10 promotes lung cancer proliferation via AKT phosphorylation.
Neoplasms
HDAC10 Regulates Cancer Stem-Like Cell Properties in KRAS-Driven Lung Adenocarcinoma.
Neoplasms
Histone Deacetylase (HDAC) 10 Suppresses Cervical Cancer Metastasis through Inhibition of Matrix Metalloproteinase (MMP) 2 and 9 Expression.
Neoplasms
Histone deacetylase 10 exerts anti-tumor effects on cervical cancer via a novel microRNA-223/TXNIP/Wnt/?-catenin pathway.
Neoplasms
Histone deacetylase 10 exerts antitumor effects on cervical cancer via a novel microRNA-223/TXNIP/Wnt/?-catenin pathway.
Neoplasms
Histone deacetylase 10 promotes autophagy-mediated cell survival.
Neoplasms
Histone deacetylase 10 suppresses proliferation and invasion by inhibiting the phosphorylation of ?-catenin and serves as an independent prognostic factor for human clear cell renal cell carcinoma.
Neoplasms
Histone deacetylase 10, a potential epigenetic target for therapy.
Neoplasms
Histone deacetylase 10-promoted autophagy as a druggable point of interference to improve the treatment response of advanced neuroblastomas.
Neoplasms
Selective Inhibitors of Histone Deacetylase 10 (HDAC-10).
Neoplasms
The HDAC6/8/10 inhibitor TH34 induces DNA damage-mediated cell death in human high-grade neuroblastoma cell lines.
Neoplasms
X-ray Crystallographic Snapshots of Substrate Binding in the Active Site of Histone Deacetylase 10.
Neuroblastoma
Binding of N8-Acetylspermidine Analogues to Histone Deacetylase 10 Reveals Molecular Strategies for Blocking Polyamine Deacetylation.
Neuroblastoma
Dual role of HDAC10 in lysosomal exocytosis and DNA repair promotes neuroblastoma chemoresistance.
Neuroblastoma
Histone deacetylase 10 promotes autophagy-mediated cell survival.
Neuroblastoma
Histone deacetylase 10-promoted autophagy as a druggable point of interference to improve the treatment response of advanced neuroblastomas.
Neuroblastoma
Selective Inhibition of Histone Deacetylase 10: Hydrogen Bonding to the Gatekeeper Residue is Implicated.
Neuroblastoma
Selective Inhibitors of Histone Deacetylase 10 (HDAC-10).
Neuroblastoma
The HDAC6/8/10 inhibitor TH34 induces DNA damage-mediated cell death in human high-grade neuroblastoma cell lines.
Ovarian Neoplasms
HDAC10 as a potential therapeutic target in ovarian cancer.
Pulmonary Disease, Chronic Obstructive
Gene expression profile of human lung in a relatively early stage of COPD with emphysema.
Stomach Neoplasms
Decreased expression of histone deacetylase 10 predicts poor prognosis of gastric cancer patients.
Stomach Neoplasms
Inhibition of histone deacetylase 10 induces thioredoxin-interacting protein and causes accumulation of reactive oxygen species in SNU-620 human gastric cancer cells.
Uterine Cervical Neoplasms
Histone Deacetylase (HDAC) 10 Suppresses Cervical Cancer Metastasis through Inhibition of Matrix Metalloproteinase (MMP) 2 and 9 Expression.
Uterine Cervical Neoplasms
Histone deacetylase 10 exerts anti-tumor effects on cervical cancer via a novel microRNA-223/TXNIP/Wnt/?-catenin pathway.
Uterine Cervical Neoplasms
Histone deacetylase 10 exerts antitumor effects on cervical cancer via a novel microRNA-223/TXNIP/Wnt/?-catenin pathway.
Uterine Cervical Neoplasms
Oncogenic miRNA-1908 targets HDAC10 and promotes the aggressive phenotype of cervical cancer cell.
