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Information on EC 2.3.1.286 - protein acetyllysine N-acetyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9NTG7

for references in articles please use BRENDA:EC2.3.1.286
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IUBMB Comments
The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2''-O-acetyl-ADP-D-ribose converts non-enzymically to 3''-O-acetyl-ADP-D-ribose.
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This record set is specific for:
Homo sapiens
UNIPROT: Q9NTG7
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
sirt1, sirt3, sirtuin, sirt2, sirtuin 1, sirtuin 3, sir2p, silent information regulator 2, sir2alpha, nad-dependent histone deacetylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD+-dependent protein deacetylase
-
-
-
-
protein lysine deacetylase
-
-
-
-
silent information regulator 2
-
-
SIRT1
SIRT2
SIRT3
-
-
sirtuin 1
Q96EB6
-
sirtuin-2 deacetylase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[protein]-N6-acetyl-L-lysine + NAD+ + H2O = [protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
broad specificity with respect to chain length of the acyl chain
Q8IXJ6, Q96EB6, Q9NTG7
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
[protein]-N6-acetyl-L-lysine:NAD+ N-acetyltransferase (NAD+-hydrolysing; 2''-O-acetyl-ADP-D-ribose-forming)
The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2''-O-acetyl-ADP-D-ribose converts non-enzymically to 3''-O-acetyl-ADP-D-ribose.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NAD+ + N2-benzyloxycarbonyl-N6-succinyl-L-lysine-7-amido-4-methylcoumarin
nicotinamide + N2-benzyloxycarbonyl-L-lysine-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
i.e. 3-[(5-[[(benzyloxy)carbonyl]amino]-5-[(4-methyl-2-oxo-2H-chromen-7-yl)carbamoyl]pentyl)carbamoyl]-propanoic acid
-
-
?
NAD+ + QTAR(N6-acetyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-acetyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
acetylated histone H3 peptide
-
-
?
NAD+ + QTAR(N6-butyryl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-butyryl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
butyrylated histone H3 peptide, about 5% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
show the reaction diagram
NAD+ + QTAR(N6-dodecanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-dodecanoyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
dodecanoylated histone H3 peptide, about 65% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-hexanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-hexanoyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
hexanoylated histone H3 peptide, about 20% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-octanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-octanoyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
octanoylated histone H3 peptide, about 35% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-palmitoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-palmitoyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
myristoylated histone H3 peptide, about 30% compared to the activity with the acetylated or hexanoylated peptide
-
-
?
NAD+ + QTAR(N6-propionyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-propionyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
propionylated histone H3 peptide, about 10% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-succinyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-succinyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
succinylated histone H3 peptide, about 10% compared to the activity with the acetylated peptide
-
-
?
NAD+ + TRSG(N6-acetyl)KVMR
nicotinamide + TRSGKVMR + 2'-O-acetyl-ADP-ribose
show the reaction diagram
peptide based on an acetyl-CoA synthetase 2 acetylation site
-
-
?
NAD+ + TRSG(N6-acetyl)KVMRRLLR
nicotinamide + TRSGKVMRRLLR + 2'-O-acetyl-ADP-ribose
show the reaction diagram
Q96EB6, Q9NTG7
acetylated substrate peptide based on the sequence of acetyl-coenzyme A synthetase 2
-
-
?
NAD+ + [chicken erythrocyte histone]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
-
-
?
NAD+ + [glutamate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glutamate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [glutamate oxaloacetate transaminase 2]-N6-acetyl-L-lysine
nicotinamide + [glutamate oxaloacetate transaminase 2]-L-lysine + 2'-O-acyl-ADP-ribose
show the reaction diagram
isoform SIRT3 is the major deacetylase of glutamate oxaloacetate transaminase 2
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
-
-
-
?
KSTGGK(Ac)APRKQ + beta-2'-deoxy-2'-fluororibo-NAD+ + H2O
?
show the reaction diagram
-
the rates with beta-2'-deoxy-2'-fluororibo-NAD+ are about 1200fold slower than the exchange rates determined with NAD+ under similar conditions
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-
?
KSTGGK(Ac)APRKQ + NAD+ + H2O
KSTGGKAPRKQ + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
-
an 11-mer histone H3 peptide
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-
?
NAD+ + N2-benzyloxycarbonyl-N6-succinyl-L-lysine-7-amido-4-methylcoumarin
nicotinamide + N2-benzyloxycarbonyl-L-lysine-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
i.e. 3-[(5-[[(benzyloxy)carbonyl]amino]-5-[(4-methyl-2-oxo-2H-chromen-7-yl)carbamoyl]pentyl)carbamoyl]-propanoic acid
-
-
?
NAD+ + QTAR(N6-acetyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-acetyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
acetylated histone H3 peptide
-
-
?
NAD+ + QTAR(N6-butyryl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-butyryl-ADP-ribose
show the reaction diagram
NAD+ + QTAR(N6-crotonyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-crotonyl-ADP-ribose
show the reaction diagram
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
show the reaction diagram
NAD+ + QTAR(N6-dodecanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-dodecanoyl-ADP-ribose
show the reaction diagram
NAD+ + QTAR(N6-hexanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-hexanoyl-ADP-ribose
show the reaction diagram
NAD+ + QTAR(N6-myristoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
myristoylated histone H3 peptide, about 45% compared to the activity with the acetylated or hexanoylated peptide
-
-
?
NAD+ + QTAR(N6-octanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-octanoyl-ADP-ribose
show the reaction diagram
NAD+ + QTAR(N6-propionyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-propionyl-ADP-ribose
show the reaction diagram
NAD+ + TRSG(N6-acetyl)KVMRRLLR
nicotinamide + TRSGKVMRRLLR + 2'-O-acetyl-ADP-ribose
show the reaction diagram
Q96EB6, Q9NTG7
acetylated substrate peptide based on the sequence of acetyl-coenzyme A synthetase 2
-
-
?
