2.3.1.286: protein acetyllysine N-acetyltransferase
This is an abbreviated version!
For detailed information about protein acetyllysine N-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.286
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2.3.1.286
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deacetylation
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resveratrol
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nad+-dependent
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nicotinamide
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deacetylases
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endothelial
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longevity
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peroxisome
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cardiac
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tnf
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obesity
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proliferator-activated
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cardiovascular
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dismutase
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neurodegenerative
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chromatin
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neuroprotective
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lifespan
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sirna
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myocardial
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amp-activated
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fibrosis
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adipose
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polyphenolic
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high-fat
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cardiomyocytes
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forkhead
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calorie
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alzheimer
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hdacs
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obese
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adipocytes
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sod2
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steatosis
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caspase-3
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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
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anti-aging
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nampt
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tfam
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mnsod
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p-ampk
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monophosphate-activated
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coactivator-1
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non-histone
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medicine
- 2.3.1.286
-
deacetylation
- resveratrol
-
nad+-dependent
- nicotinamide
- deacetylases
- endothelial
-
longevity
- peroxisome
- cardiac
- tnf
- obesity
-
proliferator-activated
- cardiovascular
- dismutase
- neurodegenerative
- chromatin
-
neuroprotective
-
lifespan
- sirna
- myocardial
-
amp-activated
- fibrosis
- adipose
-
polyphenolic
-
high-fat
- cardiomyocytes
-
forkhead
-
calorie
- alzheimer
- hdacs
-
obese
- adipocytes
- sod2
- steatosis
- caspase-3
- nafld
-
cardioprotective
-
foxo3a
-
senescence-associated
-
aging-related
-
mir-34a
-
hyperacetylation
-
anti-aging
- nampt
- tfam
- mnsod
-
p-ampk
-
monophosphate-activated
- coactivator-1
-
non-histone
- medicine
Reaction
Synonyms
Af2Sir2, Clr3, CobB, HDAC, histone deacetylase, Hst1, HST2, Hst2p, KAT, More, NAD+-dependent protein deacetylase, NAD-dependent histone deacetylase, NAD-dependent protein deacetylase, nicotinamide adenine dinucleotide-dependent protein deacetylase, patZ, peptidyl-lysine N-acetyltransferase, phnO, protein lysine acetyltransferase, protein lysine deacetylase, Rv1151c, silent information regulator 2, Sir-2, Sir2, SIR2-Af1, Sir2-Af2, Sir2A, Sir2Af2, Sir2alpha, Sir2p, SIRT1, SIRT2, SIRT3, SIRT5, sirtuin, sirtuin 1, sirtuin 3, sirtuin-2 deacetylase, YfiQ, YiaC, YjaB
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General Information
General Information on EC 2.3.1.286 - protein acetyllysine N-acetyltransferase
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evolution
malfunction
metabolism
physiological function
additional information
Phno is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
evolution
YfiQ is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
evolution
Yiac is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
evolution
YjaB is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
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NAD+-dependent SIRT1 deactivation has a key role on ischemia-reperfusion-induced apoptosis
malfunction
Q96EB6
SIRT1 depletion by RNA interference attenuates capsaicin-induced apoptosis in A-549 cancer cells and autophagy in MRC-5 cells
acetylation of Lys413 decreases catalysis and SIRT3 reactivates isocitrate dehydrogenase 2 upon deacetylation. SIRT3-dependent deacetylation of isocitrate dehydrogenase 2 suppresses cellular stress by reactive oxygen species (ROS). Acetylation of Lys413 is regulated by SIRT3 in response to calorie and glucose restriction
metabolism
Q96EB6
caloric restriction can extend life-span by inducing SIRT1 expression and promoting the long-term survival of irreplaceable cells
metabolism
Q96EB6
caloric restriction can extend life-span by inducing SIRT1 expression and promoting the long-term survival of irreplaceable cells
metabolism
Q96EB6
Sir2 is involved in the regulation of p53 function via deacetylation
metabolism
Q96EB6
SIRT1 modulates DNA repair activity, which can be regulated by the acetylation status of repair protein Ku70 following DNA damage
metabolism
the deacetylation of [histone H4]-N6-acetyl-L-lysine16 by Sirt2 may be pivotal to the formation of condensed chromatin
metabolism
the enzyme can regulate flux and anapleurosis of this central metabolic cycle
acetylation of heat shock protein 10 by isoform SIRT3 enhances medium-chain acyl-CoA dehydrogenase folding, enzyme activity, and fat oxidation
physiological function
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enzyme expression is crucial for the survival of the cell
physiological function
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the activation of SIRT1 is significantly associated with improved protection against hepatic triglyceride accumulation
physiological function
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heterochromatin assembly requires the SIR proteins Sir3, the primary structural component of SIR heterochromatin, and the Sir2-4 complex, responsible for the targeted recruitment of SIR proteins and the deacetylation of lysine 16 of histone H4
physiological function
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increase of enzyme activity by caloric restriction or osmotic stress increases genome stability and lifespan in Saccharomyces cerevisiae
physiological function
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increased enzyme expression of extends life span in a dose-dependent manner
physiological function
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maintenance of [histone H3]-L-lysine9 methylation at centromeres requires the histone deacetylases Sir2 and Clr3
physiological function
Sirt2 may act as a tumor suppressor and may function to control the cell cycle by acetylation of alpha-tubulin
physiological function
the enzyme does not repress transcription with either naked DNA templates or chromatin assembled from native (and mostly unacetylated) histones
physiological function
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the enzyme is a pro-longevity factor for replicative lifespan in Saccharomyces cerevisiae. The enzyme is required for transcriptional silencing at mating type loci, telomeres, and rDNA loci. The enzyme also represses transcription of highly expressed growth-related genes, such as PMA1 and some ribosomal protein genes
physiological function
the enzyme regulates the expression of surface antigens to evade the detection by host immune surveillance by removing medium and long chain fatty acyl groups from protein lysine residues
physiological function
Nepsilon-lysine acetyltransferases (KATs) specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. Posttranslational modifications, such as Nepsilon-lysine acetylation, regulate protein function. The enzymes show a high degree of substrate specificity
physiological function
Nepsilon-lysine acetyltransferases (KATs) specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. Posttranslational modifications, such as Nepsilon-lysine acetylation, regulate protein function. The enzymes show a high degree of substrate specificity. Enzyme YfiQ can inhibit Escherichia coli cell migration in soft agar
physiological function
Nepsilon-lysine acetyltransferases (KATs) specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. Posttranslational modifications, such as Nepsilon-lysine acetylation, regulate protein function. The enzymes show a high degree of substrate specificity. Enzyme YiaC can inhibit Escherichia coli cell migration in soft agar. Overexpression of enzyme mutant YiaC YF70A inhibits migration similarly to overexpression of wild-type YiaC
physiological function
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the enzyme is a pro-longevity factor for replicative lifespan in Saccharomyces cerevisiae. The enzyme is required for transcriptional silencing at mating type loci, telomeres, and rDNA loci. The enzyme also represses transcription of highly expressed growth-related genes, such as PMA1 and some ribosomal protein genes
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the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism