Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NAD+ + Abz-GVLK(glutaryl)AY(NO2)GV-NH2
nicotinamide + ?
-
-
-
?
NAD+ + Ac-(N6-methylmalonyl)Lys-(7-amido-4-methylcoumarin)
nicotinamide + Ac-Lys-7-amido-4-methylcoumarin + 2'-O-methylmalonyl-ADP-ribose
-
-
-
?
NAD+ + Ac-(N6-succinyl)Lys-7-amido-4-methylcoumarin
nicotinamide + Ac-Lys-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + Ac-Leu-Gly-(N6-malonyl)Lys-7-amido-4-methylcoumarin
nicotinamide + Ac-Leu-Gly-Lys-7-amido-4-methylcoumarin + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + Ac-Leu-Gly-(N6-succinyl)Lys-7-amido-4-methylcoumarin
nicotinamide + Ac-Leu-Gly-Lys-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + Ac-Suc-L-Lys-7-amido-4-methylcoumarin
nicotinamide + ?
-
-
-
?
NAD+ + AFNQG(N6-malonyl)KIFK
nicotinamide + AFNQGKIFK + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + AYVDDTPAEQM(N6-malonyl)KAER
nicotinamide + AYVDDTPAEQMKAER + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-acetyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-adipoyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-adipoyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-glutaryl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-glutaryl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-malonyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-oxalyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-oxalyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-pimeloyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-pimeloyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-suberoyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-suberoyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-GVL(N6-succinyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + benzoyl-RGVL(N6-succinyl)KEYGV-amide
nicotinamide + benzoyl-RGVLKEYGV-amide + 2'-O-acetyl-ADP-ribose
carbamoyl phosphate synthetase 1 Lys527 peptide
-
-
?
NAD+ + benzyl-(N6-succinyl)Lys-7-amido-4-methylcoumarin
nicotinamide + benzyl-Lys-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
fluorogenic substrate
-
-
?
NAD+ + DSYVGDEAQSDSYVGDEAQS(N6-malonyl)KR
nicotinamide + DSYVGDEAQSDSYVGDEAQSKR + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + ETGVDLT(N6-succinyl)KDNMALQR
nicotinamide + ETGVDLTKDNMALQR + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + FKRGVL(N6-acetyl)KEYGVKV
nicotinamide + FKRGVLKEYGVKV + 2'-O-acetyl-ADP-ribose
NAD+ + Fluor-de-Lys
nicotinamide + ?
-
-
-
?
NAD+ + IEEELGS(N6-malonyl)KAK
nicotinamide + IEEELGSKAK + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + KGLGKGGA(N6-acetyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-acetyl-ADP-ribose
NAD+ + KGLGKGGA(N6-butyryl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-butyryl-ADP-ribose
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
NAD+ + KQTAR(N6-malonyl)KSTGGWW
nicotinamide + KQTARKSTGGWW + 2'-O-malonyl-ADP-ribose
histone H3K9 malonyl peptide
-
-
?
NAD+ + KQTAR(N6-succinyl)KSTGGKA
nicotinamide + KQTARKSTGGKA + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + KQTAR(N6-succinyl)KSTGGWW
nicotinamide + KQTARKSTGGWW + 2'-O-succinyl-ADP-ribose
histone H3K9 succinyl peptide
-
-
?
NAD+ + KTRSG(N6-malonyl)KVMRRWW
nicotinamide + KTRSGKVMRRWW + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + KTRSG(N6-succinyl)KVMRRWW
nicotinamide + KTRSGKVMRRWW + 2'-O-succinyl-ADP-ribose
ACS2 Lys628 peptide
-
-
?
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, less than 10% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
decanoylated histone H3 peptide, about 35% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-dodecanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-dodecanoyl-ADP-ribose
dodecanoylated histone H3 peptide, about 35% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-hexanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-hexanoyl-ADP-ribose
hexanoylated histone H3 peptide, less than 10% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-myristoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-myristoyl-ADP-ribose
myristoylated histone H3 peptide, about 15% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-octanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-octanoyl-ADP-ribose
octanoylated histone H3 peptide, about 30% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-propionyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-propionyl-ADP-ribose
propionylated histone H3 peptide, less than 10% compared to the activity with the succinylated peptide
-
-
?
NAD+ + QTAR(N6-succinyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-succinyl-ADP-ribose
succinylated histone H3 peptide
-
-
?
NAD+ + SGASE(N6-malonyl)KDIVHSGWW
nicotinamide + SGASEKDIVHSGWW + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + SGASE(N6-succinyl)KDIVHSGWW
nicotinamide + SGASEKDIVHSGWW + 2'-O-succinyl-ADP-ribose
glutamate dehydrogenase Lys503 peptide
-
-
?
NAD+ + SKEYFS(N6-succinyl)KQK
nicotinamide + SKEYFSKQK + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + SQG(N6-succinyl)KVLQATVV
nicotinamide + SQGKVLQATVV + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + TAIG(N6-malonyl)KAGYTDK
nicotinamide + TAIGKAGYTDK + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + TRSG(N6-acetyl)KVMR
nicotinamide + TRSGKVMR + 2'-O-acetyl-ADP-ribose
peptide based on an acetyl-CoA synthetase 2 acetylation site
-
-
?
NAD+ + VLLPEYGGT(N6-succinyl)KVVLDDK
nicotinamide + VLLPEYGGTKVVLDDK + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [bovine serum albumin]-N6-acetyl-L-lysine
nicotinamide + [bovine serum albumin]-L-lysine + 2'-O-acetyl-ADP-ribose
crystallographic evidence is provided that 2'-O-acetyl ADP-ribose is a final product in the Sir2 reaction. A revised mechanism for catalysis based on the structural and functional characterization of Sir2 mutants is proposed. In this mechanism, the activation of the 2'-OH of nicotinamide ribose by His-116 is essential for the hydrolysis of the acetyl groups from N-acetyl lysine. The conserved Ser-24 and Asp-101 participate in the stabilization of local structure for NAD binding rather than direct involvement in catalysis
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [carbamoyl phosphate synthase 1]-N6-succinyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-succinyl-ADP ribose
deletion of Sirt5 in mice increases the level of succinylation on carbamoyl phosphate synthase 1
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1 derived glutarylated peptide]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1 derived glutarylated peptide]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
NAD+ + [carbamoyl phosphate synthetase 1]-N6-glutaryl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-glutaryl-ADP-ribose
-
-
-
?
NAD+ + [chicken histone]-N6-acetyl-L-lysine
nicotinamide + [chicken histone]-L-lysine + 2'-O-acetyl-ADP-ribose
chemically acetylated chicken histone. Less activity toward chemically acetylated bovine serum albumin and monoacetylated histone H4 (K16 and K8). No activity is observed with monoacetylated histone K5 and K12 histone H4 peptides
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
NAD+ + [cytochrome c]-N6-acetyl-L-lysine
nicotinamide + [cytochrome c]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [forkhead box O3]-N6-acetyl-L-lysine
nicotinamide + [forkhead box O3]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme deacetylates FOXO3 at K271 and K290
-
-
?
NAD+ + [glucose 6-phosphate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [glucose 6-phosphate dehydrogenase]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [glucose-6-phosphate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glucose-6-phosphate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [glutaminase]-N6-succinyl-L-lysine
nicotinamide + [glutaminase]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [glyceraldehyde-3-phosphate dehydrogenase]-N6-malonyl-L-lysine
nicotinamide + [glyceraldehyde-3-phosphate dehydrogenase]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + [histone H2A]-N6-succinyl-L-lysine95
nicotinamide + [histone H2A]-L-lysine95 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H2A]-N6-succinyl-L-lysine9_(4-15)-A10G peptide
nicotinamide + [histone H2A]-L-lysine9_(4-15)-A10G peptide + 2'-O-succinyl-ADP-ribose
partial desuccinylation, mutant peptide substrate
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine116
nicotinamide + [histone H2B]-L-lysine116 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine120
nicotinamide + [histone H2B]-L-lysine120 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine34
nicotinamide + [histone H2B]-L-lysine34 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine9
nicotinamide + [histone H2B]-L-lysine9 + 2'-O-succinyl-ADP-ribose
NAD+ + [histone H3 K9 peptide]-N6-acetyl-L-lysine
nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [histone H3 K9 peptide]-N6-succinyl-L-lysine
nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine122
nicotinamide + [histone H3]-L-lysine122 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine14
nicotinamide + [histone H3]-L-lysine14 + 2'-O-succinyl-ADP-ribose
partial desuccinylation, low activity
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine14_(9-20)-A15G peptide
nicotinamide + [histone H3]-L-lysine14_(9-20)-A15G peptide + 2'-O-succinyl-ADP-ribose
partial desuccinylation, mutant peptide substrate
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine56
nicotinamide + [histone H3]-L-lysine56 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine79
nicotinamide + [histone H3]-L-lysine79 + 2'-O-succinyl-ADP-ribose
partial desuccinylation
-
-
?
NAD+ + [histone H3]-N6-succinyl-L-lysine9
nicotinamide + [histone H3]-L-lysine9 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine16
nicotinamide + [histone H4]-L-lysine16 + 2'-O-acetyl-ADP-ribose
deacetylation, cf. EC 2.3.1.286
-
-
?
NAD+ + [histone H4]-N6-succinyl-L-lysine12
nicotinamide + [histone H4]-L-lysine12 + 2'-O-succinyl-ADP-ribose
partial desuccinylation
-
-
?
NAD+ + [histone H4]-N6-succinyl-L-lysine31
nicotinamide + [histone H4]-L-lysine31 + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [histone H4]-N6-succinyl-L-lysine31_(26-37)-P32A peptide
nicotinamide + [histone H4]-L-lysine31_(26-37)-P32A peptide + 2'-O-succinyl-ADP-ribose
partial desuccinylation, mutant peptide substrate
-
-
?
NAD+ + [histone H4]-N6-succinyl-L-lysine77
nicotinamide + [histone H4]-L-lysine77 + 2'-O-succinyl-ADP-ribose
almost complete desuccinylation
-
-
?
NAD+ + [histone H4]-N6-succinyl-L-lysine91
nicotinamide + [histone H4]-L-lysine91 + 2'-O-succinyl-ADP-ribose
complete desuccinylation
-
-
?
NAD+ + [IDH2]-N6-succinyl-L-lysine
nicotinamide + [IDH2]-L-lysine + 2'-O-succinyl-ADP-ribose
i.e. isocitrate dehydrogenase [NADP+]
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [peptide derived from carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [peptide derived from carbamoyl phosphate synthetase 1]-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-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [PrpE protein]-N6-acetyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-acetyl-ADP ribose
-
-
-
-
?
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
NAD+ + [pyruvate kinase M2]-N6-succinyl-L-lysine311
nicotinamide + [pyruvate kinase M2]-L-lysine311 + 2'-O-succinyl-ADP-ribose
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
additional information
?
-
NAD+ + FKRGVL(N6-acetyl)KEYGVKV
nicotinamide + FKRGVLKEYGVKV + 2'-O-acetyl-ADP-ribose
acetylated peptide derived from carbamoylphosphate synthetase 1 (CPS1)
-
-
?
NAD+ + FKRGVL(N6-acetyl)KEYGVKV
nicotinamide + FKRGVLKEYGVKV + 2'-O-acetyl-ADP-ribose
carbamoyl phosphate synthetase 1 Lys527 peptide
-
-
?
NAD+ + KGLGKGGA(N6-acetyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-acetyl-ADP-ribose
the rate of desuccinylation is about 5fold faster than the rate of deacetylation
-
-
?
NAD+ + KGLGKGGA(N6-acetyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-acetyl-ADP-ribose
-
the rate of desuccinylation is 2.3fold faster than the rate of deacetylation
-
-
?
NAD+ + KGLGKGGA(N6-butyryl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-butyryl-ADP-ribose
the rate of desuccinylation is about 10fold faster than the rate of debutyrylation
-
-
?
NAD+ + KGLGKGGA(N6-butyryl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-butyryl-ADP-ribose
-
the rate of desuccinylation is 5.8fold faster than the rate of deburyrylation
-
-
?
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
the rate of desuccinylation is about 5fold faster than the rate of depropionylation
-
-
?
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
-
the rate of desuccinylation is 3.8fold faster than the rate of depropionylation
-
-
?
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
the rate of desuccinylation is about 5fold faster than the rate of deacetylation
-
-
?
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
-
the rate of desuccinylation is 2.3fold faster than the rate of deacetylation
-
-
?
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
-
deacetylation by CobB activates the acetyl-coenzyme A synthetase
-
-
?
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
-
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle. Deacetylation of CPS1 by SIRT5 results in activation of CPS1 enzymatic activity
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
-
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
SIRT5 plays a pivotal role in ammonia detoxification and disposal by activating carbamoyl phosphate synthetase 1 (CPS1) an enzyme, catalyzing the initial step of the urea cycle for ammonia detoxification and disposal. SIRT5 deacetylates CPS1 and up-regulates its activity. During fasting, NAD+ in liver mitochondria increases, thereby triggering SIRT5 deacetylation of CPS1 and adaptation to the increase in amino acid catabolism. Indeed, SIRT5 KO mice fail to up-regulate CPS1 activity and show elevated blood ammonia during fasting
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
SIRT5 binds to, desuccinylates and activates the key antioxidant enzyme Cu/Zn superoxide dismutase (SOD1). SOD1-mediated reduction of reactive oxygen species (ROS) is increased when SIRT5 is co-expressed. Posttranslational regulation of SOD1 by means of succinylation and SIRT5-dependent desuccinylation is important for the growth of lung tumor cells
-
-
?
NAD+ + [glutaminase]-N6-succinyl-L-lysine
nicotinamide + [glutaminase]-L-lysine + 2'-O-succinyl-ADP-ribose
SIRT5 desuccinylates glutaminase residue K164 to block ubiquitination of K158
-
-
?
NAD+ + [glutaminase]-N6-succinyl-L-lysine
nicotinamide + [glutaminase]-L-lysine + 2'-O-succinyl-ADP-ribose
succinylation of glutaminase residue K164, no activity with K164R-GLS variant
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine9
nicotinamide + [histone H2B]-L-lysine9 + 2'-O-succinyl-ADP-ribose
partial desuccinylation
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine9
nicotinamide + [histone H2B]-L-lysine9 + 2'-O-succinyl-ADP-ribose
partial desuccinylation
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
the enzyme regulates protein function in diverse and often essential cellular processes, most notably translation
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
the enzyme can deacetylate acetyllysine independently whether the acetyl donor is acetyl-Coenzyme A or acetyl phosphate. Linear sequences alone are inadequate to predict CobB substrates and that structural analyses are necessary. CobB substrate acetyllyines appear to be located near the surface of the protein on a
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
weak deacetylase activity
-
-
?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5 in vivo. Lysine succinylation occurs on several mammalian proteins
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
strong succinylase activity
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
-
-
-
-
?
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
-
N-Lysine propionylation controls the activity of propionyl-CoA synthetase
-
-
?
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
-
-
?
NAD+ + [pyruvate kinase M2]-N6-succinyl-L-lysine311
nicotinamide + [pyruvate kinase M2]-L-lysine311 + 2'-O-succinyl-ADP-ribose
SIRT5 desuccinylates and activates PKM2
-
-
?
NAD+ + [pyruvate kinase M2]-N6-succinyl-L-lysine311
nicotinamide + [pyruvate kinase M2]-L-lysine311 + 2'-O-succinyl-ADP-ribose
SIRT5 also desuccinylates recombinant Flag-tagged PKM2 substrate, but does not but affect its malonylation and glutarylation. The K311E mutation and K311E/K498E double mutation of PKM2 both increase the succinylation level of PKM2 by about 25%, while mutations K62R/E, K135R/E, and K498R/E have no significant effect
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
acetylation of the response regulator RcsB controls transcription from the small RNA promoter rprA
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
reversible Nepsilon-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
-
-
?
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
SIRT5 activates urate oxidase through deacetylation in mouse liver mitochondria
-
-
?
additional information
?
-
-
it is proposed that YfiQ and CobB catalyze the reversible acetylation of a protein that mediates carbon-induced cpxP transcription
-
-
?
additional information
?
-
-
global identification of CobB substrates using an Escherichia coli proteome microarray
-
-
?
additional information
?
-
-
the enzyme shows dual enzymatic activities to catalyze the removal of two structurally different lysine acyl groups, acetyl and succinyl, from the modified lysine residues
-
-
?
additional information
?
-
-
global identification of CobB substrates using an Escherichia coli proteome microarray
-
-
?
additional information
?
-
catalytic efficiency (kcat/Km) of Sirt5 with the histone H3K9 acetyl peptide is about 500fold lower than that of Sirt1. Sirtuin 5 has only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr102 and Arg105) that bind to malonylated and succinylated substrates and define the specificity
-
-
?
additional information
?
-
no activity with Ac-Leu-Gly-(N6-acetyl)Lys-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
no activity with Ac-Leu-Gly-(N6-acetyl)Lys-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
Sirt5 does not deacetylate glutamate dehydrogenase or isocitrate dehydrogenase 2
-
-
?
additional information
?
-
-
Sirt5 does not deacetylate glutamate dehydrogenase or isocitrate dehydrogenase 2
-
-
?
additional information
?
-
Sirt5 catalyzes the desuccinylation of histone peptides, molecular mechanism, overview. Human Sirt5 is a ubiquitous desuccinylase that catalyzes the desuccinylation of diverse histone succinyl sites with sequence selectivity. Among the 13 identified sites, H2BK116su is the most favorable Sirt5 substrate, with H4K12su showing the lowest catalytic efficiency and no activity observed in the presence of H4K31su
-
-
-
additional information
?
-
-
Sirt5 catalyzes the desuccinylation of histone peptides, molecular mechanism, overview. Human Sirt5 is a ubiquitous desuccinylase that catalyzes the desuccinylation of diverse histone succinyl sites with sequence selectivity. Among the 13 identified sites, H2BK116su is the most favorable Sirt5 substrate, with H4K12su showing the lowest catalytic efficiency and no activity observed in the presence of H4K31su
-
-
-
additional information
?
-
SIRT5 catalyzes the removal of negatively charged lysine acyl modifications: succinyl, malonyl, and glutaryl groups. SIRT5 is selective only for 3-5 carbon chains acidic acyl modifications, and displays no detectable activity against either an acetyl modification, a neutral 2 carbon group, or an adipoyl, a 6-carbon acidic modification
-
-
-
additional information
?
-
SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II. Mass spectrometry identifies 14 SIRT5 target sites on the SDHA subunit of Complex II and another eight on SDHB. Molecular modeling reveals that six of the eight SIRT5 target sites on SDHB orient toward the predicted membrane interface where SDHB interacts with SDHC/SDHD
-
-
-
additional information
?
-
-
SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II. Mass spectrometry identifies 14 SIRT5 target sites on the SDHA subunit of Complex II and another eight on SDHB. Molecular modeling reveals that six of the eight SIRT5 target sites on SDHB orient toward the predicted membrane interface where SDHB interacts with SDHC/SDHD
-
-
-
additional information
?
-
enzyme activity assay method, overview
-
-
-
additional information
?
-
essential role for the conserved main chain hydrogen bonds formed by the succinyl lysine (0), +1, and +3 sites for substrate-enzyme recognition. A proline residue at the +1 site of the histone succinylation substrate is unfavorable for Sirt5 interaction. Molecular mechanism underlying the sequence-selective desuccinylase activity of Sirt5, overview. No activity with H4K31su, and mutant substrates H3K9(4-15)-S10Psu and H3K56(51-62)-S57Psu. Usage of peptides of histone substrates
-
-
-
additional information
?
-
-
essential role for the conserved main chain hydrogen bonds formed by the succinyl lysine (0), +1, and +3 sites for substrate-enzyme recognition. A proline residue at the +1 site of the histone succinylation substrate is unfavorable for Sirt5 interaction. Molecular mechanism underlying the sequence-selective desuccinylase activity of Sirt5, overview. No activity with H4K31su, and mutant substrates H3K9(4-15)-S10Psu and H3K56(51-62)-S57Psu. Usage of peptides of histone substrates
-
-
-
additional information
?
-
synthsis of substrate peptide (2-Abz)-GVLK (succ)A [Y (3-NO2)]GV-NH2
-
-
-
additional information
?
-
-
synthsis of substrate peptide (2-Abz)-GVLK (succ)A [Y (3-NO2)]GV-NH2
-
-
-
additional information
?
-
Sirt5 shows negligible activity toward lysine deacetylation
-
-
?
additional information
?
-
SIRT5 catalyzes the removal of negatively charged lysine acyl modifications: succinyl, malonyl, and glutaryl groups. SIRT5 is selective only for 3-5 carbon chains acidic acyl modifications, and displays no detectable activity against either an acetyl modification, a neutral 2 carbon group, or an adipoyl, a 6-carbon acidic modification
-
-
-
additional information
?
-
SIRT5 modifies lysine succinylation, malonylation, and glutarylation
-
-
-
additional information
?
-
three-dimensional modeling of Complex II suggests that several SIRT5-targeted lysine residues lie at the protein-lipid interface of succinate dehydrogenase subunit B. Succinylation at these sites may disrupt Complex II subunit-subunit interactions and electron transfer. SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II
-
-
-
additional information
?
-
-
three-dimensional modeling of Complex II suggests that several SIRT5-targeted lysine residues lie at the protein-lipid interface of succinate dehydrogenase subunit B. Succinylation at these sites may disrupt Complex II subunit-subunit interactions and electron transfer. SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II
-
-
-
additional information
?
-
protein malonylation and succinylation lysine sites are identified by immunoprecipitation coupled lipid chromatography-tandem mass spectrometry (LC-MS/MS) methods
-
-
-
additional information
?
-
-
protein malonylation and succinylation lysine sites are identified by immunoprecipitation coupled lipid chromatography-tandem mass spectrometry (LC-MS/MS) methods
-
-
-
additional information
?
-
protein malonylation and succinylation lysine sites are identified by immunoprecipitation coupled lipid chromatography-tandem mass spectrometry (LC-MS/MS) methods
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
-
deacetylation by CobB activates the acetyl-coenzyme A synthetase
-
-
?
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle. Deacetylation of CPS1 by SIRT5 results in activation of CPS1 enzymatic activity
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle
-
-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-succinyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-succinyl-ADP ribose
deletion of Sirt5 in mice increases the level of succinylation on carbamoyl phosphate synthase 1
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
SIRT5 plays a pivotal role in ammonia detoxification and disposal by activating carbamoyl phosphate synthetase 1 (CPS1) an enzyme, catalyzing the initial step of the urea cycle for ammonia detoxification and disposal. SIRT5 deacetylates CPS1 and up-regulates its activity. During fasting, NAD+ in liver mitochondria increases, thereby triggering SIRT5 deacetylation of CPS1 and adaptation to the increase in amino acid catabolism. Indeed, SIRT5 KO mice fail to up-regulate CPS1 activity and show elevated blood ammonia during fasting
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-glutaryl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-glutaryl-ADP-ribose
-
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
SIRT5 binds to, desuccinylates and activates the key antioxidant enzyme Cu/Zn superoxide dismutase (SOD1). SOD1-mediated reduction of reactive oxygen species (ROS) is increased when SIRT5 is co-expressed. Posttranslational regulation of SOD1 by means of succinylation and SIRT5-dependent desuccinylation is important for the growth of lung tumor cells
-
-
?
NAD+ + [forkhead box O3]-N6-acetyl-L-lysine
nicotinamide + [forkhead box O3]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme deacetylates FOXO3 at K271 and K290
-
-
?
NAD+ + [glucose 6-phosphate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [glucose 6-phosphate dehydrogenase]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [glucose-6-phosphate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glucose-6-phosphate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [glutaminase]-N6-succinyl-L-lysine
nicotinamide + [glutaminase]-L-lysine + 2'-O-succinyl-ADP-ribose
SIRT5 desuccinylates glutaminase residue K164 to block ubiquitination of K158
-
-
?
NAD+ + [histone H2B]-N6-succinyl-L-lysine9
nicotinamide + [histone H2B]-L-lysine9 + 2'-O-succinyl-ADP-ribose
partial desuccinylation
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine16
nicotinamide + [histone H4]-L-lysine16 + 2'-O-acetyl-ADP-ribose
deacetylation, cf. EC 2.3.1.286
-
-
?
NAD+ + [IDH2]-N6-succinyl-L-lysine
nicotinamide + [IDH2]-L-lysine + 2'-O-succinyl-ADP-ribose
i.e. isocitrate dehydrogenase [NADP+]
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-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-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
-
N-Lysine propionylation controls the activity of propionyl-CoA synthetase
-
-
?
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
-
-
?
NAD+ + [pyruvate kinase M2]-N6-succinyl-L-lysine311
nicotinamide + [pyruvate kinase M2]-L-lysine311 + 2'-O-succinyl-ADP-ribose
SIRT5 desuccinylates and activates PKM2
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
-
-
?
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
SIRT5 activates urate oxidase through deacetylation in mouse liver mitochondria
-
-
?
additional information
?
-
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [ATP synthase]-N6-succinyl-L-lysine
nicotinamide + [ATP synthase]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
the enzyme regulates protein function in diverse and often essential cellular processes, most notably translation
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
weak deacetylase activity
-
-
?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5 in vivo. Lysine succinylation occurs on several mammalian proteins
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
strong succinylase activity
-
-
?
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
acetylation of the response regulator RcsB controls transcription from the small RNA promoter rprA
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
reversible Nepsilon-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
additional information
?
-
-
it is proposed that YfiQ and CobB catalyze the reversible acetylation of a protein that mediates carbon-induced cpxP transcription
-
-
?
additional information
?
-
Sirt5 catalyzes the desuccinylation of histone peptides, molecular mechanism, overview. Human Sirt5 is a ubiquitous desuccinylase that catalyzes the desuccinylation of diverse histone succinyl sites with sequence selectivity. Among the 13 identified sites, H2BK116su is the most favorable Sirt5 substrate, with H4K12su showing the lowest catalytic efficiency and no activity observed in the presence of H4K31su
-
-
-
additional information
?
-
-
Sirt5 catalyzes the desuccinylation of histone peptides, molecular mechanism, overview. Human Sirt5 is a ubiquitous desuccinylase that catalyzes the desuccinylation of diverse histone succinyl sites with sequence selectivity. Among the 13 identified sites, H2BK116su is the most favorable Sirt5 substrate, with H4K12su showing the lowest catalytic efficiency and no activity observed in the presence of H4K31su
-
-
-
additional information
?