NAD+ + [alpha-tubulin peptide]-N6-acetyl-L-lysine
nicotinamide + [alpha-tubulin peptide]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [alpha-tubulin]-N6-acetyl-L-lysine40
nicotinamide + [alpha-tubulin]-L-lysine40 + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
-
-
?
NAD+ + [alpha-tubulin]-N6-acyl-L-lysine
nicotinamide + [alpha-tubulin]-L-lysine + 2'-O-acyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [BHJH-TM1 protein]-N6-myristoyl-L-lysine
nicotinamide + [BHJH-TM1 protein]-L-lysine + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [BMAL1 protein]-N6-acyl-L-lysine
nicotinamide + [BMAL1 protein]-L-lysine + 2'-O-acyl-ADP-ribose
show the reaction diagram
Q96EB6
-
-
-
?
NAD+ + [DNA repair factor Ku70]-N6-acetyl-L-lysine382
nicotinamide + [DNA repair factor Ku70]-L-lysine382 + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [Fluor de Lys]-N6-acetyl-L-lysine
nicotinamide + [Fluor de Lys]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
Q96EB6
Fluor de Lys is a fluorogenic, acetylated peptide substrate for human sirtuin 1, based on residues 379-382 of p53 (Arg-His-Lys-Lys(Ac)), a site of regulatory acetylation by the p300 and CBP acetyltransferases
-
-
?
NAD+ + [histone H2B]-N6-acetyl-L-lysine12
nicotinamide + [histone H2B]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [histone H2B]-N6-myristoyl-L-lysine12
nicotinamide + [histone H2B]-L-lysine + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine9
nicotinamide + [histone H3]-L-lysine9 + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [histone H3]-N6-myristoyl-L-lysine9
nicotinamide + [histone H3]-L-lysine + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine16
nicotinamide + [histone H4]-L-lysine16 + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [histone H4]-N6-acetyl-L-lysine8
nicotinamide + [histone H4]-L-lysine8 + 2'-O-acetyl-ADP-ribose
show the reaction diagram
deacetylated at high concentrations of enzyme
-
-
?
NAD+ + [histone H4]-N6-myristoyl-L-lysine16
nicotinamide + [histone H4]-L-lysine + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [nuclear receptor LXRalpha]-N6-acetyl-L-lysine432
nicotinamide + [nuclear receptor LXRalpha]-L-lysine432 + 2'-O-acetyl-ADP ribose
show the reaction diagram
Q96EB6
-
-
-
?
NAD+ + [nuclear receptor LXRbeta]-N6-acetyl-L-lysine433
nicotinamide + [nuclear receptor LXRbeta]-L-lysine433 + 2'-O-acetyl-ADP ribose
show the reaction diagram
Q96EB6
-
-
-
?
NAD+ + [nuclear receptor LXR]-N6-acetyl-L-lysine
nicotinamide + [nuclear receptor LXR]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
Q96EB6
SIRT1 positively regulates liver X receptors (LXRs) by deacetylation at lysine. Deacetylation of liver X receptors (LXRs) by SIRT1 may be a mechanism that affects atherosclerosis and other agingassociated diseases
-
-
?
NAD+ + [p53 protein]-N6-acetyl-L-lysine
nicotinamide + [p53 protein]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [p53 protein]-N6-acetyl-L-lysine382
nicotinamide + [p53 protein]-L-lysine382 + 2'-O-acetyl-ADP ribose
show the reaction diagram
NAD+ + [PER2 protein]-N6-acetyl-L-lysine
nicotinamide + [PER2 protein]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
show the reaction diagram
NAD+ + [protein]-N6-myristoyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
demyristoylase activity of SIRT2 is 5fold more efficient than its deacetylase activity
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
-
-
-
?
NAD+ + [thymine DNA glycosylase]-N6-acetyl-L-lysine
nicotinamide + [thymine DNA glycosylase]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
[alpha-tubulin]-N6-acetyl-L-lysine40 + NAD+ + H2O
[alpha-tubulin]-L-lysine40 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
-
-
-
?
[histone H3]-N6-acetyl-L-lysine + NAD+ + H2O
[histone H3]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD+ + [chicken erythrocyte histone]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
-
-
?
NAD+ + [glutamate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glutamate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
Sirt3 can deacetylate and thereby activate a central metabolic regulator in the mitochondrial matrix, glutamate dehydrogenase
-
-
?
NAD+ + [glutamate oxaloacetate transaminase 2]-N6-acetyl-L-lysine
nicotinamide + [glutamate oxaloacetate transaminase 2]-L-lysine + 2'-O-acyl-ADP-ribose
show the reaction diagram
isoform SIRT3 is the major deacetylase of glutamate oxaloacetate transaminase 2
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
Sirt3 can deacetylate and activate isocitrate dehydrogenase 2, an enzyme that promotes regeneration of antioxidants and catalyzes a key regulation point of the citric acid cycle
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-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
-
-
-
?
NAD+ + [alpha-tubulin]-N6-acyl-L-lysine
nicotinamide + [alpha-tubulin]-L-lysine + 2'-O-acyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [BMAL1 protein]-N6-acyl-L-lysine
nicotinamide + [BMAL1 protein]-L-lysine + 2'-O-acyl-ADP-ribose
show the reaction diagram
Q96EB6
-
-
-
?
NAD+ + [DNA repair factor Ku70]-N6-acetyl-L-lysine382
nicotinamide + [DNA repair factor Ku70]-L-lysine382 + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [histone H4]-N6-acetyl-L-lysine16
nicotinamide + [histone H4]-L-lysine16 + 2'-O-acetyl-ADP-ribose
show the reaction diagram
the deacetylation of [histone H4]-N6-acetyl-L-lysine16 may be pivotal to the formation of condensed chromatin
-
-
?
NAD+ + [nuclear receptor LXR]-N6-acetyl-L-lysine
nicotinamide + [nuclear receptor LXR]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
Q96EB6
SIRT1 positively regulates liver X receptors (LXRs) by deacetylation at lysine. Deacetylation of liver X receptors (LXRs) by SIRT1 may be a mechanism that affects atherosclerosis and other agingassociated diseases
-
-
?
NAD+ + [p53 protein]-N6-acetyl-L-lysine
nicotinamide + [p53 protein]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
Q96EB6
SIRT1 deacetylase is a negative regulator of p53 function capable of modulating cellular senescence
-
-
?
NAD+ + [p53 protein]-N6-acetyl-L-lysine382
nicotinamide + [p53 protein]-L-lysine382 + 2'-O-acetyl-ADP ribose
show the reaction diagram
Q96EB6
Sir2 is involved in the regulation of p53 function via deacetylation
-
-
?
NAD+ + [PER2 protein]-N6-acetyl-L-lysine
nicotinamide + [PER2 protein]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
Q96EB6
SIRT1 regulates circadian clock gene expression through PER2 deacetylation
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
show the reaction diagram
NAD+ + [protein]-N6-myristoyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
demyristoylase activity of SIRT2 is 5fold more efficient than its deacetylase activity
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
show the reaction diagram
Q8IXJ6, Q96EB6, Q9NTG7
-
-
-
?
NAD+ + [thymine DNA glycosylase]-N6-acetyl-L-lysine
nicotinamide + [thymine DNA glycosylase]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
Q96EB6
deacetylation and stimulation of the thymine DNA glycosylase activity by SIRT1 enhances DNA demethylation
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
contains Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(5E)-5-(1H-indol-3-ylmethylidene)-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
17% inhibition at 0.05 mM
(5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
13% inhibition at 0.05 mM
(5E)-5-[4-(benzyloxy)benzylidene]-1-ethyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
25% inhibition at 0.05 mM
(5E)-5-[4-(benzyloxy)benzylidene]-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
22% inhibition at 0.05 mM
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
41% inhibition at 0.05 mM
2-[1-[3-(amidinothio)propyl]-1H-indol-3-yl]-3-(1-methylindol-3-yl)maleimide methanesulfonate
Q8IXJ6, Q96EB6, Q9NTG7
i.e. Ro 31-8220
5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
14% inhibition at 0.05 mM
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[(1-benzyl-1H-indol-3-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[4-(propan-2-yl)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
13% inhibition at 0.05 mM
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
30% inhibition at 0.05 mM
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
Q8IXJ6, Q96EB6, Q9NTG7
i.e. EX-527
Isonicotinamide
Q96EB6, Q9NTG7
weak competitive inhibitor of hSIRT3 with respect to NAD+ in vitro
nicotinamide
resveratrol
inhibits deacetylase activity
sirtinol
Q8IXJ6, Q96EB6, Q9NTG7
24% inhibition at 0.05 mM
(4R)-1-(tert-butoxycarbonyl)-4-hydroxyprolyl-N-benzyl-N6-ethanethioyl-L-lysinamide
Q96EB6
0.05 mM, 83.4% inhibition
(4R)-1-(tert-butoxycarbonyl)-N-[(2S)-6-(ethanethioylamino)-1-oxo-1-[(2-oxo-2-phenylethyl)amino]hexan-2-yl]-4-hydroxyprolinamide
Q96EB6
0.05 mM, 97.1% inhibition
(4R)-4-hydroxyprolyl-N-benzyl-N6-ethanethioyl-L-lysinamide
Q96EB6
0.05 mM, 89.3% inhibition
(4R)-N-[(2S)-6-(ethanethioylamino)-1-oxo-1-[(2-oxo-2-phenylethyl)amino]hexan-2-yl]-4-hydroxyprolinamide
Q96EB6
0.05 mM, 96.8% inhibition
(5E)-1-ethyl-5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
(5E)-5-(1H-indol-3-ylmethylidene)-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
(5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
(5E)-5-[4-(benzyloxy)benzylidene]-1-ethyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
(5E)-5-[4-(benzyloxy)benzylidene]-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
1-(tert-butoxycarbonyl)prolyl-N-benzyl-N6-ethanethioyl-L-lysinamide
Q96EB6
0.05 mM, 93.7% inhibition
2-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-cyano-2-fluorophenyl)isonicotinamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1 and SIRT3
2-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-cyanophenyl)isonicotinamide
selective inhibitor for SIRT2, low inhibition of SIRT1 and SIRT3
2-[1-[3-(amidinothio)propyl]-1H-indol-3-yl]-3-(1-methylindol-3-yl)maleimide methanesulfonate
Q8IXJ6, Q96EB6, Q9NTG7
i.e. Ro 31-8220
3-((2-methoxynaphthalen-1-yl)methyl)-7-((2-methylbenzyl)amino)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
-
3-((2-methoxynaphthalen-1-yl)methyl)-7-((pyridin-3-ylmethyl)amino)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
i.e. ICL-SIRT078, a substrate-competitive SIRT2 inhibitor with more than 50fold selectivity against SIRT1, 3 and 5. Treatment of MCF-7 breast cancer cells with ICL-SIRT078 results in hyperacetylation of alpha-tubulin, an established SIRT2 biomarker, at doses comparable with the biochemical IC50 data, while suppressing MCF-7 proliferation at higher concentrations
3-((2-methoxynaphthalen-1-yl)methyl)-7-((thiophen-2-ylmethyl)-amino)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
-
3-((2-methoxynaphthalen-1-yl)methyl)-7-(neopentylamino)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
-
3-(azepan-1-ylsulfonyl)-N-(3-nitrophenyl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1 and SIRT3
3-(N-(4-acetylphenyl)-N-methylsulfamoyl)-N-(4-chlorophenyl)benzamide
highly selective inhibitor for SIRT2, no inhibition of SIRT1, low inhibition of and SIRT3
3-(N-(4-acetylphenyl)-N-methylsulfamoyl)-N-(4-cyanophenyl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1 and SIRT3
