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2 KKGQSTSRHKKAcLMFKTEG + 2 NAD+ + 2 H2O
KKGQSTSRHKKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + 3''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-cytochrome c + NAD+ + H2O
?
-
the enzyme does not deacetylate native acetyl-cytochrome c but does deacetylate the heat-denatured substrate
-
-
?
acetyl-poly-L-lysine + NAD+ + H2O
?
-
-
-
-
?
AGG(AcK)GG(AcK)GMG(AcK)VGA(AcK)RHSC + NAD+ + H2O
AGG(AcK)GG(AcK)GMG(AcK)VGAKRHSC + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
tetraacetylated histone-H4 N-terminal tail peptide
-
-
?
ARTKQTAR(AcK)STGG(AcK)APRKQLC + NAD+ + H2O
ARTKQTARKSTGGKAPRKQLC + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
diacetyl ated histone-H3 N-terminal tail peptide
-
-
?
fluorogenic acetyl-L-lysine + NAD+ + H2O
?
-
-
-
?
HLKSKKGQSTSRHK(K-Ac)LMFK + NAD+ + H2O
HLKSKKGQSTSRHKKLMFK + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
p53A peptide
-
-
?
hyperacetylated histone-DNA complex + NAD+ + H2O
deacetylated nuclease-resistant histone-DNA complex + ?
-
-
-
?
K382azaKAc-containing p53 peptide + NAD+ + H2O
K382azaK-containing p53 peptide + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
K382KAc-containing p53 peptide + NAD+ + H2O
K382K-containing p53 peptide + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
KKGQSTSRHKKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
KKGQSTSRHKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
KSTGGAcKAPRKQ + NAD+ + H2O
KSTGGKAPRKQ + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
KSTGGK(Ac)APRKQ + beta-2'-deoxy-2'-fluororibo-NAD+ + H2O
?
KSTGGK(Ac)APRKQ + NAD+ + H2O
KSTGGKAPRKQ + 2''-O-acetyl-ADP-D-ribose + nicotinamide
NAD+ + L-Arg-L-His-L-Lys-L-Lys(epsilon-acetyl)-7-amido-4-methylcoumarin
nicotinamide + ?
-
-
-
-
?
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
i.e. 3-[(5-[[(benzyloxy)carbonyl]amino]-5-[(4-methyl-2-oxo-2H-chromen-7-yl)carbamoyl]pentyl)carbamoyl]-propanoic acid
-
-
?
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
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
acetylated histone H3 peptide
-
-
?
NAD+ + QTAR(N6-butyryl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-butyryl-ADP-ribose
NAD+ + QTAR(N6-crotonyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-crotonyl-ADP-ribose
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
NAD+ + QTAR(N6-dodecanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-dodecanoyl-ADP-ribose
NAD+ + QTAR(N6-hexanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-hexanoyl-ADP-ribose
NAD+ + QTAR(N6-myristoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-myristoyl-ADP-ribose
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
NAD+ + QTAR(N6-palmitoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-palmitoyl-ADP-ribose
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
NAD+ + QTAR(N6-succinyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-succinyl-ADP-ribose
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
peptide based on an acetyl-CoA synthetase 2 acetylation site
-
-
?
NAD+ + TRSG(N6-acetyl)KVMRRLLR
nicotinamide + TRSGKVMRRLLR + 2'-O-acetyl-ADP-ribose
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
-
-
-
?
NAD+ + [alpha-tubulin]-N6-acetyl-L-lysine40
nicotinamide + [alpha-tubulin]-L-lysine40 + 2'-O-acetyl-ADP ribose
-
-
-
?
NAD+ + [alpha-tubulin]-N6-acyl-L-lysine
nicotinamide + [alpha-tubulin]-L-lysine + 2'-O-acyl-ADP-ribose
NAD+ + [BHJH-TM1 protein]-N6-myristoyl-L-lysine
nicotinamide + [BHJH-TM1 protein]-L-lysine + 2'-O-myristoyl-ADP-ribose
-
-
-
?
NAD+ + [BMAL1 protein]-N6-acyl-L-lysine
nicotinamide + [BMAL1 protein]-L-lysine + 2'-O-acyl-ADP-ribose
NAD+ + [chicken erythrocyte histone]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP ribose
-
-
-
?
NAD+ + [DNA repair factor Ku70]-N6-acetyl-L-lysine382
nicotinamide + [DNA repair factor Ku70]-L-lysine382 + 2'-O-acetyl-ADP-ribose
NAD+ + [Fluor de Lys protein]-N6-acyl-L-lysine
nicotinamide + [Fluor de Lys protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
-
?
NAD+ + [Fluor de Lys]-N6-acetyl-L-lysine
nicotinamide + [Fluor de Lys]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [glutamate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glutamate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [glutamate oxaloacetate transaminase 2]-N6-acetyl-L-lysine
nicotinamide + [glutamate oxaloacetate transaminase 2]-L-lysine + 2'-O-acyl-ADP-ribose
isoform SIRT3 is the major deacetylase of glutamate oxaloacetate transaminase 2
-
-
?
NAD+ + [heat shock protein 10]-N6-acetyl-L-lysine56
nicotinamide + [heat shock protein 10]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [histone H2B]-N6-acetyl-L-lysine12
nicotinamide + [histone H2B]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [histone H2B]-N6-myristoyl-L-lysine12
nicotinamide + [histone H2B]-L-lysine + 2'-O-myristoyl-ADP-ribose
-
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine9
nicotinamide + [histone H3]-L-lysine9 + 2'-O-acetyl-ADP-ribose
NAD+ + [histone H3]-N6-myristoyl-L-lysine9
nicotinamide + [histone H3]-L-lysine + 2'-O-myristoyl-ADP-ribose
-
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine16
nicotinamide + [histone H4]-L-lysine16 + 2'-O-acetyl-ADP-ribose
NAD+ + [histone H4]-N6-acetyl-L-lysine8
nicotinamide + [histone H4]-L-lysine8 + 2'-O-acetyl-ADP-ribose
deacetylated at high concentrations of enzyme
-
-
?
NAD+ + [histone H4]-N6-myristoyl-L-lysine16
nicotinamide + [histone H4]-L-lysine + 2'-O-myristoyl-ADP-ribose
-
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine413
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine413 + 2'-O-acetyl-ADP-ribose
NAD+ + [nuclear receptor LXRalpha]-N6-acetyl-L-lysine432
nicotinamide + [nuclear receptor LXRalpha]-L-lysine432 + 2'-O-acetyl-ADP ribose
Q96EB6
-
-
-
?
NAD+ + [nuclear receptor LXRbeta]-N6-acetyl-L-lysine433
nicotinamide + [nuclear receptor LXRbeta]-L-lysine433 + 2'-O-acetyl-ADP ribose
Q96EB6
-
-
-
?
NAD+ + [nuclear receptor LXR]-N6-acetyl-L-lysine
nicotinamide + [nuclear receptor LXR]-L-lysine + 2'-O-acetyl-ADP ribose
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
NAD+ + [p53 protein]-N6-acetyl-L-lysine382
nicotinamide + [p53 protein]-L-lysine382 + 2'-O-acetyl-ADP ribose
NAD+ + [PER2 protein]-N6-acetyl-L-lysine
nicotinamide + [PER2 protein]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
NAD+ + [protein]-N6-myristoyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-myristoyl-ADP-ribose
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
-
-
-
?
NAD+ + [SREBP-1c]-N6-acetyl-L-lysine
nicotinamide + [SREBP-1c]-L-lysine + 2'-O-acetyl-ADP ribose
NAD+ + [thymine DNA glycosylase]-N6-acetyl-L-lysine
nicotinamide + [thymine DNA glycosylase]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [very long-chain acyl-CoA dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [very long-chain acyl-CoA dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
[Acs protein]-N6-acetyl-L-lysine609 + NAD+ + H2O
[Acs protein]-L-lysine609 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[Alba protein]-N6-acetyl-L-lysine16 + NAD+ + H2O
[Alba protein]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[alpha-tubulin]-N6-acetyl-L-lysine40 + NAD+ + H2O
[alpha-tubulin]-L-lysine40 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[bovine serum albumin]-N6-acetyl-L-lysine + NAD+ + H2O
[bovine serum albumin]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[histone H2B]-N6-acetyl-L-lysine + NAD+ + H2O
[histone H2B]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[histone H2B]-N6-acetyl-L-lysine20 + NAD+ + H2O
[histone H2B]-L-lysine20 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H2B]-N6-acetyl-L-lysine5 + NAD+ + H2O
[histone H2B]-L-lysine5 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H2]-N6-acetyl-L-lysine + NAD+ + H2O
[histone H2]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[histone H3]-N6-acetyl-L-lysine + NAD+ + H2O
[histone H3]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[histone H3]-N6-acetyl-L-lysine14 + NAD+ + H2O
[histone H3]-L-lysine14 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H3]-N6-acetyl-L-lysine18 + NAD+ + H2O
[histone H3]-L-lysine18 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H3]-N6-acetyl-L-lysine23 + NAD+ + H2O
[histone H3]-L-lysine23 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H3]-N6-acetyl-L-lysine9 + NAD+ + H2O
[histone H3]-L-lysine9 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[histone H3]-N6-butyryl-L-lysine9 + NAD+ + H2O
[histone H3]-L-lysine9 + 2''-O-butyryl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H3]-N6-myristoyl-L-lysine9 + NAD+ + H2O
[histone H3]-L-lysine9 + 2''-O-myristoyl-ADP-D-ribose + nicotinamide
best substrate
-
-
?
[histone H3]-N6-octanoyl-L-lysine9 + NAD+ + H2O
[histone H3]-L-lysine9 + 2''-O-octanoyl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H4]-N6-acetyl-L-lysine + NAD+ + H2O
[histone H4]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[histone H4]-N6-acetyl-L-lysine12 + NAD+ + H2O
[histone H4]-L-lysine12 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H4]-N6-acetyl-L-lysine16 + NAD+ + H2O
[histone H4]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[histone H4]-N6-acetyl-L-lysine5 + NAD+ + H2O
[histone H4]-L-lysine5 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H4]-N6-acetyl-L-lysine8 + NAD+ + H2O
[histone H4]-L-lysine8 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
weak activity
-
-
?
[HU protein]-N6-acetyl-L-lysine + NAD+ + H2O
[HU protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[p53 peptide]-N6-acetyl-L-lysine382 + NAD+ + H2O
[p53 peptide]-L-lysine382 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[peptide p300]-N6-acetyl-L-lysine + NAD+ + H2O
[histone H4]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
peptide p300 with the sequence ERSTEL(K-Ac)TEI(K-Ac)EEEDQPSTS. The enzyme predominantly deacetylates at K1040 of full length peptide p300
-
-
?
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
additional information
?
-
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
KKGQSTSRHKKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
r
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
KKGQSTSRHKKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
r
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
KKGQSTSRHKKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
r
KKGQSTSRHKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
-
-
-
-
r
KKGQSTSRHKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
-
-
-
-
r
KKGQSTSRHKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
-
-
-
-
r
KSTGGK(Ac)APRKQ + beta-2'-deoxy-2'-fluororibo-NAD+ + H2O
?
-
the rates with beta-2'-deoxy-2'-fluororibo-NAD+ are about 1200fold slower than the exchange rates determined with NAD+ under similar conditions
-
-
?
KSTGGK(Ac)APRKQ + beta-2'-deoxy-2'-fluororibo-NAD+ + H2O
?
-
the rates with beta-2'-deoxy-2'-fluororibo-NAD+ are about 200fold slower than the exchange rates determined with NAD+ under similar conditions
-
-
?
KSTGGK(Ac)APRKQ + NAD+ + H2O
KSTGGKAPRKQ + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
an 11-mer histone H3 peptide
-
-
?
KSTGGK(Ac)APRKQ + NAD+ + H2O
KSTGGKAPRKQ + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
an 11-mer histone H3 peptide
-
-
?
NAD+ + QTAR(N6-butyryl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-butyryl-ADP-ribose
butyrylated histone H3 peptide
-
-
?
NAD+ + QTAR(N6-butyryl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-butyryl-ADP-ribose
butyrylated histone H3 peptide, about 20% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-butyryl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-butyryl-ADP-ribose
butyrylated histone H3 peptide, about 5% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-crotonyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-crotonyl-ADP-ribose
crotonylated histone H3 peptide, about 20% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-crotonyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-crotonyl-ADP-ribose
crotonylated histone H3 peptide, about 30% compared to the activity with the acetylated or hexanoylated peptide
-
-
?
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
decanoylated histone H3 peptide, about 50% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
decanoylated histone H3 peptide, about 65% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
decanoylated histone H3 peptide, about 80% compared to the activity with the acetylated or hexanoylated peptide
-
-
?
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
myristoylated histone H3 peptide, about 50% compared to the activity with the acetylated or hexanoylated peptide
-
-
?
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
myristoylated histone H3 peptide, about 65% compared to the activity with the acetylated or hexanoylated peptide
-
-
?
NAD+ + QTAR(N6-dodecanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-dodecanoyl-ADP-ribose
dodecanoylated histone H3 peptide, about 30% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-dodecanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-dodecanoyl-ADP-ribose
dodecanoylated histone H3 peptide, about 60% compared to the activity with the acetylated or hexanoylated peptide
-
-
?
NAD+ + QTAR(N6-dodecanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-dodecanoyl-ADP-ribose
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
hexanoylated histone H3 peptide
-
-
?
NAD+ + QTAR(N6-hexanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-hexanoyl-ADP-ribose
hexanoylated histone H3 peptide, about 20% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-hexanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-hexanoyl-ADP-ribose
hexanoylated histone H3 peptide, about 40% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-octanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-octanoyl-ADP-ribose
octanoylated histone H3 peptide
-
-
?
NAD+ + QTAR(N6-octanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-octanoyl-ADP-ribose
octanoylated histone H3 peptide, about 35% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-octanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-octanoyl-ADP-ribose
octanoylated histone H3 peptide, about 55% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-propionyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-propionyl-ADP-ribose
propionylated histone H3 peptide, about 10% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-propionyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-propionyl-ADP-ribose
propionylated histone H3 peptide, about 40% compared to the activity with the acetylated peptide
-
-
?
NAD+ + QTAR(N6-propionyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-propionyl-ADP-ribose
propionylated histone H3 peptide, about 60% compared to the activity with the acetylated or hexanoylated peptide
-
-
?
NAD+ + [alpha-tubulin]-N6-acyl-L-lysine
nicotinamide + [alpha-tubulin]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
?
NAD+ + [alpha-tubulin]-N6-acyl-L-lysine
nicotinamide + [alpha-tubulin]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
-
?
NAD+ + [BMAL1 protein]-N6-acyl-L-lysine
nicotinamide + [BMAL1 protein]-L-lysine + 2'-O-acyl-ADP-ribose
Q96EB6
-
-
-
?
NAD+ + [BMAL1 protein]-N6-acyl-L-lysine
nicotinamide + [BMAL1 protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
-
?
NAD+ + [DNA repair factor Ku70]-N6-acetyl-L-lysine382
nicotinamide + [DNA repair factor Ku70]-L-lysine382 + 2'-O-acetyl-ADP-ribose
Q96EB6
-
-
-
?
NAD+ + [DNA repair factor Ku70]-N6-acetyl-L-lysine382
nicotinamide + [DNA repair factor Ku70]-L-lysine382 + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [DNA repair factor Ku70]-N6-acetyl-L-lysine382
nicotinamide + [DNA repair factor Ku70]-L-lysine382 + 2'-O-acetyl-ADP-ribose
Q96EB6
SIRT1 modulates DNA repair activity, which can be regulated by the acetylation status of repair protein Ku70 following DNA damage
-
-
?
NAD+ + [DNA repair factor Ku70]-N6-acetyl-L-lysine382
nicotinamide + [DNA repair factor Ku70]-L-lysine382 + 2'-O-acetyl-ADP-ribose
Q96EB6
-
-
-
?
NAD+ + [Fluor de Lys]-N6-acetyl-L-lysine
nicotinamide + [Fluor de Lys]-L-lysine + 2'-O-acetyl-ADP-ribose
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+ + [Fluor de Lys]-N6-acetyl-L-lysine
nicotinamide + [Fluor de Lys]-L-lysine + 2'-O-acetyl-ADP-ribose
Q923E4
-
-
-
?
NAD+ + [glutamate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glutamate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [glutamate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glutamate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
Sirt3 can deacetylate and thereby activate a central metabolic regulator in the mitochondrial matrix, glutamate dehydrogenase
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine9
nicotinamide + [histone H3]-L-lysine9 + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine9
nicotinamide + [histone H3]-L-lysine9 + 2'-O-acetyl-ADP-ribose
deacetylated at high concentrations of enzyme
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine16
nicotinamide + [histone H4]-L-lysine16 + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine16
nicotinamide + [histone H4]-L-lysine16 + 2'-O-acetyl-ADP-ribose
the deacetylation of [histone H4]-N6-acetyl-L-lysine16 may be pivotal to the formation of condensed chromatin
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine16
nicotinamide + [histone H4]-L-lysine16 + 2'-O-acetyl-ADP-ribose
strong preference for histone H4K16Ac in their deacetylation activity in vitro and in vivo
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
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
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine413
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine413 + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine413
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine413 + 2'-O-acetyl-ADP-ribose
acetylation of Lys413 decreases catalysis and SIRT3 reactivates isocitrate dehydrogenase 2 upon deacetylation
-
-
?
NAD+ + [p53 protein]-N6-acetyl-L-lysine
nicotinamide + [p53 protein]-L-lysine + 2'-O-acetyl-ADP-ribose
Q96EB6
-
-
-
?
NAD+ + [p53 protein]-N6-acetyl-L-lysine
nicotinamide + [p53 protein]-L-lysine + 2'-O-acetyl-ADP-ribose
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
Q96EB6
-
-
-
?
NAD+ + [p53 protein]-N6-acetyl-L-lysine382
nicotinamide + [p53 protein]-L-lysine382 + 2'-O-acetyl-ADP ribose
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
Q96EB6
-
-
-
?
NAD+ + [PER2 protein]-N6-acetyl-L-lysine
nicotinamide + [PER2 protein]-L-lysine + 2'-O-acetyl-ADP-ribose
Q96EB6
SIRT1 regulates circadian clock gene expression through PER2 deacetylation
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
Q96EB6
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
-
?
NAD+ + [SREBP-1c]-N6-acetyl-L-lysine
nicotinamide + [SREBP-1c]-L-lysine + 2'-O-acetyl-ADP ribose
Q923E4
SREBP-1c is a key lipogenic activator. Deacetylation of SREBP-1c by SIRT1 inhibits SREBP-1c activity by decreasing its stability and its association with its lipogenic target gene promoters
-
-
?
NAD+ + [SREBP-1c]-N6-acetyl-L-lysine
nicotinamide + [SREBP-1c]-L-lysine + 2'-O-acetyl-ADP ribose
Q923E4
SREBP-1c is a key lipogenic activator
-
-
?
NAD+ + [thymine DNA glycosylase]-N6-acetyl-L-lysine
nicotinamide + [thymine DNA glycosylase]-L-lysine + 2'-O-acetyl-ADP-ribose
Q96EB6
-
-
-
?
NAD+ + [thymine DNA glycosylase]-N6-acetyl-L-lysine
nicotinamide + [thymine DNA glycosylase]-L-lysine + 2'-O-acetyl-ADP-ribose
Q96EB6
deacetylation and stimulation of the thymine DNA glycosylase activity by SIRT1 enhances DNA demethylation
-
-
?
[Acs protein]-N6-acetyl-L-lysine609 + NAD+ + H2O
[Acs protein]-L-lysine609 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[Acs protein]-N6-acetyl-L-lysine609 + NAD+ + H2O
[Acs protein]-L-lysine609 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
the enzyme activates Acs protein by deacetylation
-
-
?
[Alba protein]-N6-acetyl-L-lysine16 + NAD+ + H2O
[Alba protein]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[Alba protein]-N6-acetyl-L-lysine16 + NAD+ + H2O
[Alba protein]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[histone H3]-N6-acetyl-L-lysine + NAD+ + H2O
[histone H3]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[histone H3]-N6-acetyl-L-lysine + NAD+ + H2O
[histone H3]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
histone H3 with the sequence ARTKQTAR(K-Ac)STGG(K-Ac)APRKQLAS. The enzyme deacetylates K9 and K16 of diacetylated histone H3
-
-
?
[histone H3]-N6-acetyl-L-lysine + NAD+ + H2O
[histone H3]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[histone H3]-N6-acetyl-L-lysine9 + NAD+ + H2O
[histone H3]-L-lysine9 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H3]-N6-acetyl-L-lysine9 + NAD+ + H2O
[histone H3]-L-lysine9 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
least efficient substrate
-
-
?
[histone H3]-N6-acetyl-L-lysine9 + NAD+ + H2O
[histone H3]-L-lysine9 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[histone H4]-N6-acetyl-L-lysine + NAD+ + H2O
[histone H4]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
histone H3 with the sequence SGRG(K-Ac)GG(K-Ac)GLG(K-Ac)GGA(K-Ac)RHR. The enzyme predominantly deacetylates at K16 of tetra-acetylated histone H4
-
-
?
[histone H4]-N6-acetyl-L-lysine + NAD+ + H2O
[histone H4]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[histone H4]-N6-acetyl-L-lysine16 + NAD+ + H2O
[histone H4]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H4]-N6-acetyl-L-lysine16 + NAD+ + H2O
[histone H4]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
KGGAAc-KRHRKIL
-
-
?
[histone H4]-N6-acetyl-L-lysine16 + NAD+ + H2O
[histone H4]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
?
[histone H4]-N6-acetyl-L-lysine16 + NAD+ + H2O
[histone H4]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[histone H4]-N6-acetyl-L-lysine16 + NAD+ + H2O
[histone H4]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
-
-
-
-
r
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
-
-
-
-
r
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
-
-
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
?
additional information
?
-
Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
-
-
-
additional information
?
-
Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
-
-
-
additional information
?
-
Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
-
-
-
additional information
?
-
Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
-
-
-
additional information
?
-
determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
-
-
-
additional information
?
-
determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
-
-
-
additional information
?
-
determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
-
-
-
additional information
?
-
determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
-
-
-
additional information
?
-
the enzyme also acts as an aminoalkylphosphonate N-acetyltransferase, EC 2.3.1.380. Determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
-
-
-
additional information
?
-
the enzyme also acts as an aminoalkylphosphonate N-acetyltransferase, EC 2.3.1.380. Determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
-
-
-
additional information
?
-
the enzyme also acts as an aminoalkylphosphonate N-acetyltransferase, EC 2.3.1.380. Determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
-
-
-
additional information
?
-
the enzyme also acts as an aminoalkylphosphonate N-acetyltransferase, EC 2.3.1.380. Determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
-
-
-
additional information
?
-
no activity with the crotonylated histone H3 peptide QTAR(N6-crotonyl)KSTGG
-
-
?
additional information
?
-
Q96EB6
no activity with the crotonylated histone H3 peptide QTAR(N6-crotonyl)KSTGG
-
-
?
additional information
?
-
no activity with the crotonylated histone H3 peptide QTAR(N6-crotonyl)KSTGG
-
-
?
additional information
?
-
no activity with the succinylated histone H3 peptide QTAR(N6-succinyl)KSTGG
-
-
?
additional information
?
-
Q96EB6
no activity with the succinylated histone H3 peptide QTAR(N6-succinyl)KSTGG
-
-
?
additional information
?
-
no activity with the succinylated histone H3 peptide QTAR(N6-succinyl)KSTGG
-
-
?
additional information
?
-
Sirt3 has almost no activity against acetylated cytochrome c
-
-
?
additional information
?
-
-
Sirt3 has almost no activity against acetylated cytochrome c
-
-
?
additional information
?
-
the enzyme preferentially hydrolyzes medium and long chain fatty acyl lysine. The deacetylase activity of the enzyme is weak
-
-
?
additional information
?
-
-
the enzyme preferentially hydrolyzes medium and long chain fatty acyl lysine. The deacetylase activity of the enzyme is weak
-
-
?
additional information
?
-
-
the enzyme is specific for acetyl-lysine within proteins. It does not deacetylate small polycations such as acetyl-spermine or acetyl-protamine or acetylated amino termini of proteins. Furthermore, the enzyme displays conformational rather than sequence specificity, preferentially deacetylating acetyl-lysine within unstructured regions of proteins
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
hyperacetylated histone-DNA complex + NAD+ + H2O
deacetylated nuclease-resistant histone-DNA complex + ?
-
-
-
?
NAD+ + [alpha-tubulin]-N6-acyl-L-lysine
nicotinamide + [alpha-tubulin]-L-lysine + 2'-O-acyl-ADP-ribose
NAD+ + [BMAL1 protein]-N6-acyl-L-lysine
nicotinamide + [BMAL1 protein]-L-lysine + 2'-O-acyl-ADP-ribose
NAD+ + [chicken erythrocyte histone]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP ribose
-
-
-
?
NAD+ + [DNA repair factor Ku70]-N6-acetyl-L-lysine382
nicotinamide + [DNA repair factor Ku70]-L-lysine382 + 2'-O-acetyl-ADP-ribose
NAD+ + [Fluor de Lys protein]-N6-acyl-L-lysine
nicotinamide + [Fluor de Lys protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
-
?
NAD+ + [glutamate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glutamate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
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
isoform SIRT3 is the major deacetylase of glutamate oxaloacetate transaminase 2
-
-
?
NAD+ + [heat shock protein 10]-N6-acetyl-L-lysine56
nicotinamide + [heat shock protein 10]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine16
nicotinamide + [histone H4]-L-lysine16 + 2'-O-acetyl-ADP-ribose
the deacetylation of [histone H4]-N6-acetyl-L-lysine16 may be pivotal to the formation of condensed chromatin
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
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
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine413
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine413 + 2'-O-acetyl-ADP-ribose
acetylation of Lys413 decreases catalysis and SIRT3 reactivates isocitrate dehydrogenase 2 upon deacetylation
-
-
?
NAD+ + [nuclear receptor LXR]-N6-acetyl-L-lysine
nicotinamide + [nuclear receptor LXR]-L-lysine + 2'-O-acetyl-ADP ribose
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
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
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
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
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
NAD+ + [protein]-N6-myristoyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-myristoyl-ADP-ribose
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
-
-
-
?
NAD+ + [SREBP-1c]-N6-acetyl-L-lysine
nicotinamide + [SREBP-1c]-L-lysine + 2'-O-acetyl-ADP ribose
Q923E4
SREBP-1c is a key lipogenic activator. Deacetylation of SREBP-1c by SIRT1 inhibits SREBP-1c activity by decreasing its stability and its association with its lipogenic target gene promoters
-
-
?
NAD+ + [thymine DNA glycosylase]-N6-acetyl-L-lysine
nicotinamide + [thymine DNA glycosylase]-L-lysine + 2'-O-acetyl-ADP-ribose
Q96EB6
deacetylation and stimulation of the thymine DNA glycosylase activity by SIRT1 enhances DNA demethylation
-
-
?
NAD+ + [very long-chain acyl-CoA dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [very long-chain acyl-CoA dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
[Acs protein]-N6-acetyl-L-lysine609 + NAD+ + H2O
[Acs protein]-L-lysine609 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
the enzyme activates Acs protein by deacetylation
-
-
?
[Alba protein]-N6-acetyl-L-lysine16 + NAD+ + H2O
[Alba protein]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
additional information
?
-
NAD+ + [alpha-tubulin]-N6-acyl-L-lysine
nicotinamide + [alpha-tubulin]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
?
NAD+ + [alpha-tubulin]-N6-acyl-L-lysine
nicotinamide + [alpha-tubulin]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
-
?
NAD+ + [BMAL1 protein]-N6-acyl-L-lysine
nicotinamide + [BMAL1 protein]-L-lysine + 2'-O-acyl-ADP-ribose
Q96EB6
-
-
-
?
NAD+ + [BMAL1 protein]-N6-acyl-L-lysine
nicotinamide + [BMAL1 protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
-
?
NAD+ + [DNA repair factor Ku70]-N6-acetyl-L-lysine382
nicotinamide + [DNA repair factor Ku70]-L-lysine382 + 2'-O-acetyl-ADP-ribose
Q96EB6
-
-
-
?
NAD+ + [DNA repair factor Ku70]-N6-acetyl-L-lysine382
nicotinamide + [DNA repair factor Ku70]-L-lysine382 + 2'-O-acetyl-ADP-ribose
Q96EB6
SIRT1 modulates DNA repair activity, which can be regulated by the acetylation status of repair protein Ku70 following DNA damage
-
-
?
NAD+ + [DNA repair factor Ku70]-N6-acetyl-L-lysine382
nicotinamide + [DNA repair factor Ku70]-L-lysine382 + 2'-O-acetyl-ADP-ribose
Q96EB6
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
Q96EB6
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-acyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acyl-ADP-ribose
-
-
-
-
?
[Alba protein]-N6-acetyl-L-lysine16 + NAD+ + H2O
[Alba protein]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[Alba protein]-N6-acetyl-L-lysine16 + NAD+ + H2O
[Alba protein]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
-
-
-
-
r
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
-
-
-
-
r
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
-
-
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
overall reaction
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
?
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
?
additional information
?
-
Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
-
-
-
additional information
?
-
Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
-
-
-
additional information
?
-
Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
-
-
-
additional information
?
-
Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
-
-
-
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(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
10% inhibition at 0.05 mM
(5E)-5-(1H-indol-3-ylmethylidene)-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
17% inhibition at 0.05 mM; 20% inhibition at 0.05 mM
(5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
13% inhibition at 0.05 mM
(5E)-5-[4-(benzyloxy)benzylidene]-1-ethyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
25% inhibition at 0.05 mM
(5E)-5-[4-(benzyloxy)benzylidene]-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
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
41% inhibition at 0.05 mM
(7aS,12aS)-7-(4-chlorophenyl)-1,6,7,7a,12,12a-hexahydroindolo[3,2-c]pyrazolo[3,4-f]quinoline
-
about 5% inhibition at 0.05 mM
(7aS,12aS)-7-(4-methoxyphenyl)-1,6,7,7a,12,12a-hexahydroindolo[3,2-c]pyrazolo[3,4-f]quinoline
-
about 38% inhibition at 0.05 mM
(7aS,12aS)-7-phenyl-1,6,7,7a,12,12a-hexahydroindolo[3,2-c]pyrazolo[3,4-f]quinoline
-
about 18% inhibition at 0.05 mM
(7aS,12aS)-7-[4-(thiophen-2-yl)phenyl]-1,6,7,7a,12,12a-hexahydroindolo[3,2-c]pyrazolo[3,4-f]quinoline
-
about 16% inhibition at 0.05 mM
(7aS,12aS)-9-bromo-7-(4-chlorophenyl)-1,6,7,7a,12,12a-hexahydroindolo[3,2-c]pyrazolo[3,4-f]quinoline
-
about 50% inhibition at 0.05 mM
(7aS,12aS)-9-bromo-7-(4-fluorophenyl)-1,6,7,7a,12,12a-hexahydroindolo[3,2-c]pyrazolo[3,4-f]quinoline
-
about 65% inhibition at 0.05 mM
(7aS,12aS)-9-bromo-7-(4-methoxyphenyl)-1,6,7,7a,12,12a-hexahydroindolo[3,2-c]pyrazolo[3,4-f]quinoline
-
about 65% inhibition at 0.05 mM
(7aS,12aS)-9-bromo-7-phenyl-1,6,7,7a,12,12a-hexahydroindolo[3,2-c]pyrazolo[3,4-f]quinoline
-
about 70% inhibition at 0.05 mM
(7aS,12aS)-9-bromo-7-[4-(furan-2-yl)phenyl]-1,6,7,7a,12,12a-hexahydroindolo[3,2-c]pyrazolo[3,4-f]quinoline
-
about 78% inhibition at 0.05 mM
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
i.e. Ro 31-8220; i.e. Ro 31-8220; 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
3-acetylpyridine
-
16.8% inhibition at 30 mM
3-bromopyridine
-
19.1% inhibition at 30 mM
3-chloropyridine
-
9% inhibition at 30 mM
3-fluoropyridine
-
less than 2% inhibition at 30 mM
3-hydroxypyridine
-
83.9% inhibition at 15 mM
3-methoxypyridine
-
10.8% inhibition at 30 mM
3-pyridine-carboxyaldehyde
-
10.6% inhibition at 30 mM
3-Pyridinemethanol
-
22.5% inhibition at 30 mM
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
14% inhibition at 0.05 mM
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[(1-benzyl-1H-indol-3-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
20% inhibition at 0.05 mM
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[4-(propan-2-yl)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
13% inhibition at 0.05 mM
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
30% inhibition at 0.05 mM
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
-
alpha-1-O-methyl-adenosine diphosphoribose
-
-
coumermycin A1
completely inhibited by 0.2 mM
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
-
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-[(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
nicotinic acid
-
18.3% inhibition at 15 mM
prolyl-N-benzyl-N6-ethanethioyl-L-lysinamide
Q96EB6
0.05 mM, 94.8% inhibition
Pyridine
-
6.4% inhibition at 30 mM
resveratrol
inhibits deacetylase activity
[histone H3]-difluoroacetyl-L-lysine
-
[histone H3]-monofluoroacetyl-L-lysine
-
[histone H3]-thioacetyl-L-lysine
-
[histone H3]-trifluoroacetyl-L-lysine
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
i.e. EX-527; i.e. EX-527; i.e. EX-527
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
Q96EB6
-
Benzamide
-
5% inhibition at 5 mM
Benzamide
-
44% inhibition at 5 mM
cambinol
-
EX-527
-
-
Ex257
Q96EB6
specific inhibitor of isoform SIRT1
Ex257
-
specific inhibitor of isoform SIRT1
Isonicotinamide
-
4% inhibition at 5 mM
Isonicotinamide
weak competitive inhibitor of hSIRT3 with respect to NAD+ in vitro; weak inhibitor
Isonicotinamide
-
18% inhibition at 5 mM
Isonicotinamide
-
5% inhibition at 42 mM
meta-azi-propofol
only binds specifically and competitively to the enzyme when co-equilibrated with other substrates
meta-azi-propofol
-
only binds specifically and competitively to the enzyme when co-equilibrated with other substrates
N-methyl-N-nitrosourea
Q96EB6
-
N-methyl-N-nitrosourea
-
-
nicotinamide
-
-
nicotinamide
mixed noncompetitive inhibitor. Inhibition of SIRT3 involves apparent competition between the inhibitor and the enzyme cofactor NAD+; predominantly noncompetitive inhibitor
nicotinamide
0.5 mM, complete inhibition
nicotinamide
-
noncompetitive inhibitor versus NAD+
nicotinamide
-
noncompetitive inhibitor versus NAD+. 95% inhibition at 1.5 mM
nicotinamide
noncompetitive inhibitor
propofol
only binds specifically and competitively to the enzyme when co-equilibrated with other substrates
propofol
-
only binds specifically and competitively to the enzyme when co-equilibrated with other substrates
Pyrazinamide
-
4% inhibition at 5 mM
Pyrazinamide
-
1% inhibition at 5 mM
Pyrazinamide
-
1% inhibition at 5 mM
sirtinol
24% inhibition at 0.05 mM
Thionicotinamide
-
4% inhibition at 5 mM
Thionicotinamide
-
16% inhibition at 5 mM
Thionicotinamide
-
15% inhibition at 5 mM
Thionicotinamide
-
58.3% inhibition at 15 mM
[histone H3]-difluoroacetyl-L-lysine
-
-
-
[histone H3]-difluoroacetyl-L-lysine
-
-
-
[histone H3]-monofluoroacetyl-L-lysine
-
-
-
[histone H3]-monofluoroacetyl-L-lysine
-
-
-
[histone H3]-thioacetyl-L-lysine
-
most potent inhibitor
-
[histone H3]-thioacetyl-L-lysine
-
most potent inhibitor
-
[histone H3]-trifluoroacetyl-L-lysine
-
-
[histone H3]-trifluoroacetyl-L-lysine
-
-
additional information
no inhibition at 0.05 mM: (5E)-1-ethyl-5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione; no inhibition at 0.05 mM: (5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione; no inhibition by EX-527, HR 103 or Ro 31-8220; no inhibition by EX-527, HR 103 or Ro 31-8220; no inhibition by EX-527, HR 103 or Ro 31-8220
-
additional information
Q96EB6
no inhibition at 0.05 mM: (5E)-1-ethyl-5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione; no inhibition at 0.05 mM: (5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione; no inhibition by EX-527, HR 103 or Ro 31-8220; no inhibition by EX-527, HR 103 or Ro 31-8220; no inhibition by EX-527, HR 103 or Ro 31-8220
-
additional information
no inhibition at 0.05 mM: (5E)-1-ethyl-5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione; no inhibition at 0.05 mM: (5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione; no inhibition by EX-527, HR 103 or Ro 31-8220; no inhibition by EX-527, HR 103 or Ro 31-8220; no inhibition by EX-527, HR 103 or Ro 31-8220
-
additional information
-
not inhibited by benzamide
-
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0.0144
(5E)-5-[4-(benzyloxy)benzylidene]-1-ethyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.01
(5E)-5-[4-(benzyloxy)benzylidene]-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
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
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 - 0.0037
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
pH 8.0, 37°C
0.0087 - 0.0403
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
0.116
5-[(1-benzyl-1H-indol-3-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0117 - 0.0433
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
0.0098 - 0.0293
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
0.0147
5-[4-(propan-2-yl)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0075 - 0.0464
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
0.0034 - 0.0303
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
0.0104
5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0001 - 0.049
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
12200 - 13800
Isonicotinamide
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
0.132
[histone H3]-difluoroacetyl-L-lysine
Saccharomyces cerevisiae
-
at pH 7.5 and 25°C
-
0.133
[histone H3]-monofluoroacetyl-L-lysine
Saccharomyces cerevisiae
-
at pH 7.5 and 25°C
-
0.00102
[histone H3]-thioacetyl-L-lysine
Saccharomyces cerevisiae
-
at pH 7.5 and 25°C
-
0.061
[histone H3]-trifluoroacetyl-L-lysine
Saccharomyces cerevisiae
-
at pH 7.5 and 25°C
0.0008
2-[1-[3-(amidinothio)propyl]-1H-indol-3-yl]-3-(1-methylindol-3-yl)maleimide methanesulfonate
Homo sapiens
pH 8.0, 37°C
0.0035
2-[1-[3-(amidinothio)propyl]-1H-indol-3-yl]-3-(1-methylindol-3-yl)maleimide methanesulfonate
Homo sapiens
pH 8.0, 37°C
0.0037
2-[1-[3-(amidinothio)propyl]-1H-indol-3-yl]-3-(1-methylindol-3-yl)maleimide methanesulfonate
Homo sapiens
pH 8.0, 37°C
0.0087
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0403
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0117
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0433
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0098
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0293
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0075
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0464
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0034
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0303
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0001 - 0.001
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
Homo sapiens
pH 8.0, 37°C
0.02 - 0.033
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
Homo sapiens
pH 8.0, 37°C
0.049
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
Homo sapiens
pH 8.0, 37°C
0.056
cambinol
Homo sapiens
pH 8.0, 37°C
0.059
cambinol
Homo sapiens
pH 8.0, 37°C
12200
Isonicotinamide
Homo sapiens
pH 8, 37°C, weak inhibitor
13800
Isonicotinamide
Homo sapiens
pH 8, 37°C, weak competitive inhibitor of hSIRT3 with respect to NAD+ in vitro
0.0012 - 0.1
nicotinamide
Homo sapiens
pH 8.0, 37°C
0.03
nicotinamide
Homo sapiens
pH 8.0, 37°C
0.0367
nicotinamide
Homo sapiens
pH 8, 37°C
0.043
nicotinamide
Homo sapiens
pH 7.8, 37°C, substrate: TRSG(N6-acetyl)KVMR
0.05 - 0.1
nicotinamide
Homo sapiens
pH 8.0, 37°C
0.0681
nicotinamide
Homo sapiens
pH 8, 37°C
0.037 - 0.131
sirtinol
Homo sapiens
pH 8.0, 37°C
0.038 - 0.058
sirtinol
Homo sapiens
pH 8.0, 37°C
0.0003 - 0.0026
suramin
Homo sapiens
pH 8.0, 37°C
0.0011 - 0.02
suramin
Homo sapiens
pH 8.0, 37°C
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evolution
Phno is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
evolution
YfiQ is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
evolution
Yiac is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
evolution
YjaB is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
malfunction
-
NAD+-dependent SIRT1 deactivation has a key role on ischemia-reperfusion-induced apoptosis
malfunction
Q96EB6
SIRT1 depletion by RNA interference attenuates capsaicin-induced apoptosis in A-549 cancer cells and autophagy in MRC-5 cells
metabolism
acetylation of Lys413 decreases catalysis and SIRT3 reactivates isocitrate dehydrogenase 2 upon deacetylation. SIRT3-dependent deacetylation of isocitrate dehydrogenase 2 suppresses cellular stress by reactive oxygen species (ROS). Acetylation of Lys413 is regulated by SIRT3 in response to calorie and glucose restriction
metabolism
Q96EB6
caloric restriction can extend life-span by inducing SIRT1 expression and promoting the long-term survival of irreplaceable cells
metabolism
Q96EB6
caloric restriction can extend life-span by inducing SIRT1 expression and promoting the long-term survival of irreplaceable cells
metabolism
Q96EB6
Sir2 is involved in the regulation of p53 function via deacetylation
metabolism
Q96EB6
SIRT1 modulates DNA repair activity, which can be regulated by the acetylation status of repair protein Ku70 following DNA damage
metabolism
the deacetylation of [histone H4]-N6-acetyl-L-lysine16 by Sirt2 may be pivotal to the formation of condensed chromatin
metabolism
the enzyme can regulate flux and anapleurosis of this central metabolic cycle
metabolism
isoform SIRT3 levels modulate mitochondrial protein folding
physiological function
acetylation of heat shock protein 10 by isoform SIRT3 enhances medium-chain acyl-CoA dehydrogenase folding, enzyme activity, and fat oxidation
physiological function
-
enzyme expression is crucial for the survival of the cell
physiological function
-
the activation of SIRT1 is significantly associated with improved protection against hepatic triglyceride accumulation
physiological function
-
heterochromatin assembly requires the SIR proteins Sir3, the primary structural component of SIR heterochromatin, and the Sir2-4 complex, responsible for the targeted recruitment of SIR proteins and the deacetylation of lysine 16 of histone H4
physiological function
-
increase of enzyme activity by caloric restriction or osmotic stress increases genome stability and lifespan in Saccharomyces cerevisiae
physiological function
-
increased enzyme expression of extends life span in a dose-dependent manner
physiological function
-
maintenance of [histone H3]-L-lysine9 methylation at centromeres requires the histone deacetylases Sir2 and Clr3
physiological function
Sirt2 may act as a tumor suppressor and may function to control the cell cycle by acetylation of alpha-tubulin
physiological function
the enzyme does not repress transcription with either naked DNA templates or chromatin assembled from native (and mostly unacetylated) histones
physiological function
-
the enzyme is a pro-longevity factor for replicative lifespan in Saccharomyces cerevisiae. The enzyme is required for transcriptional silencing at mating type loci, telomeres, and rDNA loci. The enzyme also represses transcription of highly expressed growth-related genes, such as PMA1 and some ribosomal protein genes
physiological function
the enzyme regulates the expression of surface antigens to evade the detection by host immune surveillance by removing medium and long chain fatty acyl groups from protein lysine residues
physiological function
Nepsilon-lysine acetyltransferases (KATs) specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. Posttranslational modifications, such as Nepsilon-lysine acetylation, regulate protein function. The enzymes show a high degree of substrate specificity
physiological function
Nepsilon-lysine acetyltransferases (KATs) specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. Posttranslational modifications, such as Nepsilon-lysine acetylation, regulate protein function. The enzymes show a high degree of substrate specificity. Enzyme YfiQ can inhibit Escherichia coli cell migration in soft agar
physiological function
Nepsilon-lysine acetyltransferases (KATs) specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. Posttranslational modifications, such as Nepsilon-lysine acetylation, regulate protein function. The enzymes show a high degree of substrate specificity. Enzyme YiaC can inhibit Escherichia coli cell migration in soft agar. Overexpression of enzyme mutant YiaC YF70A inhibits migration similarly to overexpression of wild-type YiaC
physiological function
-
the enzyme is a pro-longevity factor for replicative lifespan in Saccharomyces cerevisiae. The enzyme is required for transcriptional silencing at mating type loci, telomeres, and rDNA loci. The enzyme also represses transcription of highly expressed growth-related genes, such as PMA1 and some ribosomal protein genes
-
additional information
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
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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
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461-463
2011
Homo sapiens (Q96EB6), Homo sapiens
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Homo sapiens (Q8IXJ6), Homo sapiens (Q96EB6), Homo sapiens (Q9NTG7)
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Homo sapiens (Q96EB6), Homo sapiens
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Down-regulation of sirtuin 3 is associated with poor prognosis in hepatocellular carcinoma after resection
BMC Cancer
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2014
Homo sapiens (Q9NTG7)
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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
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2001
Homo sapiens (Q96EB6)
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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)
brenda
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)
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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
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Homo sapiens (Q96EB6), Homo sapiens
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Development and characterization of 3-(benzylsulfonamido)benzamides as potent and selective SIRT2 inhibitors
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76
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2014
Homo sapiens (Q8IXJ6), Homo sapiens
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Quantitative insights for the design of substrate-based SIRT1 inhibitors
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2014
Homo sapiens (Q96EB6), Homo sapiens
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SIRT1 promotes DNA repair activity and deacetylation of Ku70
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39
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2007
Homo sapiens (Q96EB6), Homo sapiens
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SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis
Genes Dev.
20
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2006
Homo sapiens (Q8IXJ6)
brenda
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SIRT1 deacetylates and inhibits SREBP-1C activity in regulation of hepatic lipid metabolism
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285
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Mus musculus (Q923E4), Mus musculus
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SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status
J. Biol. Chem.
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2012
Mus musculus (Q8R104)
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Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins
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2013
Homo sapiens (Q8IXJ6), Homo sapiens (Q96EB6), Homo sapiens (Q9NTG7)
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SIRT1 and SIRT5 activity expression and behavioral responses to calorie restriction
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112
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2011
Rattus norvegicus
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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
brenda
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
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382
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2008
Homo sapiens (Q9NTG7), Homo sapiens
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Crystal structure analysis of human Sirt2 and its ADP-ribose complex
J. Struct. Biol.
182
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2013
Homo sapiens (Q8IXJ6), Homo sapiens
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SIRT1 deacetylates and positively regulates the nuclear receptor LXR
Mol. Cell.
28
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2007
Homo sapiens (Q96EB6)
brenda
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Distinct patterns of sirtuin expression during progression of Alzheimer's disease
Neuromolecular Med.
16
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2014
Homo sapiens (Q9NTG7)
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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
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2014
Homo sapiens (Q96EB6), Homo sapiens (Q9NTG7), Homo sapiens
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Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition
PLoS One
7
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2012
Homo sapiens (Q9NTG7), Homo sapiens
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A molecular mechanism for direct sirtuin activation by resveratrol
PLoS One
7
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2012
Homo sapiens (Q9NTG7), Homo sapiens
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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
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Homo sapiens (Q9NTG7), Homo sapiens
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Mus musculus (Q923E4)
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Homo sapiens (Q96EB6), Homo sapiens, Rattus norvegicus (Q96EB6)
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Homo sapiens (Q8IXJ6), Homo sapiens
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71
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Homo sapiens (Q8IXJ6), Homo sapiens (Q9NTG7), Homo sapiens
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Homo sapiens (Q96EB6), Homo sapiens
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Mus musculus (Q8R104)
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Homo sapiens (Q8IXJ6), Homo sapiens, Rattus norvegicus
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Enhancement of NAD+-dependent SIRT1 deacetylase activity by methylselenocysteine resets the circadian clock in carcinogen-treated mammary epithelial cells
Oncotarget
6
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2015
Rattus norvegicus, Homo sapiens (Q96EB6), Homo sapiens
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Zhang, Y.; Bharathi, S.S.; Rardin, M.J.; Uppala, R.; Verdin, E.; Gibson, B.W.; Goetzman, E.S.
SIRT3 and SIRT5 regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase
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Mus musculus (Q8R104), Mus musculus
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Tulino, R.; Benjamin, A.C.; Jolinon, N.; Smith, D.L.; Chini, E.N.; Carnemolla, A.; Bates, G.P.
SIRT1 activity is linked to its brain region-specific phosphorylation and is impaired in Huntington's disease mice
PLoS ONE
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2016
Mus musculus (Q923E4), Mus musculus
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Teng, Y.B.; Jing, H.; Aramsangtienchai, P.; He, B.; Khan, S.; Hu, J.; Lin, H.; Hao, Q.
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8529
2015
Homo sapiens (Q8IXJ6)
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Aragones, G.; Suarez, M.; Ardid-Ruiz, A.; Vinaixa, M.; Rodriguez, M.A.; Correig, X.; Arola, L.; Blade, C.
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Rattus norvegicus
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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
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2015
Homo sapiens (Q8IXJ6)
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Rattus norvegicus
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Plasmodium falciparum (Q8IE47), Plasmodium falciparum
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Increased expression of Drosophila Sir2 extends life span in a dose-dependent manner
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5
682-691
2013
Drosophila melanogaster
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2017
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Chemistry of gene silencing the mechanism of NAD+-dependent deacetylation reactions
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40
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2001
Thermotoga maritima
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Sauve, A.A.; Schramm, V.L.
Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry
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42
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2003
Archaeoglobus fulgidus, Saccharomyces cerevisiae, Mus musculus
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Smith, B.C.; Denu, J.M.
Sir2 protein deacetylases evidence for chemical intermediates and functions of a conserved histidine
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45
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Saccharomyces cerevisiae
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Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptide
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2007
Saccharomyces cerevisiae, Homo sapiens
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French, J.B.; Cen, Y.; Sauve, A.A.
Plasmodium falciparum Sir2 is an NAD+-dependent deacetylase and an acetyllysine-dependent and acetyllysine-independent NAD+ glycohydrolase
Biochemistry
47
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2008
Plasmodium falciparum
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Min, J.; Landry, J.; Sternglanz, R.; Xu, R.M.
Crystal structure of a SIR2 homolog-NAD complex
Cell
105
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2001
Archaeoglobus fulgidus
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11
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2004
Saccharomyces cerevisiae
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Schizosaccharomyces pombe
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Sirtuins Sir2-related NAD-dependent protein deacetylases
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224
2004
Archaeoglobus fulgidus (O28597), Saccharomyces cerevisiae (P53686), Homo sapiens (Q8IXJ6), Homo sapiens, Archaeoglobus fulgidus ATCC 49558 (O28597)
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Hu, P.; Wang, S.; Zhang, Y.
Highly dissociative and concerted mechanism for the nicotinamide cleavage reaction in Sir2Tm enzyme suggested by ab initio QM/MM molecular dynamics simulations
J. Am. Chem. Soc.
130
16721-16728
2008
Thermotoga maritima (Q9WYW0), Thermotoga maritima ATCC 43589 (Q9WYW0)
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Drosophila melanogaster (Q9VK34)
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Saccharomyces cerevisiae
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