Information on EC 2.4.2.B14 - protein-lysine desuccinylase (NAD+)

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

EC NUMBER
COMMENTARY hide
2.4.2.B14
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
protein-lysine desuccinylase (NAD+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD+ + [protein]-N6-acetyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [protein]-N6-succinyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain W3110 is a K12 derivative that is wild-type for chemotaxis
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NAD+ + Ac-(N6-methylmalonyl)Lys-(7-amido-4-methylcoumarin)
nicotinamide + Ac-Lys-7-amido-4-methylcoumarin + 2'-O-methylmalonyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + Ac-(N6-succinyl)Lys-7-amido-4-methylcoumarin
nicotinamide + Ac-Lys-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
NAD+ + Ac-Suc-L-Lys-7-amido-4-methylcoumarin
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
NAD+ + AFNQG(N6-malonyl)KIFK
nicotinamide + AFNQGKIFK + 2'-O-malonyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + AYVDDTPAEQM(N6-malonyl)KAER
nicotinamide + AYVDDTPAEQMKAER + 2'-O-malonyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-acetyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-adipoyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-adipoyl-ADP-ribose
show the reaction diagram
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-
-
-
?
NAD+ + benzoyl-GVL(N6-glutaryl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-glutaryl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-malonyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-malonyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-oxalyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-oxalyl-ADP-ribose
show the reaction diagram
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-
-
-
?
NAD+ + benzoyl-GVL(N6-pimeloyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-pimeloyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + benzoyl-GVL(N6-suberoyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-suberoyl-ADP-ribose
show the reaction diagram
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-
-
-
?
NAD+ + benzoyl-GVL(N6-succinyl)KEYGV-amide
nicotinamide + benzoyl-GVLKEYGV-amide + 2'-O-succinyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + benzoyl-RGVL(N6-succinyl)KEYGV-amide
nicotinamide + benzoyl-RGVLKEYGV-amide + 2'-O-acetyl-ADP-ribose
show the reaction diagram
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carbamoyl phosphate synthetase 1 Lys527 peptide
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-
?
NAD+ + DSYVGDEAQSDSYVGDEAQS(N6-malonyl)KR
nicotinamide + DSYVGDEAQSDSYVGDEAQSKR + 2'-O-malonyl-ADP-ribose
show the reaction diagram
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-
-
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?
NAD+ + ETGVDLT(N6-succinyl)KDNMALQR
nicotinamide + ETGVDLTKDNMALQR + 2'-O-succinyl-ADP-ribose
show the reaction diagram
-
-
-
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?
NAD+ + FKRGVL(N6-acetyl)KEYGVKV
nicotinamide + FKRGVLKEYGVKV + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + Fluor-de-Lys
nicotinamide + ?
show the reaction diagram
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-
-
-
?
NAD+ + IEEELGS(N6-malonyl)KAK
nicotinamide + IEEELGSKAK + 2'-O-malonyl-ADP-ribose
show the reaction diagram
-
-
-
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?
NAD+ + KGLGKGGA(N6-acetyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + KGLGKGGA(N6-butyryl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-butyryl-ADP-ribose
show the reaction diagram
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
show the reaction diagram
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
show the reaction diagram
NAD+ + KQTAR(N6-malonyl)KSTGGWW
nicotinamide + KQTARKSTGGWW + 2'-O-malonyl-ADP-ribose
show the reaction diagram
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histone H3K9 malonyl peptide
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?
NAD+ + KQTAR(N6-succinyl)KSTGGKA
nicotinamide + KQTARKSTGGKA + 2'-O-succinyl-ADP-ribose
show the reaction diagram
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-
-
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?
NAD+ + KQTAR(N6-succinyl)KSTGGWW
nicotinamide + KQTARKSTGGWW + 2'-O-succinyl-ADP-ribose
show the reaction diagram
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histone H3K9 succinyl peptide
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?
NAD+ + KTRSG(N6-malonyl)KVMRRWW
nicotinamide + KTRSGKVMRRWW + 2'-O-malonyl-ADP-ribose
show the reaction diagram
-
-
-
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?
NAD+ + KTRSG(N6-succinyl)KVMRRWW
nicotinamide + KTRSGKVMRRWW + 2'-O-succinyl-ADP-ribose
show the reaction diagram
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ACS2 Lys628 peptide
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?