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0.01 - 0.07
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
0.066 - 0.15
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
0.05 - 0.26
Acetylcadaverine
0.11 - 0.17
acetylputrescine
0.16 - 0.17
N-(8-aminooctyl)acetamide
0.9
N-butylacetamide
pH 8.0, 22°C, recombinant wild-type enzyme
0.15 - 0.18
N1,N8-diacetylspermidine
0.003
N1-acetylspermidine
-
-
0.016 - 0.18
N1-acetylspermine
0.004 - 0.27
N8-Acetylspermidine
0.14
Nalpha,Nepsilon-diacetyl-L-lysinamide
pH 8.0, 22°C, recombinant enzyme
0.06 - 0.08
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide
additional information
additional information
-
0.01
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant enzyme
0.017
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant D94A
0.022
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant wild-type enzyme
0.06
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant deletion mutant DELTAnuA2
0.06
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant N93A
0.07
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant E274L
0.066
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant wild-type enzyme
0.07
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant E274L
0.11
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant enzyme
0.11
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant N93A
0.15
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant D94A
0.05
Acetylcadaverine
pH 8.0, 22°C, recombinant mutant N93A
0.06
Acetylcadaverine
pH 8.0, 22°C, recombinant mutant E274L
0.09
Acetylcadaverine
pH 8.0, 22°C, recombinant wild-type enzyme
0.11
Acetylcadaverine
pH 8.0, 22°C, recombinant enzyme
0.26
Acetylcadaverine
pH 8.0, 22°C, recombinant mutant D94A
0.11
acetylputrescine
pH 8.0, 22°C, recombinant mutant D94A
0.13
acetylputrescine
pH 8.0, 22°C, recombinant mutant N93A
0.16
acetylputrescine
pH 8.0, 22°C, recombinant wild-type enzyme
0.16
acetylputrescine
pH 8.0, 22°C, recombinant mutant E274L
0.17
acetylputrescine
pH 8.0, 22°C, recombinant enzyme
0.16
N-(8-aminooctyl)acetamide
pH 8.0, 22°C, recombinant enzyme
0.17
N-(8-aminooctyl)acetamide
pH 8.0, 22°C, recombinant wild-type enzyme
0.15
N1,N8-diacetylspermidine
pH 8.0, 22°C, recombinant enzyme
0.18
N1,N8-diacetylspermidine
pH 8.0, 22°C, recombinant wild-type enzyme
0.016
N1-acetylspermine
-
-
0.18
N1-acetylspermine
pH 8.0, 22°C, recombinant enzyme
0.004
N8-Acetylspermidine
-
-
0.011
N8-Acetylspermidine
-
-
0.1
N8-Acetylspermidine
pH 8.0, 22°C, recombinant enzyme
0.13
N8-Acetylspermidine
pH 8.0, 22°C, recombinant wild-type enzyme
0.13
N8-Acetylspermidine
pH 8.0, 22°C, recombinant mutant E274L
0.14
N8-Acetylspermidine
pH 8.0, 22°C, recombinant mutant D94A
0.15
N8-Acetylspermidine
pH 8.0, 22°C, recombinant mutant N93A
0.211
N8-Acetylspermidine
-
-
0.27
N8-Acetylspermidine
pH 8.0, 22°C, recombinant deletion mutant DELTAnuA2
0.06
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide
pH 8.0, 22°C, recombinant enzyme
0.08
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide
pH 8.0, 22°C, recombinant wild-type enzyme
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
steady-state kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00007 - 0.053
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
0.0013 - 0.21
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
0.02 - 0.37
Acetylcadaverine
0.034 - 0.7
acetylputrescine
0.1 - 0.21
N-(8-aminooctyl)acetamide
0.06
N-butylacetamide
pH 8.0, 22°C, recombinant wild-type enzyme
0.14 - 0.48
N1,N8-diacetylspermidine
0.011
N1-acetylspermine
pH 8.0, 22°C, recombinant enzyme
0.028 - 0.9
N8-Acetylspermidine
0.0092
Nalpha,Nepsilon-diacetyl-L-lysinamide
pH 8.0, 22°C, recombinant enzyme
0.0006 - 0.013
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide
additional information
additional information
-
0.00007
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant N93A
0.00033
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant wild-type enzyme
0.00038
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant enzyme
0.00046
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant D94A
0.021
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant deletion mutant DELTAnuA2
0.053
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant E274L
0.0013
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant D94A
0.0013
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant N93A
0.0015
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant wild-type enzyme