-
SIRT5 catalyzes the removal of negatively charged lysine acyl modifications: succinyl, malonyl, and glutaryl groups. SIRT5 is selective only for 3-5 carbon chains acidic acyl modifications, and displays no detectable activity against either an acetyl modification, a neutral 2 carbon group, or an adipoyl, a 6-carbon acidic modification
-
-
-
additional information
?
-
SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II. Mass spectrometry identifies 14 SIRT5 target sites on the SDHA subunit of Complex II and another eight on SDHB. Molecular modeling reveals that six of the eight SIRT5 target sites on SDHB orient toward the predicted membrane interface where SDHB interacts with SDHC/SDHD
-
-
-
additional information
?
-
-
SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II. Mass spectrometry identifies 14 SIRT5 target sites on the SDHA subunit of Complex II and another eight on SDHB. Molecular modeling reveals that six of the eight SIRT5 target sites on SDHB orient toward the predicted membrane interface where SDHB interacts with SDHC/SDHD
-
-
-
additional information
?
-
SIRT5 catalyzes the removal of negatively charged lysine acyl modifications: succinyl, malonyl, and glutaryl groups. SIRT5 is selective only for 3-5 carbon chains acidic acyl modifications, and displays no detectable activity against either an acetyl modification, a neutral 2 carbon group, or an adipoyl, a 6-carbon acidic modification
-
-
-
additional information
?
-
SIRT5 modifies lysine succinylation, malonylation, and glutarylation
-
-
-
additional information
?
-
three-dimensional modeling of Complex II suggests that several SIRT5-targeted lysine residues lie at the protein-lipid interface of succinate dehydrogenase subunit B. Succinylation at these sites may disrupt Complex II subunit-subunit interactions and electron transfer. SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II
-
-
-
additional information
?
-
-
three-dimensional modeling of Complex II suggests that several SIRT5-targeted lysine residues lie at the protein-lipid interface of succinate dehydrogenase subunit B. Succinylation at these sites may disrupt Complex II subunit-subunit interactions and electron transfer. SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S)-2-[(naphthalen-2-yl)sulfanyl]-4-oxo-4-[(3-phenylpropyl)amino]butanoic acid
-
(2S)-4-(benzylamino)-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
-
(2S)-4-(butylamino)-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
-
(2S)-4-[3-(methylcarbamoyl)anilino]-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
-
(2S)-4-[[(5S)-5-acetamido-6-amino-6-oxohexyl]amino]-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
-
(3E)-3-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-5-iodo-1,3-dihydro-2H-indol-2-one
-
(5E)-1-ethyl-5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(5E)-5-(1H-indol-3-ylmethylidene)-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(5E)-5-[4-(benzyloxy)benzylidene]-1-ethyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(5E)-5-[4-(benzyloxy)benzylidene]-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-sulfanylidene-1,3-diazinane-4,6-dione
-
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(N6-thiosuccinyl)KSTGGKA
-
1,8-dihydroxyanthracen-9(10H)-one
-
1-(2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)-3-phenylurea
10% inhibition at 0.1 mM
2-cyano-3-[5-(4-cyanophenyl)furan-2-yl]-N-(3,4-dimethylphenyl)propanamide
-
2-cyano-N-(3,4-dimethylphenyl)-3-[5-(4-nitrophenyl)furan-2-yl]propanamide
-
3',5'-dimethyl-1'-phenyl-1H,1'H-[3,4'-bipyrazole]-5-carboxylic acid
21.54% inhibition at 0.1 mM
3-(((2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)amino)methyl)benzoic acid
32% inhibition at 0.1 mM
3-((2-(9H-pyrido[3,4-b]indol-9-yl)acetamido)methyl)benzoic acid
21% inhibition at 0.1 mM
3-((2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)carbamoyl)benzoicacid
15% inhibition at 0.1 mM
3-(3,5-dibromo-4-hydroxybenzyliden)-5-iodo-1,3-dihydroindol-2-one
i.e. GW5074, potent inhibitor for desuccinylation activity of Sirt5. 0.1 mM inhibitor reduces Sirt5 desuccinylation activity (substrate: SKEYFS-(succinylLys)-QK) to about 15%. Weaker effects in Sirt5 deacetylation assays. Deacetylation activity is reduced to about 30% in presence of 0.1 mM inhibitor
3-(3-(2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)ureido)benzoic acid
36% inhibition at 0.1 mM
3-chloro-5-(3,4-dimethoxyphenyl)-7-(trifluoromethyl)pyrazolo[1,5-a]pyrimidine-2-carboxylic acid
30.85% inhibition at 0.1 mM
3-hydroxy-5-(morpholine-4-sulfonyl)naphthalene-2-carboxylic acid
9.2% inhibition at 0.1 mM
3-hydroxy-5-[(prop-2-en-1-yl)sulfamoyl]naphthalene-2-carboxylic acid
17.43% inhibition at 0.1 mM
3-[3-[5-(4-carboxyphenyl)furan-2-yl]-2-cyanopropanamido]benzoic acid
-
3-[5-[2-cyano-3-(3,4-dimethylanilino)-3-oxopropyl]furan-2-yl]benzoic acid
-
4-(((2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)amino)methyl)benzoic acid
22% inhibition at 0.1 mM
4-((2-(9H-pyrido[3,4-b]indol-9-yl)acetamido)methyl)benzoic acid
25% inhibition at 0.1 mM
4-((2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)carbamoyl)benzoic acid
25% inhibition at 0.1 mM
4-(3,4-dimethyl-6-oxopyrano[2,3-c]pyrazol-1(6H)-yl)benzoic acid
18.70% inhibition at 0.1 mM
4-(3-(2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)ureido)benzoic acid
52% inhibition at 0.1 mM
4-(5-[(Z)-[1-(3-chloro-4-methylphenyl)-3-methyl-5-oxo-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]furan-2-yl)benzoic acid
94.3% inhibition at 0.1 mM
4-(5-[2-cyano-3-[(2,3-dihydro-1,4-benzodioxin-6-yl)amino]-3-oxopropyl]furan-2-yl)benzoic acid
-
4-(5-[2-cyano-3-[3-(methylcarbamoyl)anilino]-3-oxopropyl]furan-2-yl)benzoic acid
-
4-(5-[2-cyano-3-[4-cyano-3-(trifluoromethyl)anilino]-3-oxopropyl]furan-2-yl)benzoic acid
-
4-(5-[3-[(2H-1,3-benzodioxol-5-yl)amino]-2-cyano-3-oxopropyl]furan-2-yl)benzoic acid
-
4-(5-[3-[4-chloro-3-(trifluoromethyl)anilino]-2-cyano-3-oxopropyl]furan-2-yl)benzoic acid
-
4-(6-tert-butyl-2H-1,3-benzoxazin-3(4H)-yl)benzoic acid
24.54% inhibition at 0.1 mM
4-([(Z)-[2-(2-bromophenyl)-5-oxo-1,3-oxazol-4(5H)-ylidene]methyl]amino)benzoic acid
34.24% inhibition at 0.1 mM
4-[(4Z)-3-methyl-5-oxo-4-[(2E)-3-phenylprop-2-en-1-ylidene]-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
77.26% inhibition at 0.1 mM
4-[(E)-(4-hydroxyphenyl)diazenyl]benzoic acid
51.3% inhibition at 0.1 mM
4-[(E)-(6-hydroxyquinolin-5-yl)diazenyl]benzoic acid
61.3% inhibition at 0.1 mM
4-[(E)-[(4-bromo-3-chloro-2-hydroxyphenyl)methylidene]amino]benzoic acid
33.66% inhibition at 0.1 mM
4-[5-[(1E)-3-(4-chloro-3-nitroanilino)-2-cyano-3-oxoprop-1-en-1-yl]furan-2-yl]benzoic acid
97.14% inhibition at 0.1 mM
4-[5-[2-cyano-3-(3,4-dimethoxyanilino)-3-oxopropyl]furan-2-yl]benzoic acid
-
4-[5-[2-cyano-3-(3,4-dimethylanilino)-3-oxopropyl]furan-2-yl]-3-fluorobenzoic acid
-
4-[5-[2-cyano-3-(3,4-dimethylanilino)-3-oxopropyl]furan-2-yl]-3-methylbenzoic acid
-
4-[5-[2-cyano-3-(3,4-dimethylanilino)-3-oxopropyl]furan-2-yl]benzoic acid
-
4-[5-[2-cyano-3-(3,5-dichloroanilino)-3-oxopropyl]furan-2-yl]benzoic acid
-
4-[5-[2-cyano-3-(3,5-dimethylanilino)-3-oxopropyl]furan-2-yl]benzoic acid
-
4-[5-[2-cyano-3-(4-cyano-3-fluoroanilino)-3-oxopropyl]furan-2-yl]benzoic acid
4-[5-[3-(3-acetamidoanilino)-2-cyano-3-oxopropyl]furan-2-yl]benzoic acid
-
5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-(4-hydroxy-2,2-dimethyloxan-4-yl)-1,2-oxazole-3-carboxylic acid
17.41% inhibition at 0.1 mM
5-(4-methylphenyl)-7-(trifluoromethyl)pyrazolo[1,5-a]pyrimidine-2-carboxylic acid
11.08% inhibition at 0.1 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
-
5-[(5-[[(benzyloxy)carbonyl]amino]-6-[(diphenylmethyl)amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
-
5-[(5-[[(benzyloxy)carbonyl]amino]-6-[[(naphthalen-1-yl)methyl]amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
-
5-[(5-[[(benzyloxy)carbonyl]amino]-6-[[2-(1H-indol-3-yl)ethyl]amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
-
5-[(6-amino-5-[[(benzyloxy)carbonyl]amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
-
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[(6-[(1,3-benzothiazol-5-yl)amino]-5-[[(benzyloxy)carbonyl]amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
-
5-[(6-[(adamantan-1-yl)amino]-5-[[(benzyloxy)carbonyl]amino]-6-oxohexyl)amino]-5-sulfanylidenepentanoic acid
-
5-[(E)-(5-hydroxy-3-methyl-1-phenyl-1H-pyrazol-4-yl)diazenyl]-4H-pyrazole-3-carboxylic acid
70.03% inhibition at 0.1 mM
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[4-(propan-2-yl)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
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-[[4-(benzyloxy)phenyl]methylidene]-2-sulfanylidene-1,3-diazinane-4,6-dione
-
5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
5-[[5-[[(benzyloxy)carbonyl]amino]-6-oxo-6-([(1S)-2-oxo-1-phenyl-2-[(propan-2-yl)amino]ethyl]amino)hexyl]amino]-5-sulfanylidenepentanoic acid
-
6-carboxy-5-methyl-3-[2-(3-methylpiperidin-1-yl)-2-oxoethyl]-4-oxo-4,4a-dihydrothieno[2,3-d]pyrimidin-3-ium
15.43% inhibition at 0.1 mM
7-(diethylamino)-2-oxo-2H-1-benzopyran-3-carboxylic acid
28.91% inhibition at 0.1 mM
Ac-AR(N6-thiosuccinyl)KST-NH2
-
Ac-RR(N6-thiosuccinyl)KRR-NH2
-
AGK2
40% inhibition at 0.1 mM
benzoyl-GVL(N6-(3-acetylthiosuccinyl))KEYGV-amide
-
benzoyl-GVL(N6-(3-butylsuccinyl))KEYGV-amide
-
benzoyl-GVL(N6-(3-methyl-3-phenyl)succinyl)KEYGV-amide
-
benzoyl-GVL(N6-(3-phenyl)succinyl)KEYGV-amide
-
benzoyl-GVL(N6-(N-benzyloxycarbonyl-L-aspartyl))KEYGV-amide
-
benzoyl-GVL(N6-(N-phthaloyl-DL-gamma-glutamyl))KEYGV-amide
-
benzoyl-GVL(N6-(N2-Fmoc-beta-L-aspartyl))KEYGV-amide
-
ethyl 4-[[2-(9H-pyrido[3,4-b]indol-9-yl)acetamido]methyl]benzoate
12% inhibition at 0.1 mM
GW5074
85% inhibition at 0.1 mM
KQTAR(N6-thiosuccinyl)K
-
KQTAR(N6-thiosuccinyl)KSTGGKA
-
L-lysyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-N6-(3-carboxypropanethioyl)-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanine
-
methyl 4-[5-[2-cyano-3-(3,4-dimethylanilino)-3-oxopropyl]furan-2-yl]benzoate
-
N-(2-(9H-pyrido[3,4-b]indol-9-yl)ethyl)benzamide
7% inhibition at 0.1 mM
N-(4-chlorobenzyl)-2-(9H-pyrido[3,4-b]indol-9-yl)acetamide
18% inhibition at 0.1 mM
N-(pyridin-3-ylmethyl)-2-(9H-pyrido[3,4-b]indol-9-yl)acetamide
24% inhibition at 0.1 mM
N-([4-[(3S,6S,9S)-9-acetamido-27-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]carbamoyl]-6-(3-carbamimidamidopropyl)-2,5,8,14,21-pentaoxo-1,4,7,13,22-pentaazacycloheptacosan-3-yl]butyl]carbamothioyl)-beta-alanine
-
N-acetyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alaninamide
-
N-acetyl-L-leucyl-N6-[3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alaninamide
-
N-benzyl-2-(9H-pyrido[3,4-b]indol-9-yl)acetamide
8% inhibition at 0.1 mM
N-benzyl-2-(9H-pyrido[3,4-b]indol-9-yl)ethan-1-amine
10% inhibition at 0.1 mM
N-benzylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-phenylbutanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyrazin-2-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyridin-2-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyridin-4-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-4-phenylbutanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(cyclohexylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-([[3-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,3-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,6-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2-phenylethyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,4-dimethylphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3-phenylpropyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(4-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-1-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2,4,6-trimethylphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(3,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(3-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-methoxyphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(naphthalen-1-yl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[2-(3,5-dimethyl-1,2-oxazol-4-yl)ethyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-[[(4-tert-butylphenyl)methyl]sulfanyl]-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R-3-carboxy-3-[(3,4-dimethoxyphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(cyclohexylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-([[3-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,3-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,6-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2-phenylethyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dimethoxyphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dimethylphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3-phenylpropyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(4-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-1-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2,4,6-trimethylphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(3,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(3-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-methoxyphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(naphthalen-1-yl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[2-(3,5-dimethyl-1,2-oxazol-4-yl)ethyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-[[(4-tert-butylphenyl)methyl]sulfanyl]-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-[(7S)-7-[[(benzyloxy)carbonyl]amino]-8-([(2S)-3-(1H-indol-3-yl)-1-oxo-1-[(propan-2-yl)amino]propan-2-yl]amino)-8-oxooctanoyl]-beta-alanine
-
N-[(benzyloxy)carbonyl]-5-[2-(4-carboxybutanoyl)hydrazinyl]-L-norvalyl-N-propan-2-yl-L-tryptophanamide
-
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-threonyl-L-threonyl-L-alpha-aspartyl-L-serylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-threonyl-L-threonyl-L-alpha-aspartyl-L-serylglycyl-L-valyl-L-leucyl-N6-[3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N2-(benzenesulfonyl)-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-L-tryptophanamide
-
N2-(benzylcarbamoyl)-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-L-tryptophanamide
-
N2-benzoyl-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxy-2,2-difluorobutanoyl)-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-L-tryptophyl-L-aspartamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-L-tryptophyl-L-phenylalaninamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-L-tyrosinamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-N-propan-2-yl-D-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-N-propan-2-yl-L-alaninamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-N-propan-2-yl-L-prolinamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-N-propan-2-yl-L-tryptophanamide
enzyme binding structure, crystal structure analysis
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysyl-N-[(2S)-1,4-diamino-1-oxobutan-2-yl]-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-(4-carboxybutanethioyl)lysylglycinamide
-
N2-[(benzyloxy)carbonyl]-N6-ethanethioyl-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethoxy)carbonyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-N-adamantan-1-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-N-cyclopropyl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
enzyme binding structure, crystal structure analysis
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamothioyl]-L-lysyl-N-[(2S)-1-methoxy-3-phenylpropan-2-yl]-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(2-carboxyethyl)carbamoyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(3R)-4-carboxy-3-methylbutanoyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(3S)-4-carboxy-3-methylbutanoyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-N6-[(carboxymethyl)carbamothioyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(3-fluorobenzene-1-sulfonyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(3-fluorobenzene-1-sulfonyl)-L-lysyl-N-cyclobutyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(3-fluorobenzene-1-sulfonyl)-L-lysyl-N-cyclopentyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(3-fluorobenzene-1-sulfonyl)-L-lysyl-N-cyclopropyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(3-phenylpropanoyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(4-methoxybenzene-1-sulfonyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(4-nitrobenzene-1-sulfonyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(naphthalene-2-sulfonyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(phenylacetyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(phenylcarbamoyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-(quinoline-8-sulfonyl)-L-lysyl-L-tryptophanamide
-
N6-[(2-carboxyethyl)carbamothioyl]-N2-[4-(trifluoromethyl)benzene-1-sulfonyl]-L-lysyl-L-tryptophanamide
-
N6-[N-[(benzyloxy)carbonyl]-L-gamma-glutamyl]-N2-[(benzyloxy)carbonyl]-L-lysyl-N-propan-2-yl-L-tryptophanamide
-
4-[5-[2-cyano-3-(4-cyano-3-fluoroanilino)-3-oxopropyl]furan-2-yl]benzoic acid
competitive inhibitor
4-[5-[2-cyano-3-(4-cyano-3-fluoroanilino)-3-oxopropyl]furan-2-yl]benzoic acid
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
-
nicotinamide
-
nicotinamide
nicotinamide inhibition of Sirt5-dependent deacetylation features weak substrate-dependence but requires high, nonphysiological nicotinamide concentrations. The insensitivity of Sirt5 to physiological nicotinamide concentrations is due to a lack of non-competitive inhibition via base exchange, and the inhibition observed at very high nicotinamide concentrations is likely caused by competition with NAD+
nicotinamide
competitive inhibition
nicotinamide
NAM, 70.57% inhibition at 0.1 mM
nicotinamide
NAM, feedback inhibitor. NAM is a pan sirtuin inhibitor
nicotinamide
inhibits demalonylation and desuccinylation activity
nicotinamide
NAM, feedback inhibitor. NAM is a pan sirtuin inhibitor
suramin
-
suramin
suramin binds into the NAD+-, the product-, and the substrate-binding site
additional information
the acyl-substrate specificity of SIRT5 is adapted to selectively inhibit this isozyme. Synthesis and evaluation of mechanism-based inhibitors of SIRT5, structure-activity relationship, overview
-
additional information
-
the acyl-substrate specificity of SIRT5 is adapted to selectively inhibit this isozyme. Synthesis and evaluation of mechanism-based inhibitors of SIRT5, structure-activity relationship, overview
-
additional information
no inhibition by EX-527, HR 103 or Ro 31-8220
-
additional information
H3K9TAc and sirtinol show no inhibnition at 0.1 mM
-
additional information
-
H3K9TAc and sirtinol show no inhibnition at 0.1 mM
-
additional information
not inhibited by EX527 (i.e. 6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide)
-
additional information
-
not inhibited by EX527 (i.e. 6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide)
-
additional information
the acyl-substrate specificity of SIRT5 is adapted to selectively inhibit this isozyme. Synthesis and evaluation of mechanism-based inhibitors of SIRT5, structure-activity relationship, overview
-
additional information
-
the acyl-substrate specificity of SIRT5 is adapted to selectively inhibit this isozyme. Synthesis and evaluation of mechanism-based inhibitors of SIRT5, structure-activity relationship, overview
-
additional information
no inhibition by (2E)-4,4-dihydroxy-N-[4-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]phenyl]but-2-enamide; structure-based discovery of selective small-molecul sirtuin 5 inhibitors. Synthesis of (E)-2-cyano-N-phenyl-3-(5-phenylfuran-2-yl)acrylamide derivatives/analogues, docking study, structure-activity relationship analyses, overview. No inhibition by 14 at 0.1 mM
-
additional information
-
no inhibition by (2E)-4,4-dihydroxy-N-[4-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]phenyl]but-2-enamide; structure-based discovery of selective small-molecul sirtuin 5 inhibitors. Synthesis of (E)-2-cyano-N-phenyl-3-(5-phenylfuran-2-yl)acrylamide derivatives/analogues, docking study, structure-activity relationship analyses, overview. No inhibition by 14 at 0.1 mM
-
additional information
SIRT can be targeted by small molecules, structure-activity relationship study leading to identification of SIRT5 selective inhibitors that exhibit sub-micromolar potency via a slow, tight-binding mechanism
-
additional information
design and synthesis of 9-substituted norharmane derivatives as potential Sirt5 inhibitors, molceular docking, overview
-
additional information
analysis of potent and selective inhibitors of human sirtuin 5, screening and synthesis of 3-arylthiosuccinylated and 3-benzylthiosuccinylated peptide derivatives yielding Sirt5 inhibitors with low-nanomolar Ki values, overview. Crystal structures of Sirt5/ inhibitor complexes reveal that the compounds bind in to the active site of Sirt5. Molecular docking study, computational analysis
-
additional information
-
analysis of potent and selective inhibitors of human sirtuin 5, screening and synthesis of 3-arylthiosuccinylated and 3-benzylthiosuccinylated peptide derivatives yielding Sirt5 inhibitors with low-nanomolar Ki values, overview. Crystal structures of Sirt5/ inhibitor complexes reveal that the compounds bind in to the active site of Sirt5. Molecular docking study, computational analysis
-
additional information
SIRT can be targeted by small molecules, structure-activity relationship study leading to identification of SIRT5 selective inhibitors that exhibited sub-micromolar potency via a slow, tight-binding mechanism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.07256
(2S)-2-[(naphthalen-2-yl)sulfanyl]-4-oxo-4-[(3-phenylpropyl)amino]butanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.124
(2S)-4-(benzylamino)-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.01572 - 0.154
(2S)-4-(butylamino)-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
0.09
(2S)-4-[3-(methylcarbamoyl)anilino]-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.074
(2S)-4-[[(5S)-5-acetamido-6-amino-6-oxohexyl]amino]-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0195
(3E)-3-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-5-iodo-1,3-dihydro-2H-indol-2-one
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0559
(5E)-1-ethyl-5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.027
(5E)-5-(1H-indol-3-ylmethylidene)-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0673
(5E)-5-[4-(benzyloxy)benzylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0129
(5E)-5-[4-(benzyloxy)benzylidene]-1-ethyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0178
(5E)-5-[4-(benzyloxy)benzylidene]-1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0023
(5E)-5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-sulfanylidene-1,3-diazinane-4,6-dione
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0023
(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
0.001
(N6-thiosuccinyl)KSTGGKA
Homo sapiens
pH and temperature not specified in the publication
0.0001
1,8-dihydroxyanthracen-9(10H)-one
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0195 - 0.097
3-(3,5-dibromo-4-hydroxybenzyliden)-5-iodo-1,3-dihydroindol-2-one
0.0056
4-[5-[2-cyano-3-(4-cyano-3-fluoroanilino)-3-oxopropyl]furan-2-yl]benzoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0465
5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.03
5-(biphenyl-4-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0166
5-[(1-benzyl-1H-indol-3-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0224
5-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0126
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0394
5-[4-(propan-2-yl)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0124
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0062
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.0126
5-[[4-(benzyloxy)phenyl]methylidene]-2-sulfanylidene-1,3-diazinane-4,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0036
5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
pH 8.0, 37°C
0.04
Ac-AR(N6-thiosuccinyl)KST-NH2
Homo sapiens
pH and temperature not specified in the publication
0.025
Ac-RR(N6-thiosuccinyl)KRR-NH2
Homo sapiens
pH and temperature not specified in the publication
0.03
AR(N6-thiosuccinyl)KST
Homo sapiens
pH and temperature not specified in the publication
0.0111 - 0.0347
Isonicotinamide
0.001
KQTAR(N6-thiosuccinyl)K
Homo sapiens
pH and temperature not specified in the publication
0.005
KQTAR(N6-thiosuccinyl)KSTGGKA
Homo sapiens
pH and temperature not specified in the publication
0.005
L-lysyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-N6-(3-carboxypropanethioyl)-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanine
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0075
N-([4-[(3S,6S,9S)-9-acetamido-27-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]carbamoyl]-6-(3-carbamimidamidopropyl)-2,5,8,14,21-pentaoxo-1,4,7,13,22-pentaazacycloheptacosan-3-yl]butyl]carbamothioyl)-beta-alanine
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00035
N-acetyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alaninamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001075
N-acetyl-L-leucyl-N6-[3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alaninamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.022803
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyrazin-2-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.006966
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyridin-2-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.013244
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-3-[[2-(pyridin-4-yl)ethyl]sulfanyl]propanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001122
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-(3-carboxy-4-phenylbutanoyl)-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000644
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.014
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(cyclohexylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001799
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001148
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-([[3-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002203
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.003388
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,3-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002013
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.012503
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2,6-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.003097
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000592
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(2-phenylethyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001607
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001259
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,4-dimethylphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000647
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001384
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002061
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(3-phenylpropyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001614
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(4-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002196
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-1-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00009
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00181
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000631
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2,4,6-trimethylphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000432
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000352
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(2-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00078
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(3,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002673
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(3-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001021
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001112
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-methoxyphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0004027
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(4-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000207
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[(naphthalen-1-yl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.018493
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-carboxy-3-[[2-(3,5-dimethyl-1,2-oxazol-4-yl)ethyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001236
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R)-3-[[(4-tert-butylphenyl)methyl]sulfanyl]-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.009078
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3R-3-carboxy-3-[(3,4-dimethoxyphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000336
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-(benzylsulfanyl)-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.004