NAD+ + N2-benzyloxycarbonyl-N6-succinyl-L-lysine-7-amido-4-methylcoumarin
nicotinamide + N2-benzyloxycarbonyl-L-lysine-7-amido-4-methylcoumarin + 2'-O-succinyl-ADP-ribose
show the reaction diagram
i.e. 3-[(5-[[(benzyloxy)carbonyl]amino]-5-[(4-methyl-2-oxo-2H-chromen-7-yl)carbamoyl]pentyl)carbamoyl]-propanoic acid
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-
?
NAD+ + QTAR(N6-acetyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-acetyl-ADP-ribose
show the reaction diagram
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acetylated histone H3 peptide, less than 10% compared to the activity with the succinylated peptide
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-
?
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
show the reaction diagram
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decanoylated histone H3 peptide, about 35% compared to the activity with the succinylated peptide
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-
?
NAD+ + QTAR(N6-dodecanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-dodecanoyl-ADP-ribose
show the reaction diagram
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dodecanoylated histone H3 peptide, about 35% compared to the activity with the succinylated peptide
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-
?
NAD+ + QTAR(N6-hexanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-hexanoyl-ADP-ribose
show the reaction diagram
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hexanoylated histone H3 peptide, less than 10% compared to the activity with the succinylated peptide
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?
NAD+ + QTAR(N6-myristoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
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myristoylated histone H3 peptide, about 15% compared to the activity with the succinylated peptide
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-
?
NAD+ + QTAR(N6-octanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-octanoyl-ADP-ribose
show the reaction diagram
-
octanoylated histone H3 peptide, about 30% compared to the activity with the succinylated peptide
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-
?
NAD+ + QTAR(N6-propionyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-propionyl-ADP-ribose
show the reaction diagram
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propionylated histone H3 peptide, less than 10% compared to the activity with the succinylated peptide
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?
NAD+ + QTAR(N6-succinyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-succinyl-ADP-ribose
show the reaction diagram
-
succinylated histone H3 peptide
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?
NAD+ + SGASE(N6-malonyl)KDIVHSGWW
nicotinamide + SGASEKDIVHSGWW + 2'-O-malonyl-ADP-ribose
show the reaction diagram
-
-
-
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?
NAD+ + SGASE(N6-succinyl)KDIVHSGWW
nicotinamide + SGASEKDIVHSGWW + 2'-O-succinyl-ADP-ribose
show the reaction diagram
-
glutamate dehydrogenase Lys503 peptide
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-
?
NAD+ + SKEYFS(N6-succinyl)KQK
nicotinamide + SKEYFSKQK + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + SQG(N6-succinyl)KVLQATVV
nicotinamide + SQGKVLQATVV + 2'-O-succinyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + TAIG(N6-malonyl)KAGYTDK
nicotinamide + TAIGKAGYTDK + 2'-O-malonyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + TRSG(N6-acetyl)KVMR
nicotinamide + TRSGKVMR + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
peptide based on an acetyl-CoA synthetase 2 acetylation site
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-
?
NAD+ + VLLPEYGGT(N6-succinyl)KVVLDDK
nicotinamide + VLLPEYGGTKVVLDDK + 2'-O-succinyl-ADP-ribose
show the reaction diagram
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-
-
-
?
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [bovine serum albumin]-N6-acetyl-L-lysine
nicotinamide + [bovine serum albumin]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
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
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?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [carbamoyl phosphate synthase 1]-N6-succinyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-succinyl-ADP ribose
show the reaction diagram
-
deletion of Sirt5 in mice increases the level of succinylation on carbamoyl phosphate synthase 1
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-
?
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
show the reaction diagram
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-
-
-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
NAD+ + [carbamoyl phosphate synthetase 1]-N6-glutaryl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-glutaryl-ADP-ribose
show the reaction diagram
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-
-
-
?
NAD+ + [chicken histone]-N6-acetyl-L-lysine
nicotinamide + [chicken histone]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
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
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?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
show the reaction diagram
NAD+ + [cytochrome c]-N6-acetyl-L-lysine
nicotinamide + [cytochrome c]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
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-
-
-
?
NAD+ + [forkhead box O3]-N6-acetyl-L-lysine
nicotinamide + [forkhead box O3]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
the enzyme deacetylates FOXO3 at K271 and K290
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-
?
NAD+ + [glucose-6-phosphate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glucose-6-phosphate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [glyceraldehyde-3-phosphate dehydrogenase]-N6-malonyl-L-lysine
nicotinamide + [glyceraldehyde-3-phosphate dehydrogenase]-L-lysine + 2'-O-malonyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3 K9 peptide]-N6-acetyl-L-lysine
nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3 K9 peptide]-N6-succinyl-L-lysine
nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-succinyl-ADP-ribose
show the reaction diagram
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-
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
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-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
show the reaction diagram
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
show the reaction diagram
NAD+ + [PrpE protein]-N6-acetyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
show the reaction diagram
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
show the reaction diagram
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
show the reaction diagram
NAD+ + [urate oxidase]-N6-acetyl-L-lysine
nicotinamide + [urate oxidase]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609
nicotinamide + [acetyl-coenzyme A synthetase]-L-lysine609 + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
deacetylation by CobB activates the acetyl-coenzyme A synthetase
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-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
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
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-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
Q8K2C6
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle
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-
?
NAD+ + [carbamoyl phosphate synthase 1]-N6-succinyl-L-lysine
nicotinamide + [carbamoyl phosphate synthase 1]-L-lysine + 2'-O-succinyl-ADP ribose
show the reaction diagram
-
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
show the reaction diagram
-
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
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-
?
NAD+ + [carbamoyl phosphate synthetase 1]-N6-glutaryl-L-lysine
nicotinamide + [carbamoyl phosphate synthetase 1]-L-lysine + 2'-O-glutaryl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [Cu/Zn superoxide dismutase]-N6-succinyl-L-lysine123
nicotinamide + [Cu/Zn superoxide dismutase]-L-lysine123 + 2'-O-succinyl-ADP-ribose
show the reaction diagram
-
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
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?
NAD+ + [forkhead box O3]-N6-acetyl-L-lysine
nicotinamide + [forkhead box O3]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
the enzyme deacetylates FOXO3 at K271 and K290
-
-
?
NAD+ + [glucose-6-phosphate dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [glucose-6-phosphate dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [protein]-N6-malonyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-malonyl-ADP-ribose
show the reaction diagram
NAD+ + [protein]-N6-succinyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-succinyl-ADP-ribose
show the reaction diagram
NAD+ + [PrpE protein]-N6-propionyl-L-lysine
nicotinamide + [PrpE protein]-L-lysine + 2'-O-propionyl-ADP-ribose
show the reaction diagram
-
N-Lysine propionylation controls the activity of propionyl-CoA synthetase
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-
?
NAD+ + [pyruvate dehydrogenase complex]-N6-succinyl-L-lysine
nicotinamide + [pyruvate dehydrogenase complex]-L-lysine + O-succinyl-ADP-ribose
show the reaction diagram
-
SIRT5 represses biochemical activity of, and cellular respiration through, the protein complex
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-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [succinate dehydrogenase]-N6-succinyl-L-lysine
nicotinamide + [succinate dehydrogenase]-L-lysine + O-succinyl-ADP-ribose
show the reaction diagram
-
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
show the reaction diagram
-
SIRT5 activates urate oxidase through deacetylation in mouse liver mitochondria
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-
?
additional information
?