0.008
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant enzyme
0.21
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant E274L
0.02
Acetylcadaverine
pH 8.0, 22°C, recombinant mutant E274L
0.051
Acetylcadaverine
pH 8.0, 22°C, recombinant mutant N93A
0.14
Acetylcadaverine
pH 8.0, 22°C, recombinant enzyme
0.29
Acetylcadaverine
pH 8.0, 22°C, recombinant mutant D94A
0.37
Acetylcadaverine
pH 8.0, 22°C, recombinant wild-type enzyme
0.034
acetylputrescine
pH 8.0, 22°C, recombinant mutant E274L
0.126
acetylputrescine
pH 8.0, 22°C, recombinant mutant N93A
0.24
acetylputrescine
pH 8.0, 22°C, recombinant mutant D94A
0.35
acetylputrescine
pH 8.0, 22°C, recombinant enzyme
0.7
acetylputrescine
pH 8.0, 22°C, recombinant wild-type enzyme
0.1
N-(8-aminooctyl)acetamide
pH 8.0, 22°C, recombinant enzyme
0.21
N-(8-aminooctyl)acetamide
pH 8.0, 22°C, recombinant wild-type enzyme
0.14
N1,N8-diacetylspermidine
pH 8.0, 22°C, recombinant enzyme
0.48
N1,N8-diacetylspermidine
pH 8.0, 22°C, recombinant wild-type enzyme
0.028
N8-Acetylspermidine
pH 8.0, 22°C, recombinant mutant E274L
0.082
N8-Acetylspermidine
pH 8.0, 22°C, recombinant deletion mutant DELTAnuA2
0.123
N8-Acetylspermidine
pH 8.0, 22°C, recombinant mutant N93A
0.28
N8-Acetylspermidine
pH 8.0, 22°C, recombinant enzyme
0.58
N8-Acetylspermidine
pH 8.0, 22°C, recombinant wild-type enzyme
0.9
N8-Acetylspermidine
pH 8.0, 22°C, recombinant mutant D94A
0.0006
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide
pH 8.0, 22°C, recombinant enzyme
0.013
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide
pH 8.0, 22°C, recombinant wild-type enzyme
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0012 - 0.757
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
0.0087 - 8.84
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
0.333 - 4.11
Acetylcadaverine
0.213 - 4.375
acetylputrescine
0.93 - 1.24
N-(8-aminooctyl)acetamide
0.067
N-butylacetamide
pH 8.0, 22°C, recombinant wild-type enzyme
0.14
N1,N8-diacetylspermidine
pH 8.0, 22°C, recombinant enzyme
0.061
N1-acetylspermine
pH 8.0, 22°C, recombinant enzyme
0.215 - 6.43
N8-Acetylspermidine
0.066
Nalpha,Nepsilon-diacetyl-L-lysinamide
pH 8.0, 22°C, recombinant enzyme
0.01 - 0.163
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide
0.0012
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant N93A
0.015
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant wild-type enzyme
0.027
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant D94A
0.038
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant enzyme
0.35
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant deletion mutant DELTAnuA2
0.757
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant E274L
0.0087
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant D94A
0.012
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant N93A
0.023
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant wild-type enzyme
0.072
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant enzyme
8.84
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin
pH 8.0, 22°C, recombinant mutant E274L
0.333
Acetylcadaverine
pH 8.0, 22°C, recombinant mutant E274L
1.02
Acetylcadaverine
pH 8.0, 22°C, recombinant mutant N93A
1.16
Acetylcadaverine
pH 8.0, 22°C, recombinant mutant D94A
1.27
Acetylcadaverine
pH 8.0, 22°C, recombinant enzyme
4.11
Acetylcadaverine
pH 8.0, 22°C, recombinant wild-type enzyme
0.213
acetylputrescine
pH 8.0, 22°C, recombinant mutant E274L
0.97
acetylputrescine
pH 8.0, 22°C, recombinant mutant N93A
2.06
acetylputrescine
pH 8.0, 22°C, recombinant enzyme
2.18
acetylputrescine
pH 8.0, 22°C, recombinant mutant D94A
4.375
acetylputrescine
pH 8.0, 22°C, recombinant wild-type enzyme
0.93
N-(8-aminooctyl)acetamide
pH 8.0, 22°C, recombinant enzyme
1.24
N-(8-aminooctyl)acetamide
pH 8.0, 22°C, recombinant wild-type enzyme
0.215
N8-Acetylspermidine
pH 8.0, 22°C, recombinant mutant E274L
0.304
N8-Acetylspermidine
pH 8.0, 22°C, recombinant deletion mutant DELTAnuA2
0.82
N8-Acetylspermidine
pH 8.0, 22°C, recombinant mutant N93A
2.8
N8-Acetylspermidine
pH 8.0, 22°C, recombinant enzyme
4.46
N8-Acetylspermidine
pH 8.0, 22°C, recombinant wild-type enzyme
6.43
N8-Acetylspermidine
pH 8.0, 22°C, recombinant mutant D94A
0.01
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide
pH 8.0, 22°C, recombinant enzyme
0.163
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide
pH 8.0, 22°C, recombinant wild-type enzyme
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evolution
the enzyme adopts the characteristic arginase-deacetylase fold and employ a Zn2+-activated water molecule for catalysis. The active sites of HDAC10 and APAH (acetylpolyamine amidohydrolase, EC 3.5.1.62) are sterically constricted to enforce specificity for long, slender polyamine substrates and exclude bulky peptides and proteins containing acetyl-L-lysine. The tertiary structure (a unique 310 helix defined by the P(E,A)CE motif) provides the steric constriction that directs the polyamine substrate specificity of HDAC10. Structure and catalytic mechanism of polyamine deacetylases, comparison of HDAC and APAH, overview
evolution
the enzyme adopts the characteristic arginase-deacetylase fold and employ a Zn2+-activated water molecule for catalysis. The active sites of HDAC10 and APAH (acetylpolyamine amidohydrolase, EC 3.5.1.62) are sterically constricted to enforce specificity for long, slender polyamine substrates and exclude bulky peptides and proteins containing acetyl-L-lysine. The tertiary structure (a unique 310 helix defined by the P(E,A)CE motif) provides the steric constriction that directs the polyamine substrate specificity of HDAC10. Structure and catalytic mechanism of polyamine deacetylases, comparison of HDAC and APAH, overview
physiological function
cationic polyamines such as spermidine and spermine are critical in all forms of life, as they regulate the function of biological macromolecules. Intracellular polyamine metabolism is regulated by reversible acetylation and dysregulated polyamine metabolism is associated with neoplastic diseases such as colon cancer, prostate cancer and neuroblastoma. Both HDAC10 and its product spermidine are known to promote cellular survival through autophagy
physiological function
Cationic polyamines such as spermidine and spermine are critical in all forms of life, as they regulate the function of biological macromolecules. Intracellular polyamine metabolism is regulated by reversible acetylation. Both HDAC10 and its product spermidine are known to promote cellular survival through autophagy
physiological function
HDAC10 and spermidine act as mediators of autophagy
physiological function
HDAC10 and spermidine act as mediators of autophagy
additional information
nucleophilic attack of Zn2+-bound water at the amide carbonyl group polarized by Zn2+ and the catalytic tyrosine is facilitated by a general base. The Zn2+ ion, tyrosine, and tandem histidine residues contribute to transition state stabilization in each deacetylase. Collapse of the tetrahedral intermediate requires a proton donor, and the second histidine of the tandem pair must serve as the general acid due to its proximity to the leaving amino group. Structure-function analysis of substrate specificity, overview
additional information
-
nucleophilic attack of Zn2+-bound water at the amide carbonyl group polarized by Zn2+ and the catalytic tyrosine is facilitated by a general base. The Zn2+ ion, tyrosine, and tandem histidine residues contribute to transition state stabilization in each deacetylase. Collapse of the tetrahedral intermediate requires a proton donor, and the second histidine of the tandem pair must serve as the general acid due to its proximity to the leaving amino group. Structure-function analysis of substrate specificity, overview
additional information
nucleophilic attack of Zn2+-bound water at the amide carbonyl group polarized by Zn2+ and the catalytic tyrosine is facilitated by a general base. The Zn2+ ion, tyrosine, and tandem histidine residues contribute to transition state stabilization in each deacetylase. Collapse of the tetrahedral intermediate requires a proton donor, and the second histidine of the tandem pair must serve as the general acid due to its proximity to the leaving amino group. Structure-function analysis of substrate specificity, overview
additional information
-
nucleophilic attack of Zn2+-bound water at the amide carbonyl group polarized by Zn2+ and the catalytic tyrosine is facilitated by a general base. The Zn2+ ion, tyrosine, and tandem histidine residues contribute to transition state stabilization in each deacetylase. Collapse of the tetrahedral intermediate requires a proton donor, and the second histidine of the tandem pair must serve as the general acid due to its proximity to the leaving amino group. Structure-function analysis of substrate specificity, overview
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Suzuke, O.; Kumazawa, T.; Seno, H.; Matsumoto, T.
Acetylspermidine deacetylase activities in human organs
Med. Sci. Res.
15
675-676
1987
Homo sapiens
-
brenda
Wang, Z.; Fries, D.; Blankenship, J.
Effect of N8-acetylspermidine deacetylase inhibition on the growth of L1210 cells
Biochem. Pharmacol.
57
1095-1103
1999
Mus musculus
brenda
Menezes, A.M.S.; Blankenship, J.
Differentiation of PC 12 cells induced by inhibition of N8-acetylspermidine deacetylase using 7-[N-(3-aminopropyl)amino]heptan-2-one
Proc. West. Pharmacol. Soc.
36
21-24
1993
Rattus sp.
brenda
Huang, T.L.; Dredar, S.A.; Manneh, V.A.; Blankenship, J.W.; Fries, D.S.
Inhibition of N8-acetylspermidine deacetylase by active-site-directed metal coordination inhibitiors
J. Med. Chem.
35
2414-2418
1992
Rattus sp.
brenda
Marchant, P.; Manneh, V.A.; Blankenship, J.
N1-Acetylspermidine is not a substrate for N-acetylspermidine deacetylase
Biochim. Biophys. Acta
881
297-299
1986
Rattus sp.
brenda
Manneh, V.A.; Blankenship, J.
Inhibitor studies on the characteristics of the active site of rat liver N8-acetylspermidine deacetylase
Proc. West. Pharmacol. Soc.
28
255-258
1985
Rattus sp.
-
brenda
Libby, P.R.
Acetylspermidine deacetylase (rat liver)
Methods Enzymol.
94
329-331
1983
Rattus sp.
brenda
Santacroce, M.J.; Blankenship, J.
Inhibition of acetylspermidine deacetylating activity from rat liver
Proc. West. Pharmacol. Soc.
25
113-118
1982
Rattus sp.
brenda
Blankenship, J.
Deacetylation of N8-acetylspermidine by subcellular fractions of rat tissue
Arch. Biochem. Biophys.
189
20-27
1978
Rattus sp.
brenda
Libby, P.R.
Properties of an acetylspermidine deacetylase from rat liver
Arch. Biochem. Biophys.
188
360-363
1978
Rattus sp.
brenda
Decroos, C.; Bowman, C.M.; Christianson, D.W.
Synthesis and evaluation of N8-acetylspermidine analogues as inhibitors of bacterial acetylpolyamine amidohydrolase
Bioorg. Med. Chem.
21
4530-4540
2013
Mycoplana ramosa
brenda
Shinsky, S.A.; Christianson, D.W.
Polyamine deacetylase structure and catalysis prokaryotic acetylpolyamine amidohydrolase and eukaryotic HDAC10
Biochemistry
57
3105-3114
2018
Danio rerio (F1QCV2), Danio rerio, Homo sapiens (Q969S8), Homo sapiens
brenda
Hai, Y.; Shinsky, S.A.; Porter, N.J.; Christianson, D.W.
Histone deacetylase 10 structure and molecular function as a polyamine deacetylase
Nat. Commun.
8
15368
2017
Danio rerio (F1QCV2), Danio rerio, Homo sapiens (Q969S8), Homo sapiens
brenda