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(cyclohexylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000274
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-(phenylsulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001125
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-([[3-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000804
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000715
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,3-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000177
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000295 - 0.001977
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
0.000577
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,6-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000857
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.002742
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2-phenylethyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000046
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000326
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dimethoxyphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000046
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,4-dimethylphenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000086
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00012
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00113
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(3-phenylpropyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000102
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(4-chlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000095
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-1-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000059
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00003
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0052
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2,4,6-trimethylphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000543
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000533
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(2-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00074
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(3,4-dichlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00271
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(3-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000893
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-chlorophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001047
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-methoxyphenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.003732
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(4-nitrophenyl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000015
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[(naphthalen-1-yl)methyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.00875
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[[2-(3,5-dimethyl-1,2-oxazol-4-yl)ethyl]sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.000793
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-[[(4-tert-butylphenyl)methyl]sulfanyl]-3-carboxypropanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.04
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[3-[(naphthalen-2-yl)sulfanyl]butanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.04
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0000191
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-threonyl-L-threonyl-L-alpha-aspartyl-L-serylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0000911
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-threonyl-L-threonyl-L-alpha-aspartyl-L-serylglycyl-L-valyl-L-leucyl-N6-[3-carboxy-3-[(naphthalen-2-yl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.01572
(2S)-4-(butylamino)-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.154
(2S)-4-(butylamino)-2-[(naphthalen-2-yl)sulfanyl]-4-oxobutanoic acid
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.0195
3-(3,5-dibromo-4-hydroxybenzyliden)-5-iodo-1,3-dihydroindol-2-one
Homo sapiens
pH 7.5, temperature not specified in the publication, substrate: SKEYFS-(succinylLys)-QK
0.097
3-(3,5-dibromo-4-hydroxybenzyliden)-5-iodo-1,3-dihydroindol-2-one
Homo sapiens
pH 7.5, temperature not specified in the publication, substrate: FKRGVL-(acetylLys)-EYGVKV
0.0425
cambinol
Homo sapiens
pH and temperature not specified in the publication
0.043
cambinol
Homo sapiens
pH 8.0, 37°C
0.0111
Isonicotinamide
Homo sapiens
wild type enzyme, with 0.05 mM NAD+, at 8.0 pH and 25°C
0.0347
Isonicotinamide
Homo sapiens
wild type enzyme, at 8.0 pH and 25°C
0.000295
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.001977
N-benzylglycylglycyl-L-valyl-L-leucyl-N6-[(3S)-3-carboxy-3-[(2,5-dichlorophenyl)sulfanyl]propanoyl]-L-lysyl-L-alpha-glutamyl-L-tyrosylglycyl-L-valinamide
Homo sapiens
pH 7.8, 37°C, recombinant enzyme
0.021
nicotinamide
Homo sapiens
pH 7.8, 37°C, substrate: benzoyl-RGVL(succK)EYGV-amide
0.0457
nicotinamide
Homo sapiens
pH 8.0, 37°C, recombinant enzyme
0.0466
nicotinamide
Homo sapiens
pH and temperature not specified in the publication
0.047
nicotinamide
Homo sapiens
pH 8.0, 37°C
0.15
nicotinamide
Homo sapiens
pH and temperature not specified in the publication
0.7
nicotinamide
Homo sapiens
pH 7.8, 37°C, substrate: TRSG(acK)VMR
1.6
nicotinamide
Homo sapiens
pH 7.8, 37°C, substrate: FKRGVL(acK)EYGVKV
0.0489
sirtinol
Homo sapiens
pH and temperature not specified in the publication
0.049
sirtinol
Homo sapiens
pH 8.0, 37°C
0.0142
suramin
Homo sapiens
pH 7.5, temperature not specified in the publication, substrate: acetylated peptide derived from carbamoylphosphate synthetase 1 (CPS1)
0.022
suramin
Homo sapiens
pH and temperature not specified in the publication
0.025
suramin
Homo sapiens
pH and temperature not specified in the publication
0.0466
suramin
Homo sapiens
pH and temperature not specified in the publication
0.047
suramin
Homo sapiens
pH 8.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
in mammals, the sirtuin family comprises seven members (SIRT1-7), which possess conserved NAD+-binding and catalytic domains, while their flanking N- and C-termini are distinct from one another, and contribute to differences in subcellular localization, enzymatic activity, and substrate specificity among sirtuin proteins. Phylogenetically, SIRT5 is distinct from other mammalian sirtuins, and belongs to the so-called class III sirtuin family, a family that includes mostly prokaryotic sirtuins. Mouse Sirt5 gene encodes a single protein of 310 amino acids, corresponding to human SIRT5 isoform 1
evolution
in mammals, the sirtuin family comprises seven members (SIRT1-7), which possess conserved NAD+-binding and catalytic domains, while their flanking N- and C-termini are distinct from one another, and contribute to differences in subcellular localization, enzymatic activity, and substrate specificity among sirtuin proteins. Phylogenetically, SIRT5 is distinct from other mammalian sirtuins, and belongs to the so-called class III sirtuin family, a family that includes mostly prokaryotic sirtuins. The human SIRT5 gene encodes two main SIRT5 isoforms, SIRT5iso1 and SIRT5iso2 comprising 310 amino acids and 299 amino acids respectively, which differ slightly from one other at their C-termini, two other human SIRT5 isoforms (SIRT5iso3 and SIRT5iso4) have been reported. SIRT5iso3 is identical to SIRT5iso1 except that it lacks an internal sequence of 18 amino acids, while in SIRT5iso4 the initial 108 amino acids of SIRT5iso1 are missing, including the mitochondrial localization sequence. SIRT5iso4 completely aligns with amino acids 109-310 of SIRT5iso1. SIRT5 polymorphisms may impact human lifespan. Presence of a single-nucleotide polymorphism (SNP) (rs9382222) in a conserved region of the SIRT5 promoter correlates with reduced SIRT5 mRNA expression levels in the anterior cingulate cortex (ACC) region of the brain in individuals with the CC genotype relative to individuals with the CT genotype. SNP rs2841505 is associated with slightly reduced lifespan in cohort members with a GG genotype compared to those with other genotypes. Another SIRT5 SNP, rs4712047, displays gender-specific impact on the lifespan, females with a GG genotype exhibited an increased lifespan compared to those with a GA or a AA genotype, whereas males with a GG genotype display decreased lifespan compared to males with the other genotypes. Association of SIRT5 SNP rs2253217 with human lifespan, cohort members with TT genotype live longer than those with TC or CC genotype
evolution
mammals possess seven sirtuin family members (SIRT1-SIRT7), which display diverse subcellular localization patterns, catalytic activities, protein targets, and biological functions
evolution
SIRT5 gene encodes for four SIRT5 protein isoforms, namely SIRT5iso1, SIRT5iso2, SIRT5iso3, and SIRT5iso4
evolution
sirtuins (SIRTs) are proteins that possess nicotinxadamide-adenine dinucleotide-dependent deacetylase activity and belong to the histone deacetylase (HDAC) family, which consist of seven different subtypes in mammals (SIRT1-7)
evolution
sirtuins are a family of NAD+-dependent silent information regulator 2 (Sir2) enzymes that catalyze the removal of acyl groups from epsilon-N-amino groups of lysine residues in the proteome
evolution
sirtuins are a family of NAD+-dependent silent information regulator 2 (Sir2) enzymes that catalyze the removal of acyl groups from epsilon-N-amino groups of lysine residues in the proteome
evolution
sirtuins, which are class III histone deacetylases (HDACs), are an evolutionarily conserved family of NAD-dependent lysine deacetylases that play important roles in the regulation of aging, tumorigenesis, energy metabolism and stress resistance
malfunction
-
acetyl-coenzyme A synthetase overproduced by the cobB deletion mutant strain contains acetyllysine at residue Lys609
malfunction
-
CobB knockout cells show slightly increased acetylation levels and succinylation levels relative to the wild type cells
malfunction
deletion of Sirt5 in mice increases the level of succinylation on carbamoyl phosphate synthase 1
malfunction
-
RcsB protein isolated from a cobB deletion mutation strain is hyperacetylated
malfunction
SIRT5 knockdown in cardiomyocytes results in a marked reduction in cell viability, and a significant increase in the number of apoptotic cells
malfunction
SIRT5 knockdown represses lung cancer cell growth and transformation in vitro and in vivo. SIRT5 knockdown makes lung cancer cells more sensitive to drug (cis-diamminedichloroplatinum, 5-fluorouracil or bleomycin) treatment in vitro and in vivo. Nrf2, which is a core transcription factor for lung cancer growth and drug resistance, is a target of SIRT5
malfunction
-
knockdown or knockout of the enzyme leads to high levels of cellular reactive oxygen species. SIRT5 inactivation leads to the inhibition of isocitrate dehydrogenase 2 and glucose-6-phosphate dehydrogenase, thereby decreasing NADPH production, lowering GSH, impairing the ability to scavenge ROS, and increasing cellular susceptibility to oxidative stress
malfunction
because these modifications by Sirt5 cover a broad range of pivotal protein substrates involved in cellular metabolism and metabolic energy homeostasis, aberrant activity of Sirt5 is considered to be a very critical factor for many human diseases, for example, cancer, Alzheimer's disease, and Parkinson's disease
malfunction
depletion of SIRT5, a lysine desuccinylase, leads to increased ubiquitination of glutaminase. SIRT5 knockdown acts as a marker for subsequent ubiquitination at residue K158
malfunction
in addition to mitochondrial proteins, a large number of cytosolic and nuclear proteins exhibit increased succinylation, malonylation, and glutarylation upon SIRT5 deletion. Despite the broad expression and unique activity profile of SIRT5, which is non-redundant with other mitochondrial sirtuins, Sirt5 knockout (KO) mice display no strong phenotypes or major metabolic abnormalities, and germline ablation of Sirt5 is well tolerated in mice under basal, unstressed conditions. Sirt5 KO mice on the C57BL/6 background are born at a sub-Mendelian ratio, an effect not observed in Sirt5 KO 129/J background animals. Sirt5 ablation in mice causes a dramatic increase of Ksucc, Kmal, and Kglu levels, globally across multiple tissues and embryonic fibroblasts, while it has very little impact on Kac levels
malfunction
SIRT5 deficiency decreases TLR-triggered inflammation in both acute and immunosuppressive phases of sepsis. Acetylation of p65 K310 is impaired in SIRT5-/- peritoneal macrophages upon TLR4 activation. The p65 overexpression-induced NF-kappaB reporter activity is significantly increased by SIRT5 overexpression, but impaired by SIRT1/2 overexpression in HEK-293T cells. Decreased expression of SIRT5 is found in cultured macrophages upon primary or second LPS stimulation
malfunction
SIRT5 knockout mice on the Sv129 background exhibit less browning capacity in subcutaneous white adipose tissue compared to controls and show apparent cold intolerance, suggesting that SIRT5 can modulate the browning process in vivo. Knockdown of SIRT5 impairs brown adipocyte differentiation of C3H10T1/2 multipotent mesenchymal cells and blocks adipogenic gene activation. Lipid accumulation and basal and uncoupled oxygen consumption rates are significantly reduced in SIRT5 knockdown cells. The expression levels of PPARgamma, PRDM16, and UCP1 are significantly augmented in the SIRT5 overexpression cells, which is consistent with the increased lipid accumulation. UCP1 expression is significantly increased in SIRT5 overexpression groups. Knockdown of SIRT5 reduces 2-oxoglutarate concentration and supplementation of 2-oxoglutarate partially rescues brown adipocyte differentiation in SIRT5 knockdown cells. Knockdown of SIRT5 results in increased H3K9me2 and H3K9me3 levels in the promoter regions of Ppargamma and Prdm16
malfunction
SIRT5 polymorphisms may impact human lifespan. Presence of a single-nucleotide polymorphism (SNP) (rs9382222) in a conserved region of the SIRT5 promoter correlates with reduced SIRT5 mRNA expression levels in the anterior cingulate cortex (ACC) region of the brain in individuals with the CC genotype relative to individuals with the CT genotype. SNP rs2841505 is associated with slightly reduced lifespan in cohort members with a GG genotype compared to those with other genotypes. Another SIRT5 SNP, rs4712047, displays gender-specific impact on the lifespan, females with a GG genotype exhibited an increased lifespan compared to those with a GA or a AA genotype, whereas males with a GG genotype display decreased lifespan compared to males with the other genotypes. Association of SIRT5 SNP rs2253217 with human lifespan, cohort members with TT genotype live longer than those with TC or CC genotype. In addition to mitochondrial proteins, a large number of cytosolic and nuclear proteins exhibit increased succinylation, malonylation, and glutarylation upon SIRT5 deletion