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it is proposed that YfiQ and CobB catalyze the reversible acetylation of a protein that mediates carbon-induced cpxP transcription
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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the zinc-binding domain of the sirtuin proteins may play a similar role in substrate-specific recognition
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
(N6-thiosuccinyl)KSTGGKA
-
-
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
5-(1H-indol-3-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
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-[(6-methoxynaphthalen-1-yl)methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
5-[4-(benzyloxy)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
5-[4-(propan-2-yl)benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
5-[4-[(2-chlorobenzyl)oxy]-3-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
5-[4-[(4-bromobenzyl)oxy]benzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
5-[[5-(2,3-dichlorophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
-
Ac-AR(N6-thiosuccinyl)KST-NH2
-
-
Ac-RR(N6-thiosuccinyl)KRR-NH2
-
-
AGK2
-
40% inhibition at 0.1 mM
AR(N6-thiosuccinyl)KST
-
-
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
-
-
cambinol
-
-
fisetin
-
-
Isonicotinamide
-
-
KQTAR(N6-thiosuccinyl)K
-
-
KQTAR(N6-thiosuccinyl)KSTGGKA
-
-
nicotinamide
sirtinol
-
-
suramin
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
piceatannol
-
stimulates EC50: 0.07 mM
resveratrol
-
0.2 mM resveratrol can stimulate the Sirt5 deacetylase activity against the fluorophore-modified peptide substrate Fluor-de-Lys
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.084
Ac-(N6-succinyl)Lys-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
-
0.033
Ac-Leu-Gly-(N6-succinyl)Lys-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
-
0.0243
benzoyl-GVL(N6-acetyl)KEYGV-amide
-
pH 7.8, 37°C
-
0.0065
benzoyl-GVL(N6-adipoyl)KEYGV-amide
-
pH 7.8, 37°C
-
0.0041
benzoyl-GVL(N6-glutaryl)KEYGV-amide
-
pH 7.8, 37°C
-
0.0051
benzoyl-GVL(N6-malonyl)KEYGV-amide
-
pH 7.8, 37°C
-
0.416
benzoyl-GVL(N6-oxalyl)KEYGV-amide
-
pH 7.8, 37°C
-
0.0805
benzoyl-GVL(N6-pimeloyl)KEYGV-amide
-
pH 7.8, 37°C
-
0.409
benzoyl-GVL(N6-suberoyl)KEYGV-amide
-
pH 7.8, 37°C
-
0.0038
benzoyl-GVL(N6-succinyl)KEYGV-amide
-
pH 7.8, 37°C
-
0.0058
KQTAR(N6-malonyl)KSTGGWW
-
pH 7.5, 37°C
-
0.0061
KQTAR(N6-succinyl)KSTGGWW
-
pH 7.5, 37°C
-
0.45
KTRSG(N6-malonyl)KVMRRWW
-
pH 7.5, 37°C
-
0.15
KTRSG(N6-succinyl)KVMRRWW
-
pH 7.5, 37°C
-
0.069 - 1.605
NAD+
0.014
SGASE(N6-malonyl)KDIVHSGWW
-
pH 7.5, 37°C
-
0.0087
SGASE(N6-succinyl)KDIVHSGWW
-
pH 7.5, 37°C
-
0.0147 - 0.02
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
0.086
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.72
[protein]-N6-acetyl-L-lysine
-
mutant enzyme Y102A, at 8.0 pH and 25°C
0.29 - 1.658
[protein]-N6-succinyl-L-lysine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009
Ac-(N6-succinyl)Lys-7-amido-4-methylcoumarin
Homo sapiens
-
pH 8.0, 37°C
-
0.03
Ac-Leu-Gly-(N6-succinyl)Lys-7-amido-4-methylcoumarin
Homo sapiens
-
pH 8.0, 37°C
-
0.00039
benzoyl-GVL(N6-acetyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
-
0.01
benzoyl-GVL(N6-adipoyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
-
0.077
benzoyl-GVL(N6-glutaryl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
-
0.019
benzoyl-GVL(N6-malonyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
-
0.0016
benzoyl-GVL(N6-oxalyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
-
0.00028
benzoyl-GVL(N6-pimeloyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
-
0.00053
benzoyl-GVL(N6-suberoyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
-
0.053
benzoyl-GVL(N6-succinyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
-
0.025
KQTAR(N6-malonyl)KSTGGWW
Homo sapiens
-
pH 7.5, 37°C
-
0.037
KQTAR(N6-succinyl)KSTGGWW
Homo sapiens
-
pH 7.5, 37°C
-
0.268
KTRSG(N6-malonyl)KVMRRWW
Homo sapiens
-
pH 7.5, 37°C
