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Information on EC 2.3.1.286 - protein acetyllysine N-acetyltransferase and Organism(s) Mus musculus and UniProt Accession Q923E4
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2.3.1.286 protein acetyllysine N-acetyltransferaseIUBMB Comments
The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2''-O-acetyl-ADP-D-ribose converts non-enzymically to 3''-O-acetyl-ADP-D-ribose.
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Word Map
- 2.3.1.286
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deacetylation
- resveratrol
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nad+-dependent
- nicotinamide
- deacetylases
- endothelial
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longevity
- peroxisome
- cardiac
- tnf
- obesity
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proliferator-activated
- cardiovascular
- dismutase
- neurodegenerative
- chromatin
-
neuroprotective
-
lifespan
- sirna
- myocardial
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amp-activated
- fibrosis
- adipose
-
polyphenolic
-
high-fat
- cardiomyocytes
-
forkhead
-
calorie
- alzheimer
- hdacs
-
obese
- adipocytes
- sod2
- steatosis
- caspase-3
- nafld
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cardioprotective
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foxo3a
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senescence-associated
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aging-related
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mir-34a
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hyperacetylation
-
anti-aging
- nampt
- tfam
- mnsod
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p-ampk
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monophosphate-activated
- coactivator-1
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non-histone
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
sirt1, sirt3, sirtuin, sirt2, sirtuin 1, sirtuin 3, sir2p, silent information regulator 2, sir2alpha, nad-dependent histone deacetylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NAD+-dependent protein deacetylase
-
-
-
-
protein lysine deacetylase
-
-
-
-
Sir2
-
-
-
-
SIRT3
SYSTEMATIC NAME
IUBMB Comments
[protein]-N6-acetyl-L-lysine:NAD+ N-acetyltransferase (NAD+-hydrolysing; 2''-O-acetyl-ADP-D-ribose-forming)
The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2''-O-acetyl-ADP-D-ribose converts non-enzymically to 3''-O-acetyl-ADP-D-ribose.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + [Fluor de Lys]-N6-acetyl-L-lysine
nicotinamide + [Fluor de Lys]-L-lysine + 2'-O-acetyl-ADP-ribose
Q923E4
-
-
-
?
NAD+ + [SREBP-1c]-N6-acetyl-L-lysine
nicotinamide + [SREBP-1c]-L-lysine + 2'-O-acetyl-ADP ribose
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
KKGQSTSRHKKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
-
-
-
r
KKGQSTSRHKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
-
-
-
-
r
NAD+ + [heat shock protein 10]-N6-acetyl-L-lysine56
nicotinamide + [heat shock protein 10]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine413
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine413 + 2'-O-acetyl-ADP-ribose
NAD+ + [very long-chain acyl-CoA dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [very long-chain acyl-CoA dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
-
-
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
r
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
-
?
NAD+ + [SREBP-1c]-N6-acetyl-L-lysine
nicotinamide + [SREBP-1c]-L-lysine + 2'-O-acetyl-ADP ribose
Q923E4
SREBP-1c is a key lipogenic activator. Deacetylation of SREBP-1c by SIRT1 inhibits SREBP-1c activity by decreasing its stability and its association with its lipogenic target gene promoters
-
-
?
NAD+ + [SREBP-1c]-N6-acetyl-L-lysine
nicotinamide + [SREBP-1c]-L-lysine + 2'-O-acetyl-ADP ribose
Q923E4
SREBP-1c is a key lipogenic activator
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine413
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine413 + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine413
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine413 + 2'-O-acetyl-ADP-ribose
acetylation of Lys413 decreases catalysis and SIRT3 reactivates isocitrate dehydrogenase 2 upon deacetylation
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + [SREBP-1c]-N6-acetyl-L-lysine
nicotinamide + [SREBP-1c]-L-lysine + 2'-O-acetyl-ADP ribose
Q923E4
SREBP-1c is a key lipogenic activator. Deacetylation of SREBP-1c by SIRT1 inhibits SREBP-1c activity by decreasing its stability and its association with its lipogenic target gene promoters
-
-
?
NAD+ + [heat shock protein 10]-N6-acetyl-L-lysine56
nicotinamide + [heat shock protein 10]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [isocitrate dehydrogenase 2]-N6-acetyl-L-lysine413
nicotinamide + [isocitrate dehydrogenase 2]-L-lysine413 + 2'-O-acetyl-ADP-ribose
acetylation of Lys413 decreases catalysis and SIRT3 reactivates isocitrate dehydrogenase 2 upon deacetylation
-
-
?
NAD+ + [very long-chain acyl-CoA dehydrogenase]-N6-acetyl-L-lysine
nicotinamide + [very long-chain acyl-CoA dehydrogenase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
?
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
-
-
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
overall reaction
-
-
r
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP-activated protein kinase-alpha1
Q923E4
positive regulator of SIRT1 function
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
acetylation of heat shock protein 10 by isoform SIRT3 enhances medium-chain acyl-CoA dehydrogenase folding, enzyme activity, and fat oxidation
metabolism
acetylation of Lys413 decreases catalysis and SIRT3 reactivates isocitrate dehydrogenase 2 upon deacetylation. SIRT3-dependent deacetylation of isocitrate dehydrogenase 2 suppresses cellular stress by reactive oxygen species (ROS). Acetylation of Lys413 is regulated by SIRT3 in response to calorie and glucose restriction
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
Q923E4
phosphorylation of Thr522 is an important allosteric mechanism to activate SIRT1 in response to stress. While non-phosphorylation of this residue leads to formation of less-active oligomers, phosphorylation helps to maintain the monomeric status of SIRT1, resulting in increased activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform SIRT1 activity is down-regulated in the brains of two complementary Huntington's disease mouse models
Q923E4
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ponugoti, B.; Kim, D.H.; Xiao, Z.; Smith, Z.; Miao, J.; Zang, M.; Wu, S.Y.; Chiang, C.M.; Veenstra, T.D.; Kemper, J.K.
SIRT1 deacetylates and inhibits SREBP-1C activity in regulation of hepatic lipid metabolism
J. Biol. Chem.
285
33959-33970
2010
Mus musculus (Q923E4), Mus musculus
Yu, W.; Dittenhafer-Reed, K.E.; Denu, J.M.
SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status
J. Biol. Chem.
287
14078-14086
2012
Mus musculus (Q8R104)
Guo, X.; Kesimer, M.; Tolun, G.; Zheng, X.; Xu, Q.; Lu, J.; Sheehan, J.K.; Griffith, J.D.; Li, X.
The NAD(+)-dependent protein deacetylase activity of SIRT1 is regulated by its oligomeric status
Sci. Rep.
2
640
2012
Mus musculus (Q923E4)
Lu, Z.; Chen, Y.; Aponte, A.M.; Battaglia, V.; Gucek, M.; Sack, M.N.
Prolonged fasting identifies heat shock protein 10 as a sirtuin 3 substrate: elucidating a new mechanism linking mitochondrial protein acetylation to fatty acid oxidation enzyme folding and function
J. Biol. Chem.
290
2466-2476
2015
Mus musculus (Q8R104)
Zhang, Y.; Bharathi, S.S.; Rardin, M.J.; Uppala, R.; Verdin, E.; Gibson, B.W.; Goetzman, E.S.
SIRT3 and SIRT5 regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase
PLoS ONE
10
e0122297
2015
Mus musculus (Q8R104), Mus musculus
Tulino, R.; Benjamin, A.C.; Jolinon, N.; Smith, D.L.; Chini, E.N.; Carnemolla, A.; Bates, G.P.
SIRT1 activity is linked to its brain region-specific phosphorylation and is impaired in Huntington's disease mice
PLoS ONE
11
e0145425
2016
Mus musculus (Q923E4), Mus musculus
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