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
ECTree
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Engineering
Engineering on EC 2.3.1.286 - protein acetyllysine N-acetyltransferase
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Q115A
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the mutant shows very weak deacetylation activity compared to the wild type enzyme
E78A
site-directed mutagenesis, mutation of the conserved catalytic amino acid prevents PhnO-dependent acetylation
F70A
site-directed mutagenesis, mutation of the conserved catalytic amino acid reduces YiaC-dependent acetylation compared to wild-type. Overexpression of YiaC YF70A inhibits cell migration similarly to overexpression of wild-type YiaC
Y115A
site-directed mutagenesis, mutation of the conserved catalytic amino acid prevents YiaC-dependent acetylation. Mutant YiaC Y115A is unable to inhibit cell migration in contrast to the wild-type enzyme
Y117A
site-directed mutagenesis, mutation of the conserved catalytic amino acid reduces YjaB-dependent acetylation compared to wild-type
Y117F
site-directed mutagenesis, mutation of the conserved catalytic amino acid does not alter YjaB-dependent acetylation compared to wild-type
Y128A
site-directed mutagenesis, mutation of the conserved catalytic amino acid prevents PhnO-dependent acetylation
D118N
the mutant retains approximately 13% of the activity of the wild type protein
H135A
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the kcat/Km profile for the mutant exhibits no pH dependence over the range tested (pH 5.4-9.4), with kcat/Km values 2 orders of magnitude lower than wild type at high pH values
I117F
the mutant is nearly as active as the wild type protein (about 75% activity)
I117L
the mutant retains approximately 25% of the activity of the wild type protein
I117V
the mutant is nearly as active as the wild type protein (about 65% activity)
D101N
additional information
the mutation affects the deacetylation activity of the enzyme
D101N
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the mutation affects the deacetylation activity of the enzyme
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generation and analysis of the DELTAackA pta yfiQ mutant lacking the two known mechanisms of protein acetylation, but residual acetylation remains
additional information
generation and analysis of the DELTAackA pta yfiQ mutant lacking the two known mechanisms of protein acetylation, but residual acetylation remains
additional information
generation and analysis of the DELTAackA pta yfiQ mutant lacking the two known mechanisms of protein acetylation, but residual acetylation remains
additional information
generation and analysis of the DELTAackA pta yfiQ mutant lacking the two known mechanisms of protein acetylation, but residual acetylation remains