-
0.079
KTRSG(N6-succinyl)KVMRRWW
Homo sapiens
-
pH 7.5, 37°C
-
0.000026 - 0.04
NAD+
0.028
SGASE(N6-malonyl)KDIVHSGWW
Homo sapiens
-
pH 7.5, 37°C
-
0.014
SGASE(N6-succinyl)KDIVHSGWW
Homo sapiens
-
pH 7.5, 37°C
-
0.052 - 0.135
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
0.242
[histone H3 K9 peptide]-N6-succinyl-L-lysine
Escherichia coli
-
pH 8.0, 37°C, wild-type enzyme
-
0.000066
[protein]-N6-acetyl-L-lysine
Homo sapiens
-
mutant enzyme Y102A, at 8.0 pH and 25°C
0.000026 - 0.04
[protein]-N6-succinyl-L-lysine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
Ac-(N6-succinyl)Lys-7-amido-4-methylcoumarin
Homo sapiens
-
pH 8.0, 37°C
197648
0.92
Ac-Leu-Gly-(N6-succinyl)Lys-7-amido-4-methylcoumarin
Homo sapiens
-
pH 8.0, 37°C
197647
0.016
benzoyl-GVL(N6-acetyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
197639
1.54
benzoyl-GVL(N6-adipoyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
197644
18.7
benzoyl-GVL(N6-glutaryl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
197643
3.76
benzoyl-GVL(N6-malonyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
197641
0.004
benzoyl-GVL(N6-oxalyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
197640
0.004
benzoyl-GVL(N6-pimeloyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
197645
0.001
benzoyl-GVL(N6-suberoyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
197646
13.9
benzoyl-GVL(N6-succinyl)KEYGV-amide
Homo sapiens
-
pH 7.8, 37°C
197642
4.3
KQTAR(N6-malonyl)KSTGGWW
Homo sapiens
-
pH 7.5, 37°C
197634
6.1
KQTAR(N6-succinyl)KSTGGWW
Homo sapiens
-
pH 7.5, 37°C
197633
0.6
KTRSG(N6-malonyl)KVMRRWW
Homo sapiens
-
pH 7.5, 37°C
197638
0.52
KTRSG(N6-succinyl)KVMRRWW
Homo sapiens
-
pH 7.5, 37°C
197637
2
SGASE(N6-malonyl)KDIVHSGWW
Homo sapiens
-
pH 7.5, 37°C
197636
1.6
SGASE(N6-succinyl)KDIVHSGWW
Homo sapiens
-
pH 7.5, 37°C
197635
3 - 8.9
[histone H3 K9 peptide]-N6-acetyl-L-lysine
197650
0.022 - 2.8
[histone H3 K9 peptide]-N6-succinyl-L-lysine
197649
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0106
benzoyl-GVL(N6-(3-acetylthiosuccinyl))KEYGV-amide
-
pH 7.8, 37°C
0.0172
benzoyl-GVL(N6-(3-butylsuccinyl))KEYGV-amide
-
pH 7.8, 37°C
0.0043
benzoyl-GVL(N6-(3-methyl-3-phenyl)succinyl)KEYGV-amide
-
pH 7.8, 37°C
0.1
benzoyl-GVL(N6-(3-phenyl)succinyl)KEYGV-amide
-
pH 7.8, 37°C
0.0381
benzoyl-GVL(N6-(N-benzyloxycarbonyl-L-aspartyl))KEYGV-amide
-
pH 7.8, 37°C
0.0249
benzoyl-GVL(N6-(N-phthaloyl-DL-gamma-glutamyl))KEYGV-amide
-
pH 7.8, 37°C
0.046
benzoyl-GVL(N6-(N2-Fmoc-beta-L-aspartyl))KEYGV-amide
-
pH 7.8, 37°C
0.0175
nicotinamide
-
wild type enzyme, at pH 8.0 and 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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-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
0.0195 - 0.097
3-(3,5-dibromo-4-hydroxybenzyliden)-5-iodo-1,3-dihydroindol-2-one
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
0.0036
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
0.043
cambinol
Homo sapiens
-
pH 8.0, 37°C
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
0.021 - 1.6
nicotinamide
0.049
sirtinol
Homo sapiens
-
pH 8.0, 37°C
0.0142 - 0.047
suramin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
in the cerebellar cortex, SIRT5 can be found in Purkinje cells, and is mainly distributed in the cytoplasm, but is not markedly expressed in the molecular layer or granular layer cells
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
predominantly nuclear
Manually annotated by BRENDA team
-
SIRT5 is overexpressed in human non-small cell lung cancer cells, high expression of SIRT5 predicts poor survival
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 4°C, crystal structure of wild-type enzyme, mutant enzyme S24A, mutant enzyme H80N, mutant enzyme F159A, and triple Sir2 mutant (D102G/F159A/R170A)
-
vapor diffusion at 20°C, crystal structure of the enzyme bound to KGLGKGGA(N6-succinyl)KRHRKW
-