3-(N-(4-acetylphenyl)-N-methylsulfamoyl)-N-(5-chloropyridin-2-yl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1, no inhibition of and SIRT3
3-(N-(4-bromophenyl)-N-methylsulfamoyl)-N-(4-chloro-2-fluorophenyl)-N-methylbenzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1 and SIRT3
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-(methylsulfinyl)phenyl)benzamide
highly selective inhibitor for SIRT2, no inhibition of SIRT1, low inhibition of and SIRT3
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-(methylsulfonyl)phenyl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1 and SIRT3
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-cyano-2-fluorophenyl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1 and SIRT3
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-cyanophenyl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1, no inhibition of and SIRT3
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(5-cyanopyridin-2-yl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1, no inhibition of and SIRT3
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(5-fluoropyridin-2-yl)benzamide
highly selective inhibitor for SIRT2, no inhibition of SIRT1 and SIRT3
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(6-chloropyridazin-3-yl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1
3-(N-(5-chloropyridin-2-yl)-N-methylsulfamoyl)-N-(4-cyanophenyl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1 and SIRT3
4-bromo-N-(3-(N-methyl-N-(4-(methylsulfonyl)phenyl)sulfamoyl)phenyl)benzamide
selective inhibitor for SIRT2, low inhibition of SIRT1 and SIRT3
5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[(1-benzyl-1H-indol-3-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[4-(propan-2-yl)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Q8IXJ6, Q96EB6, Q9NTG7
-
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
7-((3-fluorobenzyl)amino)-3-((2-methoxynaphthalen-1-yl)methyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
-
7-((3-methoxybenzyl)amino)-3-((2-methoxynaphthalen-1-yl)-methyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
-
7-(benzylamino)-3-((2-methoxynaphthalen-1-yl)methyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
-
cambinol
EX-527
Ex257
Q96EB6
specific inhibitor of isoform SIRT1
Isonicotinamide
Q96EB6, Q9NTG7
weak inhibitor
macrocyclic peptide inhibitor S2iL5
the inhibitor binds to the active site of SIRT2 through extensive interactions. The inhibitor induces an open-to-closed domain movement and a helix-to-coil transition in a SIRT2-specific region
-
meta-azi-propofol
only binds specifically and competitively to the enzyme when co-equilibrated with other substrates
methyl N2-(tert-butoxycarbonyl)-N6-ethanethioyl-L-lysyl-D-alaninate
Q96EB6
0.05 mM, 81.3% inhibition
N-(3-(N-(4-chlorophenyl)-N-methylsulfamoyl)phenyl)-4-cyanobenzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1, no inhibition of and SIRT3
N-(4-acetylphenyl)-3-(N-(4-acetylphenyl)-N-methylsulfamoyl)benzamide
highly selective inhibitor for SIRT2, no inhibition of SIRT1 and SIRT3
N-(4-bromo-2-fluorophenyl)-3-(N-(4-bromophenyl)-N-methylsulfamoyl)-N-methylbenzamide
highly selective inhibitor for SIRT2, no inhibition of SIRT1 and SIRT3
N-(4-chlorophenyl)-3-(N-methyl-N-(4-(methylsulfonyl)phenyl)sulfamoyl)benzamide
highly selective inhibitor for SIRT2, no inhibition of SIRT1 and SIRT3
N-(4-cyanophenyl)-3-(N-(4-(1-hydroxyethyl)phenyl)-N-methylsulfamoyl)benzamide
-
N-(4-cyanophenyl)-3-(N-(4-fluorophenyl)-N-methylsulfamoyl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1 and SIRT3
N-(4-cyanophenyl)-3-(N-(4-methoxyphenyl)-N-methylsulfamoyl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1 and SIRT3
N-(4-cyanophenyl)-3-(N-methyl-N-(4-(methylsulfonyl)phenyl)sulfamoyl)benzamide
highly selective inhibitor for SIRT2, low inhibition of SIRT1, no inhibition of and SIRT3
N-methyl-N-nitrosourea
Q96EB6
-
N-[(2S)-6-(ethanethioylamino)-1-oxo-1-[(2-oxo-2-phenylethyl)amino]hexan-2-yl]-5-oxoprolinamide
Q96EB6
0.05 mM, 98.2% inhibition
N-[(2S)-6-(ethanethioylamino)-1-[[2-(morpholin-4-yl)ethyl]amino]-1-oxohexan-2-yl]-6-oxoheptanamide
Q96EB6
0.05 mM, 61.1% inhibition
N2-(tert-butoxycarbonyl)-N6-ethanethioyl-N-[2-(4-methoxyphenyl)-2-oxoethyl]-L-lysinamide
Q96EB6
0.05 mM, 95.6% inhibition
N2-(tert-butoxycarbonyl)-N6-ethanethioyl-N-[2-(morpholin-4-yl)ethyl]-L-lysinamide
Q96EB6
0.05 mM, 37.5% inhibition
N2-[(benzyloxy)carbonyl]-N6-ethanethioyl-N-[2-(morpholin-4-yl)ethyl]-L-lysinamide
Q96EB6
0.05 mM, 54.9% inhibition
N6-ethanethioyl-N2-(6-oxoheptanoyl)-N-(2-oxo-2-phenylethyl)-L-lysinamide
Q96EB6
0.05 mM, 97.7% inhibition
nicotinamide
prolyl-N-benzyl-N6-ethanethioyl-L-lysinamide
Q96EB6
0.05 mM, 94.8% inhibition
propofol
only binds specifically and competitively to the enzyme when co-equilibrated with other substrates
sirtinol
splitomicin
-
suramin
Q8IXJ6, Q96EB6, Q9NTG7
-
tenovin-1
-
tenovin-6
-
[histone H3]-difluoroacetyl-L-lysine
-
-
-
[histone H3]-monofluoroacetyl-L-lysine
-
-
-
[histone H3]-thioacetyl-L-lysine
-
most potent inhibitor
-
[histone H3]-trifluoroacetyl-L-lysine
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
[histone H3]-N6-acetyl-L-lysine9
at pH 8.0 and 37°C
0.00024
[histone H3]-N6-myristoyl-L-lysine9
at pH 8.0 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.275
[histone H3]-N6-acetyl-L-lysine9
at pH 8.0 and 37°C
0.018
[histone H3]-N6-myristoyl-L-lysine9
at pH 8.0 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.5
[histone H3]-N6-acetyl-L-lysine9
at pH 8.0 and 37°C
74
[histone H3]-N6-myristoyl-L-lysine9
at pH 8.0 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00062
3-((2-methoxynaphthalen-1-yl)methyl)-7-((pyridin-3-ylmethyl)amino)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
pH 7.5, temperature not specified in the publication
0.0339
nicotinamide
-
at pH 7.5 and 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0037
2-[1-[3-(amidinothio)propyl]-1H-indol-3-yl]-3-(1-methylindol-3-yl)maleimide methanesulfonate
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0403
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.116
5-[(1-benzyl-1H-indol-3-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0433
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0293
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0464
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0303
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.049
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
13800
Isonicotinamide
Homo sapiens
Q96EB6, Q9NTG7
pH 8, 37°C, weak competitive inhibitor of hSIRT3 with respect to NAD+ in vitro
0.03 - 0.043
nicotinamide
0.0144
(5E)-5-[4-(benzyloxy)benzylidene]-1-ethyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.01
(5E)-5-[4-(benzyloxy)benzylidene]-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0097
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0102
2-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-cyano-2-fluorophenyl)isonicotinamide
Homo sapiens
pH and temperature not specified in the publication
0.0049
2-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-cyanophenyl)isonicotinamide
Homo sapiens
pH and temperature not specified in the publication
0.0008 - 0.0035
2-[1-[3-(amidinothio)propyl]-1H-indol-3-yl]-3-(1-methylindol-3-yl)maleimide methanesulfonate
0.0172
3-((2-methoxynaphthalen-1-yl)methyl)-7-((2-methylbenzyl)amino)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
Homo sapiens
pH 7.5, temperature not specified in the publication
0.00145
3-((2-methoxynaphthalen-1-yl)methyl)-7-((pyridin-3-ylmethyl)amino)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
Homo sapiens
pH 7.5, temperature not specified in the publication
0.006
3-((2-methoxynaphthalen-1-yl)methyl)-7-((thiophen-2-ylmethyl)-amino)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
Homo sapiens
pH 7.5, temperature not specified in the publication
0.00652
3-((2-methoxynaphthalen-1-yl)methyl)-7-(neopentylamino)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
Homo sapiens
pH 7.5, temperature not specified in the publication
0.0108
3-(azepan-1-ylsulfonyl)-N-(3-nitrophenyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0068
3-(N-(4-acetylphenyl)-N-methylsulfamoyl)-N-(4-chlorophenyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0073
3-(N-(4-acetylphenyl)-N-methylsulfamoyl)-N-(4-cyanophenyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0132
3-(N-(4-acetylphenyl)-N-methylsulfamoyl)-N-(5-chloropyridin-2-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0075
3-(N-(4-bromophenyl)-N-methylsulfamoyl)-N-(4-chloro-2-fluorophenyl)-N-methylbenzamide
Homo sapiens
pH and temperature not specified in the publication
0.0095
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-(methylsulfinyl)phenyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0098
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-(methylsulfonyl)phenyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0066
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-cyano-2-fluorophenyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0061
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(4-cyanophenyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0199
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(5-cyanopyridin-2-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0091
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(5-fluoropyridin-2-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0156
3-(N-(4-chlorophenyl)-N-methylsulfamoyl)-N-(6-chloropyridazin-3-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0061
3-(N-(5-chloropyridin-2-yl)-N-methylsulfamoyl)-N-(4-cyanophenyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0063
4-bromo-N-(3-(N-methyl-N-(4-(methylsulfonyl)phenyl)sulfamoyl)phenyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0203
5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0087
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0117
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0098
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0147
5-[4-(propan-2-yl)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0075
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0034
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0104
5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
Q8IXJ6, Q96EB6, Q9NTG7
pH 8.0, 37°C
0.0001 - 0.033
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
0.004
7-((3-fluorobenzyl)amino)-3-((2-methoxynaphthalen-1-yl)methyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
Homo sapiens
pH 7.5, temperature not specified in the publication
0.0019
7-((3-methoxybenzyl)amino)-3-((2-methoxynaphthalen-1-yl)-methyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
Homo sapiens
pH 7.5, temperature not specified in the publication
0.0211
7-(benzylamino)-3-((2-methoxynaphthalen-1-yl)methyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one
Homo sapiens
pH 7.5, temperature not specified in the publication
0.056 - 0.059
cambinol
12200
Isonicotinamide
Homo sapiens
Q96EB6, Q9NTG7
pH 8, 37°C, weak inhibitor
0.0038
N-(3-(N-(4-chlorophenyl)-N-methylsulfamoyl)phenyl)-4-cyanobenzamide
Homo sapiens
pH and temperature not specified in the publication
0.0189
N-(4-acetylphenyl)-3-(N-(4-acetylphenyl)-N-methylsulfamoyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0069
N-(4-bromo-2-fluorophenyl)-3-(N-(4-bromophenyl)-N-methylsulfamoyl)-N-methylbenzamide
Homo sapiens
pH and temperature not specified in the publication
0.0159
N-(4-chlorophenyl)-3-(N-methyl-N-(4-(methylsulfonyl)phenyl)sulfamoyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0115
N-(4-cyanophenyl)-3-(N-(4-(1-hydroxyethyl)phenyl)-N-methylsulfamoyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0094
N-(4-cyanophenyl)-3-(N-(4-fluorophenyl)-N-methylsulfamoyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0096
N-(4-cyanophenyl)-3-(N-(4-methoxyphenyl)-N-methylsulfamoyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0095
N-(4-cyanophenyl)-3-(N-methyl-N-(4-(methylsulfonyl)phenyl)sulfamoyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0012 - 0.1
nicotinamide
0.037 - 0.131
sirtinol
0.0003 - 0.02
suramin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
assay at
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Q96EB6
-
Manually annotated by BRENDA team
Q96EB6
-
Manually annotated by BRENDA team
Q96EB6
fetal lung cell
Manually annotated by BRENDA team
Q96EB6
-
Manually annotated by BRENDA team
Q96EB6
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Q96EB6
SIRT1 and p53 colocalize in nuclear bodies (punctate structures found in the nuclei of certain cells) upon upregulation of the promyelocytic leukemia protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme can regulate flux and anapleurosis of this central metabolic cycle
malfunction
Q96EB6
SIRT1 depletion by RNA interference attenuates capsaicin-induced apoptosis in A-549 cancer cells and autophagy in MRC-5 cells
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SIR3_HUMAN
399
0
43573
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
x * 37000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of Sirt3 in complex with fluor-de-Lys peptide and resveratrol and crystal structure of Sirt3 in complex with fluor-de-Lys peptide and piceatannol
in complex with ADP ribose, microseed matrix seeding, using 25% (w/v) PEG 3350, 0.2 M MgCl2 in 0.1 M bis-Tris buffer pH 5.5
crystallization at 4°C by the sitting-drop vapor diffusion method. Crystal structure of human SIRT2 in complex with a macrocyclic peptide inhibitor S2iL5, at 2.5 A resolution
hanging drop vapor diffusion using a 1:1 drop ratio. The 2.5 A crystal structure of the SIRT1 catalytic domain bound to NAD+ and 6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide (EX527)
Q96EB6
in complex with ADP ribose, microseed matrix seeding, using 17.5% (w/v) PEG 10000, 0.1 M ammonium acetate in 0.1 M bis-Tris buffer pH 6.8 at 20°C
in complex with BHJH-TM1 protein, hanging drop vapor diffusion method, using 25% (w/v) PEG 3350, 0.1 M HEPES buffer, pH 7.5
recombinant sirtuin 1 comprising residues 140–747 is crystallized using the hanging-drop vapour diffusion method. The crystal diffracted to 3.4 A resolution and belong to space group P622, with unit-cell parameters a = b = 203.1, c = 625.3 A , and is estimated to contain between six and 12 molecules per asymmetric unit
Q96EB6
Sirt2 is crystallized in complex with the product analog, ADP-ribose, and this crystal structure is solved at 2.3 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex S75 gel filtration
HisTrap column chromatography and Superdex S75 gel filtration
Ni-NTA column chromatography and Superdex G200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) CodonPlus RIPL cells
expression in Escherichia coli
a gene encoding the C-terminally His-tagged SIRT1 catalytic domain is expressed in SF9 cells
Q96EB6
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) CodonPlus RIPL cells
expression in Escherichia coli
Q96EB6
recombinant human SIRT2 (43-356) is expressed as a His-Sumo fusion protein in Escherichia coli
SIRT1-FL (full-length human SIRT1) is cloned in the pECE vector (clone 1791) and N-terminally truncated SIRT1 (SIRT1-NT with residues 7–83 deleted) cloned in the pCDNA3.1 vector. To express the FLAGtagged hSIRT1 (human SIRT1) proteins, the hSIRT1 constructs are transfected into HEK (human embryonic kidney)-293T cells
Q96EB6
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
down-regulation of intratumoral and peritumoral Sirt3 are both associated with poor outcome in hepatocellular carcinoma
expression of SIRT3 shows a strong negative correlation with the progression of Alzheimer’s disease
isoform SIRT3 expression is reduced in human pancreatic tumors
expression of SIRT1 is induced in human cells that are treated with human serum. Insulin and insulin-like growth factor 1 (IGF-1) attenuate this response
Q96EB6
isoform SIRT1 mRNA is upregulated in chronic lymphocytic leukemia
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
down-regulation of intratumoral and peritumoral Sirt3 are both associated with poor outcome in hepatocellular carcinoma. Intratumoral Sirt3 is a favorable prognostic predictor in early stage patients
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Holbourn, K.P.; Lloyd, M.D.; Thompson, A.S.; Threadgill, M.D.; Acharya, K.R.
Cloning, purification, crystallization and preliminary crystallographic analysis of the human histone deacetylase sirtuin 1
Acta Crystallogr. Sect. F
67
461-463
2011
Homo sapiens (Q96EB6), Homo sapiens
Manually annotated by BRENDA team
Maurer, B.; Rumpf, T.; Scharfe, M.; Stolfa, D.A.; Schmitt, M.L.; He, W.; Verdin, E.; Sippl, W.; Jung, M.
Inhibitors of the NAD(+)-dependent protein desuccinylase and demalonylase Sirt5
ACS Med. Chem. Lett.
3
1050-1053
2012
Homo sapiens (Q8IXJ6), Homo sapiens (Q96EB6), Homo sapiens (Q9NTG7)
Manually annotated by BRENDA team
Madabushi, A.; Hwang, B.J.; Jin, J.; Lu, A.L.
Histone deacetylase SIRT1 modulates and deacetylates DNA base excision repair enzyme thymine DNA glycosylase
Biochem. J.
456
89-98
2013
Homo sapiens (Q96EB6), Homo sapiens
Manually annotated by BRENDA team
Wang, J.X.; Yi, Y.; Li, Y.W.; Cai, X.Y.; He, H.W.; Ni, X.C.; Zhou, J.; Cheng, Y.F.; Jin, J.J.; Fan, J.; Qiu, S.J.
Down-regulation of sirtuin 3 is associated with poor prognosis in hepatocellular carcinoma after resection
BMC Cancer
14
297
2014
Homo sapiens (Q9NTG7)
Manually annotated by BRENDA team
Vaziri, H.; Dessain, S.K.; Ng Eaton, E.; Imai, S.I.; Frye, R.A.; Pandita, T.K.; Guarente, L.; Weinberg, R.A.
hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
Cell
107
149-159
2001
Homo sapiens (Q96EB6)
Manually annotated by BRENDA team
Asher, G.; Gatfield, D.; Stratmann, M.; Reinke, H.; Dibner, C.; Kreppel, F.; Mostoslavsky, R.; Alt, F.W.; Schibler, U.
SIRT1 regulates circadian clock gene expression through PER2 deacetylation
Cell
134
317-328
2008
Homo sapiens (Q96EB6)
Manually annotated by BRENDA team
Di Fruscia, P.; Zacharioudakis, E.; Liu, C.; Moniot, S.; Laohasinnarong, S.; Khongkow, M.; Harrison, I.F.; Koltsida, K.; Reynolds, C.R.; Schmidtkunz, K.; Jung, M.; Chapman, K.L.; Steegborn, C.; Dexter, D.T.; Sternberg, M.J.; Lam, E.W.; Fuchter, M.J.
The discovery of a highly selective 5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one SIRT2 inhibitor that is neuroprotective in an in vitro Parkinson's disease model
ChemMedChem
10
69-82
2015
Homo sapiens (Q8IXJ6)
Manually annotated by BRENDA team
Langley, E.; Pearson, M.; Faretta, M.; Bauer, U.M.; Frye, R.A.; Minucci, S.; Pelicci, P.G.; Kouzarides, T.
Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
EMBO J.
21
2383-2396
2002
Homo sapiens (Q96EB6), Homo sapiens
Manually annotated by BRENDA team
Khanfar, M.A.; Quinti, L.; Wang, H.; Choi, S.H.; Kazantsev, A.G.; Silverman, R.B.
Development and characterization of 3-(benzylsulfonamido)benzamides as potent and selective SIRT2 inhibitors
Eur. J. Med. Chem.
76
414-426
2014
Homo sapiens (Q8IXJ6), Homo sapiens
Manually annotated by BRENDA team
Kokkonen, P.; Mellini, P.; Nyrhil, O.; Rahnasto-Rilla, M.; Suuronen, T.; Kiviranta P.; Huhtiniemi, T.; Poso, A.; Jarho, E.; Lahtela-Kakkonen, M.
Quantitative insights for the design of substrate-based SIRT1 inhibitors
Eur. J. Pharm. Sci.
59
12-19
2014
Homo sapiens (Q96EB6), Homo sapiens
Manually annotated by BRENDA team
Jeong, J.; Juhn, K.; Lee, H.; Kim, S.H.; Min, B.H.; Lee, K.M.; Cho, M.H.; Park, G.H.; Lee, K.H.
SIRT1 promotes DNA repair activity and deacetylation of Ku70
Exp. Mol. Med.
39
8-13
2007
Homo sapiens (Q96EB6), Homo sapiens
Manually annotated by BRENDA team
Vaquero, A.; Scher, M.B.; Lee, D.H.; Sutton, A.; Cheng, H.L.; Alt, F.W.; Serrano, L.; Sternglanz, R.; Reinberg, D.
SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis
Genes Dev.
20
1256-1261
2006
Homo sapiens (Q8IXJ6)
Manually annotated by BRENDA team
Feldman, J.L.; Baeza, J.; Denu, J.M.
Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins
J. Biol. Chem.
288
31350-31356
2013
Homo sapiens (Q8IXJ6), Homo sapiens (Q96EB6), Homo sapiens (Q9NTG7)
Manually annotated by BRENDA team
Zhao, X.; Allison, D.; Condon, B.; Zhang, F.; Gheyi, T.; Zhang, A.; Ashok, S.; Russell, M.; MacEwan, I.; Qian, Y.; Jamison, J.A.; Luz, J.G.
The 2.5 A crystal structure of the SIRT1 catalytic domain bound to nicotinamide adenine dinucleotide (NAD+) and an indole (EX527 analogue) reveals a novel mechanism of histone deacetylase inhibition
J. Med. Chem.
56
963-969
2013
Homo sapiens (Q96EB6), Homo sapiens
Manually annotated by BRENDA team
Schlicker, C.; Gertz, M.; Papatheodorou, P.; Kachholz, B.; Becker, C.F.; Steegborn, C.
Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
J. Mol. Biol.
382
790-801
2008
Homo sapiens (Q9NTG7), Homo sapiens
Manually annotated by BRENDA team
Moniot, S.; Schutkowski, M.; Steegborn, C.
Crystal structure analysis of human Sirt2 and its ADP-ribose complex
J. Struct. Biol.
182
136-143
2013
Homo sapiens (Q8IXJ6), Homo sapiens
Manually annotated by BRENDA team
Li, X.; Zhang, S.; Blander, G.; Tse, J.G.; Krieger, M.; Guarente, L.
SIRT1 deacetylates and positively regulates the nuclear receptor LXR
Mol. Cell.
28
91-106
2007
Homo sapiens (Q96EB6)
Manually annotated by BRENDA team
Lutz, M.I.; Milenkovic, I.; Regelsberger, G.; Kovacs, G.G.
Distinct patterns of sirtuin expression during progression of Alzheimer's disease
Neuromolecular Med.
16
405-414
2014
Homo sapiens (Q9NTG7)
Manually annotated by BRENDA team
Guan, X.; Lin, P.; Knoll, E.; Chakrabarti, R.
Mechanism of inhibition of the human sirtuin enzyme SIRT3 by nicotinamide: computational and experimental studies
PLoS One
15
e107729
2014
Homo sapiens (Q96EB6), Homo sapiens (Q9NTG7), Homo sapiens
Manually annotated by BRENDA team
Fischer, F.; Gertz, M.; Suenkel, B.; Lakshminarasimhan, M.; Schutkowski, M.; Steegborn, C.
Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition
PLoS One
7
e45098
2012
Homo sapiens (Q9NTG7), Homo sapiens
Manually annotated by BRENDA team
Gertz, M.; Nguyen, G.T.; Fischer, F.; Suenkel, B.; Schlicker, C.; Frnzel, B.; Tomaschewski, J.; Aladini, F.; Becker, C.; Wolters, D.; Steegborn, C.
A molecular mechanism for direct sirtuin activation by resveratrol
PLoS One
7
e49761
2012
Homo sapiens (Q9NTG7), Homo sapiens
Manually annotated by BRENDA team
Onyango, P.; Celic, I.; McCaffery, J.M.; Boeke, J.D.; Feinberg, A.P.
SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria
Proc. Natl. Acad. Sci. USA
99
13653-13658
2002
Homo sapiens (Q9NTG7), Homo sapiens
Manually annotated by BRENDA team
Cohen, H.Y.; Miller, C.; Bitterman, K.J.; Wall, N.R.; Hekking, B.; Kessler, B.; Howitz, K.T.; Gorospe, M.; de Cabo, R.; Sinclair, D.A.
Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
Science
305
390-392
2004
Homo sapiens (Q96EB6), Homo sapiens, Rattus norvegicus (Q96EB6)
Manually annotated by BRENDA team
Yamagata, K.; Goto, Y.; Nishimasu, H.; Morimoto, J.; Ishitani, R.; Dohmae, N.; Takeda, N.; Nagai, R.; Komuro, I.; Suga, H.; Nureki, O.
Structural basis for potent inhibition of SIRT2 deacetylase by a macrocyclic peptide inducing dynamic structural change
Structure
22
345-352
2014
Homo sapiens (Q8IXJ6), Homo sapiens
Manually annotated by BRENDA team
Rumpf, T.; Gerhardt, S.; Einsle, O.; Jung, M.
Seeding for sirtuins: microseed matrix seeding to obtain crystals of human Sirt3 and Sirt2 suitable for soaking
Acta Crystallogr. Sect. F
71
1498-1510
2015
Homo sapiens (Q8IXJ6), Homo sapiens (Q9NTG7), Homo sapiens
Manually annotated by BRENDA team
Bhalla, S.; Gordon, L.I.
Functional characterization of NAD dependent de-acetylases SIRT1 and SIRT2 in B-cell chronic lymphocytic leukemia (CLL)
Cancer Biol. Ther.
17
300-309
2016
Homo sapiens
Manually annotated by BRENDA team
Yang, H.; Zhou, L.; Shi, Q.; Zhao, Y.; Lin, H.; Zhang, M.; Zhao, S.; Yang, Y.; Ling, Z.Q.; Guan, K.L.; Xiong, Y.; Ye, D.
SIRT3-dependent GOT2 acetylation status affects the malate-aspartate NADH shuttle activity and pancreatic tumor growth
EMBO J.
34
1110-1125
2015
Homo sapiens (Q9NTG7), Homo sapiens
Manually annotated by BRENDA team
Lee, Y.H.; Chen, H.Y.; Su, L.J.; Chueh, P.J.
Sirtuin 1 (SIRT1) deacetylase activity and NAD+/NADH ratio are imperative for capsaicin-mediated programmed cell death
J. Agric. Food Chem.
63
7361-7370
2015
Homo sapiens (Q96EB6), Homo sapiens
Manually annotated by BRENDA team
Weiser, B.P.; Eckenhoff, R.G.
Propofol inhibits SIRT2 deacetylase through a conformation-specific, allosteric site
J. Biol. Chem.
290
8559-8568
2015
Rattus norvegicus, Homo sapiens (Q8IXJ6), Homo sapiens
Manually annotated by BRENDA team
Song, H.Y.; Park, S.H.; Kang, H.J.; Vassilopoulos, A.
Deacetylation assays to unravel the interplay between sirtuins (SIRT2) and specific protein-substrates
J. Vis. Exp.
108
53563
2016
Homo sapiens (Q8IXJ6)
Manually annotated by BRENDA team
Fang, M.; Guo, W.R.; Park, Y.; Kang, H.G.; Zarbl, H.
Enhancement of NAD+-dependent SIRT1 deacetylase activity by methylselenocysteine resets the circadian clock in carcinogen-treated mammary epithelial cells
Oncotarget
6
42879-42891
2015
Rattus norvegicus, Homo sapiens (Q96EB6), Homo sapiens
Manually annotated by BRENDA team
Teng, Y.B.; Jing, H.; Aramsangtienchai, P.; He, B.; Khan, S.; Hu, J.; Lin, H.; Hao, Q.
Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies
Sci. Rep.
5
8529
2015
Homo sapiens (Q8IXJ6)
Manually annotated by BRENDA team
Pasha, J.; Kandagatla, B.; Sen, S.; Seerapu, G.; Bujji, S.; Haldar, D.; Nanduri, S.; Oruganti, S.
Amberlyst-15 catalyzed Povarov reaction of N-arylidene-1H-indazol-6-amines and indoles: a greener approach to the synthesis of exo-1,6,7,7a,12,12a-hexahydroindolo[3,2-c]pyrazolo[3,4-f]quinolines as potential sirtuin inhibitors
Tetrahedron Lett.
56
2289-2292
2015
Homo sapiens (Q8IXJ6)
-
Manually annotated by BRENDA team
Smith, B.C.; Denu, J.M.
Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptide
Biochemistry
46
14478-14486
2007
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
North, B.J.; Verdin, E.
Sirtuins Sir2-related NAD-dependent protein deacetylases
Genome Biol.
5
224
2004
Archaeoglobus fulgidus (O28597), Saccharomyces cerevisiae (P53686), Homo sapiens (Q8IXJ6), Homo sapiens, Archaeoglobus fulgidus ATCC 49558 (O28597)
Manually annotated by BRENDA team
Jackson, M.D.; Schmidt, M.T.; Oppenheimer, N.J.; Denu, J.M.
Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases
J. Biol. Chem.
278
50985-50998
2003
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team