malfunction
SIRT5-/- mice have mild lactic acidosis. SIRT5 deficiency does not affect the abundance of the respiratory chain complexes in liver mitochondria. Complex II and ATP synthase activities are reduced in SIRT5-/- liver
malfunction
Sirt5-deficiency-mediated IL-1beta upregulation in LPS-stimulated macrophages, which can be attenuated by activation of PKM2 using TEPP-46. Sirt5-deficient mice are more susceptible to dextran sodium sulfate (DSS)-induced colitis, which is associated with Sirt5 deficiency prompted PKM2 hypersuccinylation and boosted IL-1beta production. Both activation of PKM2 and neutralization of IL-1beta in vivo confer protection against dextran sodium sulfate (DSS)-induced colitis in Sirt5-deficiency mice
malfunction
SIRT5-deficient HEK-293 cells show defects in both Complex I- and Complex II-driven respiration. Humans with Complex II deficiency have mild lactic acidosis
malfunction
SIRT5-KO mice have reduced survival upon transverse aortic constriction (TAC) compared with wild-type mice but exhibit no mortality when undergoing a sham control operation. The increased mortality with TAC is associated with increased pathological hypertrophy and with key abnormalities in both cardiac performance and ventricular compliance. An accelerated development of cardiac dysfunction in SIRT5KO mice in response to TAC, explaining increased mortality upon cardiac stress. Protein succinylation is increased in SIRT5-KO hearts and abundant on enzymes in oxidative metabolism. SIRT5-KO mouse phenotype, detailed overview
malfunction
the SIRT5 deficiency mouse model shows that it is dispensable for metabolic homeostasis under normal conditions. The ob/ob-SIRT5 OE mice show decreased malonylation and succinylation, improved cellular glycolysis, suppressed gluconeogenesis, enhanced fatty acid oxidation, and attenuated hepatic steatosis. Hepatic overexpression of SIRT5 ameliorates the metabolic abnormalities of ob/obmice, probably through demalonylating and desuccinylating proteins in the main metabolic pathways. SIRT5 and related acylation might be potential targets for metabolic disorders
malfunction
-
the SIRT5 deficiency mouse model shows that it is dispensable for metabolic homeostasis under normal conditions. The ob/ob-SIRT5 OE mice show decreased malonylation and succinylation, improved cellular glycolysis, suppressed gluconeogenesis, enhanced fatty acid oxidation, and attenuated hepatic steatosis. Hepatic overexpression of SIRT5 ameliorates the metabolic abnormalities of ob/obmice, probably through demalonylating and desuccinylating proteins in the main metabolic pathways. SIRT5 and related acylation might be potential targets for metabolic disorders
-
metabolism
because ammonia generated during fasting is toxic, SIRT5 might play a protective role by converting ammonia to non-toxic urea through deacetylation and activation of carbamoyl phosphate synthase 1
metabolism
human SIRT5 potentially controls various primate-specific functions via two isoforms with different intracellular localizations or stabilities
metabolism
-
overexpression of CobB reduces the 6fold glucose-dependent induction to a more modest 3fold induction
metabolism
reversible Nepsilon-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells
metabolism
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle. Deacetylation of CPS1 by SIRT5 results in activation of CPS1 enzymatic activity
metabolism
SIRT5 has an emerging role in the metabolic adaptation to fasting, high protein diet and calorie restriction
metabolism
SIRT5 is a protein responsible for growth and drug resistance in human non-small cell lung cancer cells
metabolism
SIRT5 is involved in the regulation of oxidative stress induced apoptosis in cardiomyocytes
metabolism
SIRT5 plays a pivotal role in ammonia detoxification and disposal by activating carbamoyl phosphate synthetase 1 an enzyme, catalyzing the initial step of the urea cycle for ammonia detoxification and disposal
metabolism
-
sirtuin deacetylase CobB deficiency leads to both site-specific and global changes in protein acetylation stoichiometry, affecting central metabolism
metabolism
the enzyme is involved in regulation of mitochondrial energy metabolism
metabolism
-
the Gcn5-like acetyltransferase YfiQ and the sirtuin deacetylase CobB play crucial roles in the transcription regulation of the periplasmic stress-responsive promoter cpxP when cells of Escherichia coli grow in the presence of glucose, an environment that induces protein acetylation
metabolism
function of sirtuin family members in the inflammatory responses, overview. SIRT5 and SIRT1/2 have opposite expression patterns and functions in macrophages. Cytoplasmic SIRT5 counteracts the inhibitory effects of SIRT2 and enhances the innate inflammatory responses in macrophages and even in endotoxin-tolerant macrophages by promoting acetylation of p65 and activation of NF-kappaB pathway. Mechanistically, SIRT5 competes with SIRT2 to interact with NF-kappaB p65, in a deacetylase activity-independent way, to block the deacetylation of p65 by SIRT2, which consequently leads to increased acetylation of p65 and the activation of NF-kB pathway and its downstream cytokines
metabolism
protein malonylation and succinylation lysine sites are identified by immunoprecipitation coupled lipid chromatography-tandem mass spectrometry (LC-MS/MS) methods. A total of 955 malonylation sites on 434 proteins and 1377 succinylation sites on 429 proteins were identified and quantitated. Malonylation is the major SIRT5 target in the glycolysis/gluconeogenesis pathway, whereas succinylation is the preferred SIRT5 target in the oxidative phosphorylation pathway. Identification, quantification, and analysis of malonylome and succinylome
metabolism
SIRT5 regulates brown adipogenic gene activation at least partly through an indirect effect on histone modifications, linkage between epigenetics and cell differentiation. SIRT5 is implicated in the urea cycle by activating carbamoyl phosphate synthetase 1. SIRT5 modifies lysine succinylation, malonylation, and glutarylation both inside and outside of the mitochondria and impacts multiple enzymes involved in diverse mitochondrial metabolic pathways. SIRT5 has crucial effects on cellular metabolite flux
metabolism
-
protein malonylation and succinylation lysine sites are identified by immunoprecipitation coupled lipid chromatography-tandem mass spectrometry (LC-MS/MS) methods. A total of 955 malonylation sites on 434 proteins and 1377 succinylation sites on 429 proteins were identified and quantitated. Malonylation is the major SIRT5 target in the glycolysis/gluconeogenesis pathway, whereas succinylation is the preferred SIRT5 target in the oxidative phosphorylation pathway. Identification, quantification, and analysis of malonylome and succinylome
-
physiological function
-
acetylation of the response regulator RcsB controls transcription from the small RNA promoter rprA
physiological function
-
deacetylation by CobB activates the acetyl-coenzyme A synthetase
physiological function
protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5
physiological function
SIRT5 is a central regulator of Lys succinylation in mammalian cells
physiological function
SIRT5 is involved in influencing oocyte quality and in-vitro-fertilisation outcomes
physiological function
SIRT5 overexpression increases ATP synthesis and oxygen consumption in HepG2 cells, but does not affect mitochondrial biogenesis
physiological function
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
physiological function
the enzyme regulates protein function in diverse and often essential cellular processes, most notably translation. CobB is the predominate deacetylase in Escherichia coli loop or a helix that protrudes into the solution and thus in position to be an easily accessible target
physiological function
-
the enzyme prevents cigarette smoke extract-induced apoptosis in lung epithelial cells via deacetylation of FOXO3
physiological function
adipose tissue plays a vital role in metabolic regulation. SIRT5 regulates brown adipocyte differentiation and browning of subcutaneous white adipose tissue. SIRT5 modifies lysine succinylation, malonylation, and glutarylation both inside and outside of the mitochondria. SIRT5 can desuccinylate and deglutarylate IDH2 and G6PD, respectively, thereby activating both enzymes to maintain cellular NADPH homeostasis and redox potential during oxidative stress. SIRT5 is essential for brown adipocyte differentiation in vitro and has an impact on browning of subcutaneous adipose tissue in vivo. SIRT5 may play an important role in adaptive thermogenesis of brown/beige adipocytes
physiological function
human sirtuin 5 (Sirt5) catalyzes the sequence-selective desuccinylation of numerous histone succinyl sites. Compared with Sirt1, 2, 3, and 6, enzyme Sirt5 exhibits relatively weak deacetylation activity but can more efficiently remove negatively charged modifications, such as malonylation, glutarylation, and especially succinylation, from lysine residues. Sirt5 is considered a desuccinylase
physiological function
in mitochondria, the sirtuin SIRT5 is an NAD+-dependent protein deacylase controls several metabolic pathways. A wide range of SIRT5 targets have been identified. SIRT5 functions in organismal metabolic homeostasis. SIRT5 plays a role in cardiac stress responses
physiological function
potential role of isozyme SIRT5iso2 in neuron system
physiological function
role of SIRT5 as a significant regulator of cellular homeostasis in a context- and cell-type specific manner. SIRT5 regulates protein substrates involved in glycolysis, TCA cycle, fatty acid oxidation, electron transport chain, ketone body formation, nitrogenous waste management, and ROS detoxification, among other processes. SIRT5 plays pivotal roles in cardiac physiology and stress responses, and is involved in the regulation of numerous aspects of myocardial energy metabolism. SIRT5 is implicated in neoplasia, as both a tumor promoter and suppressor in a context-specific manner, and may serve a protective function in the setting of neurodegenerative disorders. SIRT5 displays a unique affinity for negatively charged acyl lysine modifications, and performs protein desuccinylation, demalonylation, and deglutarylation reactions. SIRT5 is selective only for 3-5 carbon chains acidic acyl modifications, and displays no detectable activity against either an acetyl modification, a neutral 2 carbon group, or an adipoyl, a 6-carbon acidic modification. SIRT5 regulates glycolysis, the TCA cycle and the electron transport chain. It plays a role in fatty acid beta-oxidation and promotes reactive oxygen species (ROS) detoxification. SIRT5 contributes to nitrogenous waste management and maintains cardiac homeostasis under stress. SIRT5 plays Janus-faced roles in cancer, it acts as a tumor promoter and s tumor suppressor. Role of SIRT5 in the pathogenesis of neurodegenerative disorders. Physiological function of SIRT5 , detailed overview
physiological function
role of SIRT5 as a significant regulator of cellular homeostasis in a context- and cell-type specific manner. SIRT5 regulates protein substrates involved in glycolysis, TCA cycle, fatty acid oxidation, electron transport chain, ketone body formation, nitrogenous waste management, and ROS detoxification, among other processes. SIRT5 plays pivotal roles in cardiac physiology and stress responses, and is involved in the regulation of numerous aspects of myocardial energy metabolism. SIRT5 is implicated in neoplasia, as both a tumor promoter and suppressor in a context-specific manner, and may serve a protective function in the setting of neurodegenerative disorders. SIRT5 displays a unique affinity for negatively charged acyl lysine modifications, and performs protein desuccinylation, demalonylation, and deglutarylation reactions. SIRT5 is selective only for 3-5 carbon chains acidic acyl modifications, and displays no detectable activity against either an acetyl modification, a neutral 2 carbon group, or an adipoyl, a 6-carbon acidic modification. SIRT5 regulates glycolysis, the TCA cycle and the electron transport chain. It plays a role in fatty acid beta-oxidation and promotes reactive oxygen species (ROS) detoxification. SIRT5 contributes to nitrogenous waste management and maintains cardiac homeostasis under stress. SIRT5 plays Janus-faced roles in cancer, it acts as a tumor promoter and s tumor suppressor. Role of SIRT5 in the pathogenesis of neurodegenerative disorders. Physiological function of SIRT5, detailed overview
physiological function
SIRT5 enhances acetylation (K310) of NF-kappaB p65 in response to innate stimuli. SIRT5 enhances acetylation of p65 by blocking p65 interaction of SIRT2. Endogenous SIRT5 interacts with p65 in the cytoplasm of macrophages. SIRT5 rescues hypo-inflammatory response in endotoxin-tolerant macrophages
physiological function
Sirt5 has only weak deacetylation, but has robust desuccinylation, demalonylation, and deglutarylation activities in vitro and in vivo. Modifications by Sirt5 cover a broad range of pivotal protein substrates involved in cellular metabolism and metabolic energy homeostasis
physiological function
SIRT5 is a lysine desuccinylase known to regulate mitochondrial fatty acid oxidation and the urea cycle. SIRT5 binds to cardiolipin and regulates the electron transport chain. SIRT5 is targeted to protein complexes on the inner mitochondrial membrane via affinity for cardiolipin to promote respiratory chain function. SIRT5 restores membrane binding of very-long-chain acyl-CoA dehydrogenase (VLCAD). SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 counteracts succinylation of mitochondrial membrane proteins, overview
physiological function
SIRT5 is a lysine desuccinylase known to regulate mitochondrial fatty acid oxidation and the urea cycle. SIRT5 binds to cardiolipin and regulates the electron transport chain. SIRT5 is targeted to protein complexes on the inner mitochondrial membrane via affinity for cardiolipin to promote respiratory chain function. Three-dimensional modeling of Complex II suggests that several SIRT5-targeted lysine residues lie at the protein-lipid interface of succinate dehydrogenase subunit B. Succinylation at these sites may disrupt Complex II subunit-subunit interactions and electron transfer. SIRT5 restores membrane binding of very-long-chain acyl-CoA dehydrogenase (VLCAD). SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 counteracts succinylation of mitochondrial membrane proteins, overview
physiological function
SIRT5 plays an important role in inhibiting inflammation. SIRT5 suppresses the pro-inflammatory response in macrophages at least in part by regulating PKM2 succinylation, activity, and function. SIRT5 desuccinylates and activates pyruvate kinase M2 (PKM2) to block macrophage IL-1beta production and to prevent DSS-induced colitis in mice. Lys311 is a key succinylated site in the regulation of PKM2 activity. SIRT5-regulated hypersuccinylation inhibits the pyruvate kinase activity of PKM2 by promoting its tetramer-to-dimer transition. A succinylation-mimetic PKM2 K311E mutation promotes nuclear accumulation and increases protein kinase activity. SIRT5-dependent succinylation promotes PKM2 entry into nucleus, where a complex of PKM2-HIF1alpha is formed at the promoter of interleukin-1beta gene in LPS-stimulated macrophages. SIRT5-dependent succinylation promotes PKM2 dimerization and increases its protein kinase activity
physiological function
SIRT5, a mitochondrial NAD+-dependent lysine deacylase, plays a key role in stabilizing glutaminase. In transformed cells, SIRT5 regulates glutamine metabolism by desuccinylating glutaminase and thereby protecting it from ubiquitin-mediated degradation. SIRT5 is upregulated during cellular transformation and supports proliferation and tumorigenesis. SIRT5 is upregulated during oncogenic transformation and stabilizes glutaminase, an enzyme with important functions in cancer-cell metabolic reprogramming. Elevated SIRT5 expression in human breast tumors correlates with poor patient prognosis. Role for SIRT5 in metabolic reprogramming and mammary tumorigenesis. SIRT5 supports proliferation and anchorage-independent growth
physiological function
Sirtuin 5 (SIRT5) is a NAD+-dependent lysine deacylase. SIRT5 deacylates metabolism-related proteins and attenuates hepatic steatosis in obese ob/ob mice
physiological function
sirtuin 5 (SIRT5) is upregulated in patients with type 2 diabetes. Elevated SIRT5 expression is positively associated with age and blood glucose levels, and negatively associated with pancreatic and duodenal homeobox 1 (PDX1) expression. SIRT5 regulates pancreatic beta cell proliferation and insulin secretion in type 2 diabetes. SIRT5 suppresses the proliferation of pancreatic beta cells in vitro. While SIRT5 possesses weak deacetylase activity, it catalyzes the modification of acidic lysine residues by glutaryxadlation, succinylation, and malonylation well. PDX1 is transcriptionally regulated by SIRT5 via H4K16 deacetylation. PDX1 is involved in SIRT5-mediated insulin secretion and pancreatic beta cell proliferation
physiological function
sirtuins are NAD+-dependent enzymes that regulate diverse cellular processes, thereby maintaining metabolic homeostasis and genomic integrity.Sirtuin-family deacylases promote health and longevity in mammals. The sirtuin SIRT5 localizes predominantly to the mitochondrial matrix. SIRT5 preferentially removes negatively charged modifications from its target lysines: succinylation, malonylation, and glutarylation. It regulates protein substrates involved in glucose oxidation, ketone body formation, ammonia detoxification, fatty acid oxidation, and ROS management
physiological function
sirtuins are protein deacylases that regulate metabolism and stress responses and are implicated in aging-related diseases
physiological function
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
physiological function
-
Sirtuin 5 (SIRT5) is a NAD+-dependent lysine deacylase. SIRT5 deacylates metabolism-related proteins and attenuates hepatic steatosis in obese ob/ob mice
-
additional information
lysine succinylation (Ksucc), malonylation (Kmal), and glutarylation (Kglu), derived from succinyl-CoA, malonyl-CoA, and glutaryl-CoA respectively, have emerged as functionally important modifications, but most likely have distinct functions from Kac in regulating metabolism and other cellular processes. The presence of succinyl, malonyl, or glutaryl moiety confers upon a modified lysine residue a negative charge at physiological pH. SIRT5 preferentially catalyzes the removal of these negatively charged acidic modifications, thereby functioning as the dominant cellular desuccinylase, demalonylase, and deglutarylase. Compared to other sirtuins, SIRT5 possess a larger acyl binding pocket, able to accommodate these acyl modifications, which are bulkier than an acetyl group. The presence of alanine (Ala86), arginine (Arg105), and tyrosine (Tyr102) residues in the catalytic pocket of SIRT5 appears to be responsible for its specificity for negatively charged acyl groups
additional information
lysine succinylation (Ksucc), malonylation (Kmal), and glutarylation (Kglu), derived from succinyl-CoA, malonyl-CoA, and glutaryl-CoA respectively, have emerged as functionally important modifications, but most likely have distinct functions from Kac in regulating metabolism and other cellular processes. The presence of succinyl, malonyl, or glutaryl moiety confers upon a modified lysine residue a negative charge at physiological pH. SIRT5 preferentially catalyzes the removal of these negatively charged acidic modifications, thereby functioning as the dominant cellular desuccinylase, demalonylase, and deglutarylase. Compared to other sirtuins, SIRT5 possess a larger acyl binding pocket, able to accommodate these acyl modifications, which are bulkier than an acetyl group. The presence of alanine (Ala86), arginine (Arg105), and tyrosine (Tyr102) residues in the catalytic pocket of SIRT5 appears to be responsible for its specificity for negatively charged acyl groups
additional information
molecular mechanism underlying the sequence-selective desuccinylase activity of Sirt5, overview. Human Sirt5 is a ubiquitous desuccinylase that catalyzes the desuccinylation of diverse histone succinyl sites with sequence selectivity. Among the 13 identified sites, H2BK116su is the most favorable Sirt5 substrate, with H4K12su showing the lowest catalytic efficiency and no activity observed in the presence of H4K31su
additional information
-
molecular mechanism underlying the sequence-selective desuccinylase activity of Sirt5, overview. Human Sirt5 is a ubiquitous desuccinylase that catalyzes the desuccinylation of diverse histone succinyl sites with sequence selectivity. Among the 13 identified sites, H2BK116su is the most favorable Sirt5 substrate, with H4K12su showing the lowest catalytic efficiency and no activity observed in the presence of H4K31su
additional information
the mitochondrial processing peptidase cleavage site of SIRT5 leaves an amphipathic helix on the mature protein at the extreme N terminus. This N-terminal amphipathic helix has three positively charged residues that orient into the solvent as seen in the SIRT5 crystal structure These positively charged residues might confer cardiolipin binding to SIRT5, similar to the amphipathic helix previously identified in very-long-chain acyl-CoA dehydrogenase (VLCAD)
additional information
-
the mitochondrial processing peptidase cleavage site of SIRT5 leaves an amphipathic helix on the mature protein at the extreme N terminus. This N-terminal amphipathic helix has three positively charged residues that orient into the solvent as seen in the SIRT5 crystal structure These positively charged residues might confer cardiolipin binding to SIRT5, similar to the amphipathic helix previously identified in very-long-chain acyl-CoA dehydrogenase (VLCAD)
additional information
the mitochondrial processing peptidase cleavage site of SIRT5 leaves an amphipathic helix on the mature protein at the extreme N-terminus. This N-terminal amphipathic helix has three positively charged residues that orient into the solvent as seen in the SIRT5 crystal structure These positively charged residues might confer cardiolipin binding to SIRT5, similar to the amphipathic helix previously identified in very-long-chain acyl-CoA dehydrogenase (VLCAD)
additional information
-
the mitochondrial processing peptidase cleavage site of SIRT5 leaves an amphipathic helix on the mature protein at the extreme N-terminus. This N-terminal amphipathic helix has three positively charged residues that orient into the solvent as seen in the SIRT5 crystal structure These positively charged residues might confer cardiolipin binding to SIRT5, similar to the amphipathic helix previously identified in very-long-chain acyl-CoA dehydrogenase (VLCAD)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Starai, V.J.; Celic, I.; Cole, R.N.; Boeke, J.D.; Escalante-Semerena, J.C.
Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
Science
298
2390-2392
2002
Salmonella enterica
brenda
Ogura, M.; Nakamura, Y.; Tanaka, D.; Zhuang, X.; Fujita, Y.; Obara, A.; Hamasaki, A.; Hosokawa, M.; Inagaki, N.
Overexpression of SIRT5 confirms its involvement in deacetylation and activation of carbamoyl phosphate synthetase 1
Biochem. Biophys. Res. Commun.
393
73-78
2010
Mus musculus (Q8K2C6)
brenda
Nakagawa, T.; Lomb, D.J.; Haigis, M.C.; Guarente, L.
SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
Cell
137
560-570
2009
Mus musculus (Q8K2C6)
brenda
Maurer, B.; Rumpf, T.; Scharfe, M.; Stolfa, D.A.; Schmitt, M.L.; He, W.; Verdin, E.; Sippl, W.; Jung, M.
Inhibitors of the NAD(+)-dependent protein desuccinylase and demalonylase Sirt5
ACS Med. Chem. Lett.
3
1050-1053
2012
Homo sapiens (Q9NXA8)
brenda
Nakagawa, T.; Guarente, L.
Urea cycle regulation by mitochondrial sirtuin, SIRT5
Aging
1
578-581
2009
Mus musculus (Q8K2C6)
brenda
Roessler, C.; Nowak, T.; Pannek, M.; Gertz, M.; Nguyen, G.T.; Scharfe, M.; Born, I.; Sippl, W.; Steegborn, C.; Schutkowski, M.
Chemical probing of the human sirtuin 5 active site reveals its substrate acyl specificity and peptide-based inhibitors
Angew. Chem. Int. Ed. Engl.
53
10728-10732
2014
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Lin, Z.F.; Xu, H.B.; Wang, J.Y.; Lin, Q.; Ruan, Z.; Liu, F.B.; Jin, W.; Huang, H.H.; Chen, X.
SIRT5 desuccinylates and activates SOD1 to eliminate ROS
Biochem. Biophys. Res. Commun.
441
191-195
2013
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Suenkel, B.; Fischer, F.; Steegborn, C.
Inhibition of the human deacylase Sirtuin 5 by the indole GW5074
Bioorg. Med. Chem. Lett.
23
143-146
2012
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Tan, M.; Peng, C.; Anderson, K.A.; Chhoy, P.; Xie, Z.; Dai, L.; Park, J.; Chen, Y.; Huang, H.; Zhang, Y.; Ro, J.; Wagner, G.R.; Green, M.F.; Madsen, A.S.; Schmiesing, J.; Peterson, B.S.; Xu, G.; Ilkayeva, O.R.; Muehlbauer, M.J.; Braulke, T.; Mhlhausen, C.; Backos, D.S.; Olsen, C.A.; McGuire, P.J.; Pletcher, S.D.; Lombard, D.B.; Hirschey, M.D.; Zhao, Y.
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
Cell Metab.
19
605-617
2014
Homo sapiens (Q9NXA8)
brenda
Liu, B.; Che, W.; Zheng, C.; Liu, W.; Wen, J.; Fu, H.; Tang, K.; Zhang, J.; Xu, Y.
SIRT5: a safeguard against oxidative stress-induced apoptosis in cardiomyocytes
Cell. Physiol. Biochem.
32
1050-1059
2013
Rattus norvegicus (Q68FX9)
brenda
Buler, M.; Aatsinki, S.M.; Izzi, V.; Uusimaa, J.; Hakkola, J.
SIRT5 is under the control of PGC-1alpha and AMPK and is involved in regulation of mitochondrial energy metabolism
FASEB J.
28
3225-3237
2014
Mus musculus (Q8K2C6), Mus musculus
brenda
Zhang, Q.F.; Gu, J.; Gong, P.; Wang, X.D.; Tu, S.; Bi, L.J.; Yu, Z.N.; Zhang, Z.P.; Cui, Z.Q.; Wei, H.P.; Tao, S.C.; Zhang, X.E.; Deng, J.Y.
Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase
FEBS J.
280
1966-1979
2013
Escherichia coli, Escherichia coli AD494
brenda
Nakamura, Y.; Ogura, M.; Ogura, K.; Tanaka, D.; Inagaki, N.
SIRT5 deacetylates and activates urate oxidase in liver mitochondria of mice
FEBS Lett.
586
4076-4081
2012
Mus musculus (Q8K2C6), Mus musculus
brenda
Matsushita, N.; Yonashiro, R.; Ogata, Y.; Sugiura, A.; Nagashima, S.; Fukuda, T.; Inatome, R.; Yanagi, S.
Distinct regulation of mitochondrial localization and stability of two human Sirt5 isoforms
Genes Cells
16
190-202
2011
Homo sapiens (Q9NXA8), Homo sapiens
brenda
He, B.; Du, J.; Lin, H.
Thiosuccinyl peptides as Sirt5-specific inhibitors
J. Am. Chem. Soc.
134
1922-1925
2012
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Hu, L.I.; Chi, B.K.; Kuhn, M.L.; Filippova, E.V.; Walker-Peddakotla, A.J.; Bsell, K.; Becher, D.; Anderson, W.F.; Antelmann, H.; Wolfe, A.J.
Acetylation of the response regulator RcsB controls transcription from a small RNA promoter
J. Bacteriol.
195
4174-4186
2013
Escherichia coli
brenda
Chang, J.H.; Kim, H.C.; Hwang, K.Y.; Lee, J.W.; Jackson, S.P.; Bell, S.D.; Cho, Y.
Structural basis for the NAD-dependent deacetylase mechanism of Sir2
J. Biol. Chem.
277
34489-34498
2002
Archaeoglobus fulgidus (O28597)
brenda
Garrity, J.; Gardner, J.G.; Hawse, W.; Wolberger, C.; Escalante-Semerena, J.C.
N-Lysine propionylation controls the activity of propionyl-CoA synthetase
J. Biol. Chem.
282
30239-30245
2007
Salmonella enterica
brenda
Zhou, Y.; Zhang, H.; He, B.; Du, J.; Lin, H.; Cerione, R.A.; Hao, Q.
The bicyclic intermediate structure provides insights into the desuccinylation mechanism of human sirtuin 5 (SIRT5)
J. Biol. Chem.
287
28307-28314
2012
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Feldman, J.L.; Baeza, J.; Denu, J.M.
Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins
J. Biol. Chem.
288
31350-31356
2013
Homo sapiens (Q9NXA8)
brenda
Baeza, J.; Dowell, J.A.; Smallegan, M.J.; Fan, J.; Amador-Noguez, D.; Khan, Z.; Denu, J.M.
Stoichiometry of site-specific lysine acetylation in an entire proteome
J. Biol. Chem.
289
21326-21338
2014
Escherichia coli
brenda
Geng, Y.Q.; Li, T.T.; Liu, X.Y.; Li, Z.H.; Fu, Y.C.
SIRT1 and SIRT5 activity expression and behavioral responses to calorie restriction
J. Cell. Biochem.
112
3755-3761
2011
Rattus norvegicus (Q68FX9)
brenda
Madsen, A.S.; Olsen, C.A.
Substrates for efficient fluorometric screening employing the NAD-dependent sirtuin 5 lysine deacylase (KDAC) enzyme
J. Med. Chem.
55
5582-5590
2012
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Zhao, K.; Chai, X.; Marmorstein, R.
Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli
J. Mol. Biol.
337
731-741
2004
Escherichia coli (P75960), Escherichia coli
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
J. Mol. Biol.
382
790-801
2008
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Szczepankiewicz, B.G.; Dai, H.; Koppetsch, K.J.; Qian, D.; Jiang, F.; Mao, C.; Perni, R.B.
Synthesis of carba-NAD and the structures of its ternary complexes with SIRT3 and SIRT5
J. Org. Chem.
77
7319-7329
2012
Homo sapiens (Q9NXA8), Homo sapiens
brenda
AbouElfetouh, A.; Kuhn, M.L.; Hu, L.I.; Scholle, M.D.; Sorensen, D.J.; Sahu, A.K.; Becher, D.; Antelmann, H.; Mrksich, M.; Anderson, W.F.; Gibson, B.W.; Schilling, B.; Wolfe, A.J.
The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites
Microbiologyopen
4
66-83
2015
Escherichia coli (P75960)
brenda
Peng, C.; Lu, Z.; Xie, Z.; Cheng, Z.; Chen, Y.; Tan, M.; Luo, H.; Zhang, Y.; He, W.; Yang, K.; Zwaans, B.M.; Tishkoff, D.; Ho, L.; Lombard, D.; He, T.C.; Dai, J.; Verdin, E.; Ye, Y.; Zhao, Y.
The first identification of lysine malonylation substrates and its regulatory enzyme
Mol. Cell. Proteomics
10
M111.012658
2011
Mus musculus (Q8K2C6)
brenda
Colak, G.; Xie, Z.; Zhu, A.Y.; Dai, L.; Lu, Z.; Zhang, Y.; Wan, X.; Chen, Y.; Cha, Y.H.; Lin, H.; Zhao, Y.; Tan, M.
Identification of lysine succinylation substrates and the succinylation regulatory enzyme CobB in Escherichia coli
Mol. Cell. Proteomics
12
3509-3520
2013
Escherichia coli
brenda
Park, J.; Chen, Y.; Tishkoff, D.X.; Peng, C.; Tan, M.; Dai, L.; Xie, Z.; Zhang, Y.; Zwaans, B.M.; Skinner, M.E.; Lombard, D.B.; Zhao, Y.
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
Mol. Cell.
50
919-930
2013
Mus musculus (Q8K2C6)
brenda
Li, R.; Gu, J.; Chen, Y.Y.; Xiao, C.L.; Wang, L.W.; Zhang, Z.P.; Bi, L.J.; Wei, H.P.; Wang, X.D.; Deng, J.Y.; Zhang, X.E.
CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY
Mol. Microbiol.
76
1162-1174
2010
Escherichia coli, Escherichia coli W3110 / ATCC 27325
brenda
Lima, B.P.; Antelmann, H.; Gronau, K.; Chi, B.K.; Becher, D.; Brinsmade, S.R.; Wolfe, A.J.
Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter
Mol. Microbiol.
81
1190-1204
2011
Escherichia coli
brenda
Lutz, M.I.; Milenkovic, I.; Regelsberger, G.; Kovacs, G.G.
Distinct patterns of sirtuin expression during progression of Alzheimer's disease
Neuromolecular Med.
16
405-414
2014
Homo sapiens (Q9NXA8)
brenda
Thao, S.; Chen, C.S.; Zhu, H.; Escalante-Semerena, J.C.
Nepsilon-lysine acetylation of a bacterial transcription factor inhibits its DNA-binding activity
PLoS One
5
e15123
2010
Escherichia coli (P75960)
brenda
Fischer, F.; Gertz, M.; Suenkel, B.; Lakshminarasimhan, M.; Schutkowski, M.; Steegborn, C.
Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition
PLoS One
7
e45098
2012
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Gertz, M.; Nguyen, G.T.; Fischer, F.; Suenkel, B.; Schlicker, C.; Frnzel, B.; Tomaschewski, J.; Aladini, F.; Becker, C.; Wolters, D.; Steegborn, C.
A molecular mechanism for direct sirtuin activation by resveratrol
PLoS One
7
e49761
2012
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Ringel, A.E.; Roman, C.; Wolberger, C.
Alternate deacylating specificities of the archaeal sirtuins Sir2Af1 and Sir2Af2
Protein Sci.
23
1686-1697
2014
Escherichia coli, Archaeoglobus fulgidus (O28597), Archaeoglobus fulgidus
brenda
Pacella-Ince, L.; Zander-Fox, D.L.; Lane, M.
Mitochondrial SIRT5 is present in follicular cells and is altered by reduced ovarian reserve and advanced maternal age
Reprod. Fertil. Dev.
26
1072-1083
2014
Homo sapiens (Q9NXA8)
brenda
Du, J.; Zhou, Y.; Su, X.; Yu, J.J.; Khan, S.; Jiang, H.; Kim, J.; Woo, J.; Kim, J.H.; Choi, B.H.; He, B.; Chen, W.; Zhang, S.; Cerione, R.A.; Auwerx, J.; Hao, Q.; Lin, H.
Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase
Science
334
806-809
2011
Homo sapiens (Q9NXA8), Mus musculus (Q8K2C6)
brenda
Schuetz, A.; Min, J.; Antoshenko, T.; Wang, C.L.; Allali-Hassani, A.; Dong, A.; Loppnau, P.; Vedadi, M.; Bochkarev, A.; Sternglanz, R.; Plotnikov, A.N.
Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin
Structure
15
377-389
2007
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Lu, W.; Zuo, Y.; Feng, Y.; Zhang, M.
SIRT5 facilitates cancer cell growth and drug resistance in non-small cell lung cancer
Tumour Biol.
35
10699-10705
2014
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Wang, Y.; Zhu, Y.; Xing, S.; Ma, P.; Lin, D.
SIRT5 prevents cigarette smoke extract-induced apoptosis in lung epithelial cells via deacetylation of FOXO3
Cell Stress Chaperones
20
805-810
2015
Homo sapiens
brenda
Zhou, L.; Wang, F.; Sun, R.; Chen, X.; Zhang, M.; Xu, Q.; Wang, Y.; Wang, S.; Xiong, Y.; Guan, K.L.; Yang, P.; Yu, H.; Ye, D.
SIRT5 promotes IDH2 desuccinylation and G6PD deglutarylation to enhance cellular antioxidant defense
EMBO Rep.
17
811-822
2016
Mus musculus
brenda
Roessler, C.; Tueting, C.; Meleshin, M.; Steegborn, C.; Schutkowski, M.
A novel continuous assay for the deacylase sirtuin 5 and other deacetylases
J. Med. Chem.
58
7217-7223
2015
Homo sapiens (Q9NXA8)
brenda
Nishida, Y.; Rardin, M.J.; Carrico, C.; He, W.; Sahu, A.K.; Gut, P.; Najjar, R.; Fitch, M.; Hellerstein, M.; Gibson, B.W.; Verdin, E.
SIRT5 regulates both cytosolic and mitochondrial protein malonylation with glycolysis as a major target
Mol. Cell
59
321-332
2015
Mus musculus (Q8K2C6)
brenda
Yu, J.; Haldar, M.; Mallik, S.; Srivastava, D.K.
Role of the substrate specificity-defining residues of human SIRT5 in modulating the structural stability and inhibitory features of the enzyme
PLoS ONE
11
e0152467
2016
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Rajabi, N.; Auth, M.; Troelsen, K.R.; Pannek, M.; Bhatt, D.P.; Fontenas, M.; Hirschey, M.D.; Steegborn, C.; Madsen, A.S.; Olsen, C.A.
Mechanism-based inhibitors of the human sirtuin 5 deacylase structure-activity relationship, biostructural, and kinetic insight
Angew. Chem. Int. Ed. Engl.
56
14836-14841
2017
Danio rerio (Q6DHI5), Danio rerio, Homo sapiens (Q9NXA8), Homo sapiens
brenda
Du, Y.; Hu, H.; Hua, C.; Du, K.; Wei, T.
Tissue distribution, subcellular localization, and enzymatic activity analysis of human SIRT5 isoforms
Biochem. Biophys. Res. Commun.
503
763-769
2018
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Hang, T.; Chen, W.; Wu, M.; Zhan, L.; Wang, C.; Jia, N.; Zhang, X.; Zang, J.
Structural insights into the molecular mechanism underlying Sirt5-catalyzed desuccinylation of histone peptides
Biochem. J.
476
211-223
2019
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Wang, F.; Wang, K.; Xu, W.; Zhao, S.; Ye, D.; Wang, Y.; Xu, Y.; Zhou, L.; Chu, Y.; Zhang, C.; Qin, X.; Yang, P.; Yu, H.
SIRT5 desuccinylates and activates pyruvate kinase M2 to block macrophage IL-1beta production and to prevent DSS-induced colitis in mice
Cell Rep.
19
2331-2344
2017
Mus musculus (A0A1Y7VM56)
brenda
Liu, S.; Ji, S.; Yu, Z.J.; Wang, H.L.; Cheng, X.; Li, W.J.; Jing, L.; Yu, Y.; Chen, Q.; Yang, L.L.; Li, G.B.; Wu, Y.
Structure-based discovery of new selective small-molecule sirtuin 5 inhibitors
Chem. Biol. Drug Des.
91
257-268
2018
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Kumar, S.; Lombard, D.B.
Functions of the sirtuin deacylase SIRT5 in normal physiology and pathobiology
Crit. Rev. Biochem. Mol. Biol.
53
311-334
2018
Mus musculus (A0A1Y7VM56), Homo sapiens (Q9NXA8)
brenda
Shuai, L.; Zhang, L.N.; Li, B.H.; Tang, C.L.; Wu, L.Y.; Li, J.; Li, J.Y.
SIRT5 regulates brown adipocyte differentiation and browning of subcutaneous white adipose tissue
Diabetes
68
1449-1461
2019
Mus musculus (A0A1Y7VM56)
brenda
Du, Y.; Hu, H.; Qu, S.; Wang, J.; Hua, C.; Zhang, J.; Wei, P.; He, X.; Hao, J.; Liu, P.; Yang, F.; Li, T.; Wei, T.
SIRT5 deacylates metabolism-related proteins and attenuates hepatic steatosis in ob/ob mice
EBioMedicine
36
347-357
2018
Mus musculus (A0A1Y7VM56), Mus musculus, Mus musculus C57BL/6 (A0A1Y7VM56)
brenda
Ma, Y.; Fei, X.
SIRT5 regulates pancreatic beta-cell proliferation and insulin secretion in type 2 diabetes
Exp. Therap. Med.
16
1417-1425
2018
Homo sapiens (Q9NXA8), Homo sapiens
brenda
Qin, K.; Han, C.; Zhang, H.; Li, T.; Li, N.; Cao, X.
NAD+ dependent deacetylase Sirtuin 5 rescues the innate inflammatory response of endotoxin tolerant macrophages by promoting acetylation of p65
J. Autoimmun.
81
120-129
2017
Mus musculus (Q8K2C6)
brenda
Zhang, Y.; Bharathi, S.S.; Rardin, M.J.; Lu, J.; Maringer, K.V.; Sims-Lucas, S.; Prochownik, E.V.; Gibson, B.W.; Goetzman, E.S.
Lysine desuccinylase SIRT5 binds to cardiolipin and regulates the electron transport chain
J. Biol. Chem.
292
10239-10249
2017
Mus musculus (A0A1Y7VM56), Mus musculus, Homo sapiens (Q9NXA8), Homo sapiens
brenda
Hershberger, K.A.; Abraham, D.M.; Martin, A.S.; Mao, L.; Liu, J.; Gu, H.; Locasale, J.W.; Hirschey, M.D.
Sirtuin 5 is required for mouse survival in response to cardiac pressure overload
J. Biol. Chem.
292
19767-19781
2017
Mus musculus (A0A1Y7VM56), Mus musculus
brenda
Yang, L.; He, Y.; Chen, Q.; Qian, S.; Wang, Z.
Design and synthesis of new 9-substituted norharmane derivatives as potential Sirt5 inhibitors
J. Heterocycl. Chem.
54
1457-1466
2017
Homo sapiens (Q9NXA8)
-
brenda
Kalbas, D.; Liebscher, S.; Nowak, T.; Meleshin, M.; Pannek, M.; Popp, C.; Alhalabi, Z.; Bordusa, F.; Sippl, W.; Steegborn, C.; Schutkowski, M.
Potent and selective inhibitors of human sirtuin 5
J. Med. Chem.
61
2460-2471
2018
Danio rerio (Q6DHI5), Homo sapiens (Q9NXA8), Homo sapiens
brenda
Kumar, S.; Lombard, D.B.
Generation and purification of catalytically active recombinant sirtuin5 (SIRT5) protein
Methods Mol. Biol.
1436
241-257
2016
Homo sapiens (Q9NXA8)
brenda
Greene, K.S.; Lukey, M.J.; Wang, X.; Blank, B.; Druso, J.E.; Lin, M.J.; Stalnecker, C.A.; Zhang, C.; Negron Abril, Y.; Erickson, J.W.; Wilson, K.F.; Lin, H.; Weiss, R.S.; Cerione, R.A.
SIRT5 stabilizes mitochondrial glutaminase and supports breast cancer tumorigenesis
Proc. Natl. Acad. Sci. USA
116
26625-26632
2019
Homo sapiens (Q9NXA8), Homo sapiens
brenda