crystals of native and selenomethionine-derivatized cobB are grown at room temperature using the hanging-drop, vapor-diffusion method. The crystal structure of the Escherichia coli cobB core domain (residues 40–274) in complex with an 11-residue peptide containing residues 12–19 of histone H4 and acetylated at lysine 16 is determined by a combination of Zn2+ and Se multiwavelength anomalous diffraction to 1.96 A resolution
-
crystal structure of Sirt5 in complex with a thioacetyl peptide is obtained, The corresponding acetyl peptide could not be crystallized with Sirt5
-
crystal structure of Sirt5 in complex with fluor-de-Lys peptide and resveratrol and crystal structure of Sirt5 in complex with fluor-de-Lys peptide and piceatannol
-
crystal structures of a binary complex of SIRT5 with an H3K9 succinyl peptide and a binary complex of SIRT5 with a bicyclic intermediate obtained by incubating SIRT5-H3K9 thiosuccinyl peptide co-crystals with NAD+
-
hanging drop vapor diffusion method at 18°C. X-ray crystal structures of the ternary complex of SIRT5 bound to a peptide substrate and carba-NAD+ (an unreactive NAD+ analogue)
-
hanging drop vapor-diffusion method at 20°C. Crystal structures of SIRT5 in complex with ADP-ribose, and crystal structures of SIRT5 bound to suramin
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52.9
-
melting temperature
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
a de novo protein synthesis inhibition experiment using cycloheximide shows that the SIRT5iso1-specific C-terminus is necessary for maintaining the stability of SIRT5iso1
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Hitrap column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are grown by hanging drop vapor diffusion method, truncated SIRT5(34–302) is cloned and expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
overexpression in Escherichia coli BL21
-
wild-type enzyme and active site mutants Y92F and R95M
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cigarette smoke extract induces the enzyme
-
enhanced expression of SIRT5 in the cerebral tissue of calorie restriction rats compared with rats that remained fed ad libitum
-
expression of SIRT5 increases during the progression of Alzheimer’s disease
-
overexpression of AMP-activated protein kinase (AMPK) in mouse hepatocytes downregulates expression of SIRT5 mRNA by 58%. The antidiabetes drug metformin (1 mM), an established AMPK activator, reduces the mouse SIRT5 protein level by 44% in cultured hepatocytes and by 31% in liver in vivo (300 mg/kg, 7 d)
-
SIRT5 is significantly down-regulated in cardiomyocytes upon oxidative stress
-
the enzyme expression is not affected by chemical oxidant treatment
-
women with reduced ovarian reserve or advanced maternal age have decreased SIRT5 mRNA, protein and desuccinylation activity in granulosa and cumulus cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D101N
-
the decreased NAD-dependent deacetylase activity for the mutant proteins is at least partly due to reduced binding affinities for NAD+
F159A
-
the Km value of the mutant enzyme is twice that of wild type enzyme, whereas the kcat is 5fold less. In the F159A mutant, two water molecules occupy the position of the Phe159 ring
H80N
-
mutant retains about 60% of the NAD binding ability of wild type Sir2
S24A
-
the decreased NAD-dependent deacetylase activity for the mutant proteins is at least partly due to reduced binding affinities for NAD+
R95M
-
desuccinylation decreases about 100fold, deacetylation decreases about 3fold
Y92F
-
desuccinylation decreases about 42fold, deacetylation decreases about 3fold
H158Y
-
mutation significantly increases the Km for desuccinylation
R105M
-
mutation significantly increases the Km for desuccinylation
Y102A
-
the mutant enzyme catalyzes both deacetylation and desuccinylation reactions with comparable efficiencies
Y102A/R105I
-
the mutant enzyme favores the deacetylase reaction over the desuccinylation reaction
Y102F
-
mutation significantly increases the Km for desuccinylation
H158Y
-
catalytically inactive
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine