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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
nat8l, aspartate n-acetyltransferase, l-aspartate n-acetyltransferase, aspartate acetyltransferase,
more
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acetyltransferase, aspartate
-
-
-
aspartate acetyltransferase
-
-
-
aspartate N-acetyltransferase
L-aspartate N-acetyltransferase
-
-
-
ANAT
-
aspartate N-acetyltransferase
-
-
aspartate N-acetyltransferase
-
aspartate N-acetyltransferase
-
-
NAT
-
-
NAT8L
-
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acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartate
-
-
-
-
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Acyl group transfer
-
-
-
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acetyl-CoA:L-aspartate N-acetyltransferase
-
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acetyl-CoA + 2,3-diaminosuccinate
CoA + ?
-
-
?
acetyl-CoA + 3-methyl-L-aspartate
CoA + N-acetyl-3-methyl-L-aspartate
-
-
?
acetyl-CoA + glutamate
CoA + N-acetylglutamate
-
[14C]glutamate is acetylated with an approximately 50-fold lower affinity and a similar Vmax compared with aspartate
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartate
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
reaction of EC 2.3.1.1
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamic acid
additional information
?
-
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
highly specific
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
highly specific
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
decreases in enzyme activity occur in a number of neurological disorders, possible role in neuronal mitochondrial energy metabolism
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamic acid
less than 1% of the activity with L-aspartate
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamic acid
less than 1% of the activity with L-aspartate
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamic acid
-
only 10% activity compared to L-aspartate
-
?
additional information
?
-
-
reduced CoA with acetyl-AMP can substitute for acetyl-CoA, about 50% of activity with acetyl-CoA
-
?
additional information
?
-
-
highly specific for L-aspartate with 3% or less active for L-glutamate, L-asparagine, L-glutamine, or aspartate-glutamate dipeptide
-
?
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acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartate
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
decreases in enzyme activity occur in a number of neurological disorders, possible role in neuronal mitochondrial energy metabolism
-
-
?
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KCl
-
2fold enzyme activity at 0.05 - 0.1 M
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(2S)-2-(3-phenylpropanamido)butanedioic acid
-
(2S)-2-(3-phenylpropanamido)pentanedioic acid
-
(2S)-2-[[(benzyloxy)carbonyl]amino]butanedioic acid
-
(2S)-2-[[(benzyloxy)carbonyl]amino]pentanedioic acid
-
4-aminomethyl(N-carboethyl,N-4-carboxy-2,6-dichlorobenzyl)phthalate
-
-
Acyl-AMP derivatives
-
e.g. acetyl-AMP, butyryl-AMP, strong
-
adenosine 3',5'-monophosphate
truncated bisubstrate analog
adenosine 5'-diphosphate
truncated bisubstrate analog
adenosine 5'-monophosphate
truncated bisubstrate analog
Adenosine 5'-triphosphate
truncated bisubstrate analog
CHAPS
-
40% of activity at 12 mM, 10% of activity at 20 mM
cholamido propane sulfonate
-
cyclohexylmaltoside
cymal5, high inhibition at CMC concentration
DMSO
20% inhibition at 40% v/v
glutamate
-
Glutamate is a competitive inhibitor. No inhibition is observed with other amino acids, indicating that the enzyme is specific.
lauryldimethylamine-N-oxide
complete inhibition at CMC concentration
N-(2,6-dibromo-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
-
N-(2,6-dichloro-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
-
N-(acetylcysteaminyl boc ester)aspartate
truncated bisubstrate analog
-
N-(acetylcysteinyl boc ester)aspartate
truncated bisubstrate analog
-
N-(acetylcysteinyl)aspartate
truncated bisubstrate analog
-
N-acetyl-(dimethyl)aspartyl-conjugated CoA
coenzyme A coupled to methylated N-acetyl aspartate, bisubstrate inhibitor
N-acetyl-L-aspartic acid
-
IC50: 0.85 mM
N-acetylaspartate
truncated bisubstrate analog
N-acetylaspartyl-conjugated CoA
coenzyme A coupled to N-acetyl aspartate, bisubstrate inhibitor
N-carbobenzyloxy-L-aspartic acid
-
N-carbobenzyloxy-L-glutamic acid
-
-
N-chloroacetylaspartate
truncated bisubstrate analog
-
n-decyl-N,N-dimethylamine-N-oxide
high inhibition at CMC concentration
N-methyl-N-nonanoyl-beta-D-glucosylamine
Mega-9, high inhibition at CMC concentration
n-nonyl-beta-D-glucopyranoside
high inhibition at CMC concentration
N-propionyl-(dimethyl)aspartyl-conjugated CoA
coenzyme A coupled to N-propionyl aspartate, bisubstrate inhibitor
octyl pentaglycol
high inhibition at CMC concentration
octyl tetraglycol
high inhibition at CMC concentration
octylglucoside
high inhibition at CMC concentration
polymaleic anhydride C10
-
polymaleic anhydride C12
-
polymaleic anhydride C16
high inhibition at CMC concentration
polymaleic anhydride C4
high inhibition at CMC concentration
polymaleic anhydride C6
complete inhibition at CMC concentration
polymaleic anhydride C8
-
SDS
complete inhibition at CMC concentration
sodium dodecanoyl sarcosine
-
additional information
effect of different detergents on the enzyme activity: non-ionic detergents such as Triton X-100 are less disruptive to protein structures than ionic detergents such as SDS, detergents such as C12E8, Tween 20 and several maltosides caused minimal disruption of the enzyme, with greater than 50% residual activity after incubation with CMC levels of each of these detergents. In contrast, significant loss of activity is observed upon incubation with C8 detergents, cymal5, octylglucoside and some shorter chain polymaleic anhydride (pmal) detergents. Ionic detergent SDS and a zwitterionic detergent lauryldimethylamine-N-oxide cause nearly complete loss of catalytic activity
-
additional information
-
effect of different detergents on the enzyme activity: non-ionic detergents such as Triton X-100 are less disruptive to protein structures than ionic detergents such as SDS, detergents such as C12E8, Tween 20 and several maltosides caused minimal disruption of the enzyme, with greater than 50% residual activity after incubation with CMC levels of each of these detergents. In contrast, significant loss of activity is observed upon incubation with C8 detergents, cymal5, octylglucoside and some shorter chain polymaleic anhydride (pmal) detergents. Ionic detergent SDS and a zwitterionic detergent lauryldimethylamine-N-oxide cause nearly complete loss of catalytic activity
-
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Methamphetamine
maximum increase in activity in SH-SY5Y cells is found at 1 microM methamphetamine at 24 h, increase in activity is about 2fold
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Adenocarcinoma
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Alzheimer Disease
Transcriptional regulation of N-acetylaspartate metabolism in the 5xFAD model of Alzheimer's disease: Evidence for neuron-glia communication during energetic crisis.
Canavan Disease
Brain Nat8l Knockdown Suppresses Spongiform Leukodystrophy in an Aspartoacylase-Deficient Canavan Disease Mouse Model.
Canavan Disease
Design and optimization of aspartate N-acetyltransferase inhibitors for the potential treatment of Canavan disease.
Canavan Disease
Discovery of Novel Inhibitors of a Critical Brain Enzyme Using a Homology Model and a Deep Convolutional Neural Network.
Carcinoma
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Carcinoma, Non-Small-Cell Lung
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Carcinoma, Non-Small-Cell Lung
Correction: Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Carcinoma, Squamous Cell
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Lung Neoplasms
Bridging the gap between non-targeted stable isotope labeling and metabolic flux analysis.
Lung Neoplasms
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Lung Neoplasms
Correction: Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Neoplasms
Bridging the gap between non-targeted stable isotope labeling and metabolic flux analysis.
Neoplasms
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Neoplasms
Role of Increased n-acetylaspartate Levels in Cancer.
Nervous System Diseases
Structure of the Brain N-Acetylaspartate Biosynthetic Enzyme NAT8L Revealed by Computer Modeling.
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0.92
2,3-diaminosuccinate
pH 7.4, temperature not specified in the publication
0.36
3-methyl-L-aspartate
pH 7.4, temperature not specified in the publication
8.6
L-glutamate
pH 7.4, temperature not specified in the publication
additional information
additional information
-
0.001
acetyl-CoA
wild-type, pH 7.1, 30°C
0.0031
acetyl-CoA
pH 7.4, temperature not specified in the publication
0.009
acetyl-CoA
-
in presence of 0.5 mM CHAPS
0.012
acetyl-CoA
mutant P142A, pH 7.1, 30°C
0.013
acetyl-CoA
-
in presence of 1 mM CHAPS
0.017
acetyl-CoA
mutant S132F/R133F, pH 7.1, 30°C
0.019
acetyl-CoA
mutant R133A, pH 7.1, 30°C
0.058
acetyl-CoA
-
pH 7.1, 37°C
0.082
acetyl-CoA
mutant R81A, pH 7.1, 30°C
0.127
acetyl-CoA
mutant E101A, pH 7.1, 30°C
0.14
acetyl-CoA
mutant R220K, pH 7.1, 30°C
0.4
acetyl-CoA
mutant R220A, pH 7.1, 30°C
0.8 - 1.06
acetyl-CoA
-
pH 7.0, 37°C, slightly varying Km depending on source organelle
0.09
L-aspartate
-
-
0.09
L-aspartate
wild-type, pH 7.1, 30°C
0.095
L-aspartate
mutant P142A, pH 7.1, 30°C
0.128
L-aspartate
mutant S132F/R133F, pH 7.1, 30°C
0.16
L-aspartate
pH 7.4, temperature not specified in the publication
0.166 - 0.174
L-aspartate
-
pH 7.0, 37°C, slightly varying Km depending on source organelle
0.2
L-aspartate
mutant R81A, pH 7.1, 30°C
0.434
L-aspartate
mutant E101A, pH 7.1, 30°C
0.58
L-aspartate
-
pH 7.1, 37°C
1.61
L-aspartate
mutant R220K, pH 7.1, 30°C
3.37
L-aspartate
mutant R220A, pH 7.1, 30°C
additional information
additional information
-
Km value for acetyl-CoA
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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0.035
2,3-diaminosuccinate
pH 7.4, temperature not specified in the publication
0.0018
3-methyl-L-aspartate
pH 7.4, temperature not specified in the publication
0.0071
acetyl-CoA
pH 7.4, temperature not specified in the publication
0.0071
L-aspartate
pH 7.4, temperature not specified in the publication
0.023
L-glutamate
pH 7.4, temperature not specified in the publication
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0.031
(2S)-2-(3-phenylpropanamido)butanedioic acid
pH 7.4, temperature not specified in the publication
0.038
(2S)-2-(3-phenylpropanamido)pentanedioic acid
pH 7.4, temperature not specified in the publication
0.017
(2S)-2-[[(benzyloxy)carbonyl]amino]butanedioic acid
pH 7.4, temperature not specified in the publication
0.012
(2S)-2-[[(benzyloxy)carbonyl]amino]pentanedioic acid
pH 7.4, temperature not specified in the publication
0.0006
4-aminomethyl(N-carboethyl,N-4-carboxy-2,6-dichlorobenzyl)phthalate
pH 7.4, temperature not specified in the publication
-
2.3
adenosine 3',5'-monophosphate
pH not specified in the publication, temperature not specified in the publication
1.1
adenosine 5'-diphosphate
pH not specified in the publication, temperature not specified in the publication
4
adenosine 5'-monophosphate
pH not specified in the publication, temperature not specified in the publication
0.96
Adenosine 5'-triphosphate
pH not specified in the publication, temperature not specified in the publication
0.00077
N-(2,6-dibromo-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
pH 7.4, temperature not specified in the publication
0.00061
N-(2,6-dichloro-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
pH 7.4, temperature not specified in the publication
2.1
N-(acetylcysteaminyl boc ester) aspartate
pH not specified in the publication, temperature not specified in the publication
-
0.87
N-(acetylcysteinyl boc ester)aspartate
pH not specified in the publication, temperature not specified in the publication
-
1.03
N-(acetylcysteinyl) aspartate
pH not specified in the publication, temperature not specified in the publication
-
0.018
N-acetyl-(dimethyl)aspartyl-conjugated CoA
pH not specified in the publication, temperature not specified in the publication
0.56
N-acetyl-L-aspartate
-
-
1.6
N-acetylaspartate
pH not specified in the publication, temperature not specified in the publication
0.000275
N-acetylaspartyl-conjugated CoA
pH not specified in the publication, temperature not specified in the publication
0.017
N-carbobenzyloxy-L-aspartic acid
pH 7.4, temperature not specified in the publication
0.012
N-carbobenzyloxy-L-glutamic acid
pH 7.4, temperature not specified in the publication
-
0.2
N-chloroacetylaspartate
pH not specified in the publication, temperature not specified in the publication
-
0.000048
N-propionyl-(dimethyl)aspartyl-conjugated CoA
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
Ki values for various inhibitors
-
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0.42
CoA
Rattus norvegicus
-
IC50: 0.42 mM
0.85
N-acetyl-L-aspartic acid
Rattus norvegicus
-
IC50: 0.85 mM
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0.0015
-
activity of cloned mouse NAT8L fusion protein with N-terminal His6 tag
0.0018
-
activity of cloned mouse NAT8L fusion protein with C-terminal His6 tag
0.0025
-
activity of cloned wild type mouse NAT8L protein
70
recombinant enzyme, pH 7.4, temperature not specified in the publication
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5.2 - 8
-
about 13% of maximal activity at pH 5.2, about 50% of maximal activity at pH 8.0
6 - 9.5
the enzymatic activity decreases at pH values below pH 7.5. A fit of the Vmax/Km data to a model which assumes that the protonation of a single group leads to loss of activity results in a pK value of 6.8 for a group that must be ionized for the enzyme to remain catalytically active. By contrast, the Vmax profile does not show substantial changes across the pH range
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37
-
assay at
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-
-
-
brenda
-
-
-
brenda
-
Uniprot
brenda
normal patients and patients with Canavan disease
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
male Sprague-Dawley rat
-
-
brenda
male sprague-dawley rats
-
-
brenda
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-
brenda
-
brenda
-
brenda
-
brenda
-
brenda
-
-
brenda
-
cultured
brenda
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
highest levels in brain and spinal cord
brenda
additional information
-
In PCR, no specific amplification was observed with liver, kidney, lung, skeletal muscle, testis and heart cDNA of mice.
brenda
additional information
-
highest activity in the brainstem and the spinal cord, lowest activity in the retina, no activity in heart, kidney or liver of rat
brenda
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enzyme is present in both cytoplasm and mitochondria
brenda
-
most likely endoplasmic reticulum
-
brenda
-
-
-
brenda
additional information
-
not in mitochondria
-
brenda
exclusively associated with the endoplasmic reticulum. the membrane region comprises alpha-helices and the catalytic site is in the cytosol. The membrane region, i.e. region 4, is necessary and sufficient to target isoform NAT8L to the endoplasmic reticulum
brenda
-
-
brenda
membrane-associated, the enzyme contains a membrane anchor region
brenda
-
-
brenda
enzyme is present in both cytoplasm and mitochondria
brenda
-
-
brenda
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malfunction
Canavan disease is a fatal, neurological disease that is caused by an interruption in the metabolism of a critical amino acid, N-acetyl-L-aspartic acid. Defects at multiple locations in the aspA gene that codes for aspartoacylase, EC 3.5.1.15, lead to mutant forms of this enzyme that are either not expressed or rapidly degraded, or have significantly impaired catalytic activity, resulting in N-acetyl-L-aspartic acid accumulation. A second gene knock-out in the Nat8l gene which codes for aspartate N-acetyltransferase, the enzyme that synthesizes N-acetyl-L-aspartic acid, reverses these adverse effects, leading to normal myelination and a decrease in Canavan disease symptoms
physiological function
overexpression of Nat8L drains glucose-derived acetyl-CoA into the N-acetyl-L-aspartate pool at the expense of cellular lipids and certain amino acids. A combined activation of neutral and lysosomal (acid) lipolysis is responsible for the increased lipid degradation. Nat8l overexpression increases the number of autophagosomes and autolysosomes. Expression of Nat8l and aspartoacylase are nutritionally regulated and respond robustly to changes in glucose availability
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NAT8L_DANRE
282
1
32270
Swiss-Prot
other Location (Reliability: 1 )
NAT8L_HUMAN
302
1
32837
Swiss-Prot
other Location (Reliability: 2 )
NAT8L_MOUSE
299
1
32777
Swiss-Prot
other Location (Reliability: 1 )
NAT8L_RAT
299
1
32719
Swiss-Prot
other Location (Reliability: 1 )
NAT8L_XENTR
271
1
30726
Swiss-Prot
Mitochondrion (Reliability: 5 )
A0A375A7H2_9GAMM
169
0
18298
TrEMBL
-
A0A1S2X6C5_SALSA
90
0
10091
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A085U967_YERRU
167
0
18349
TrEMBL
-
A0A2K8W1D4_9GAMM
170
0
18387
TrEMBL
-
A0A482ZQH8_9GAMM
165
0
18299
TrEMBL
-
A0A090PF97_9VIBR
160
0
17162
TrEMBL
-
A0A076LLY5_9GAMM
167
0
18060
TrEMBL
-
A0A0A1R6H8_9ENTR
167
0
18116
TrEMBL
-
A0A090U527_9VIBR
160
0
17141
TrEMBL
-
A0A0G4JSI5_9GAMM
188
0
20896
TrEMBL
-
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33900
x * 56000-60000, recombinant MBP-His-tagged enzyme without membrane anchor, SDS-PAGE, x * 33900, recombinant His-tagged enzyme without membrane anchor, SDS-PAGE
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multimer
-
at least 10 bands on SDS-PAGE indicating a large enzyme complex
?
x * 33000-35000, SDS-PAGE of recombinant His-tagged protein
?
x * 56000-60000, recombinant MBP-His-tagged enzyme without membrane anchor, SDS-PAGE, x * 33900, recombinant His-tagged enzyme without membrane anchor, SDS-PAGE
?
x * 33000-35000, SDS-PAGE of recombinant His-tagged protein
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molecular modeling of the active site shows that only the amino acid aspartate, but not glutamate, can fit into the active site pocket
purified recombinant His-tagged truncated enzyme, X-ray diffraction structure determination and analysis
molecular modeling of the active site shows that only the amino acid aspartate, but not glutamate, can fit into the active site pocket
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C128A
mutation in region 4, 94% of wild-type expression, 88% of wild-type activity
C139A
mutation in region 4, 70% of wild-type expression, 126% of wild-type activity
D168A
mutation in region 5, 46% of wild-type expression, no residual activity
D168E
mutation in region 5, 63% of wild-type expression, 7% of wild-type activity
E101A
mutation in region 3, 97% of wild-type expression, 42% of wild-type activity
E101D
mutation in region 3, 61% of wild-type expression, 99% of wild-type activity
P142A
mutation in region 4, 113% of wild-type expression, 116% of wild-type activity
R133A
mutation in region 4, 78% of wild-type expression, 64% of wild-type activity
R133K
mutation in region 4, 69% of wild-type expression, 89% of wild-type activity
R220A
mutation in region 5, 101% of wild-type expression, 14% of wild-type activity
R220K
mutation in region 5, 104% of wild-type expression, 25% of wild-type activity
R81A
mutation in region 3, 57% of wild-type expression, 37% of wild-type activity
R81K
mutation in region 3, 90% of wild-type expression, 82% of wild-type activity
S132F/R133F
mutation in region 4, 92% of wild-type expression, 41% of wild-type activity
additional information
transfection of truncated forms of isoform NAT8L into HEK-293T cells indicates that the 68 N-terminal residues, i.e. regions 1 and 2, have no importance for the catalytic activity and the subcellular localization of the enzyme. The membrane region, i.e. region 4, is necessary and sufficient to target isoform NAT8L to the endoplasmic reticulum
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100
-
no enzyme activity after boiling
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0-5°C, 8-10 mg protein/ml, stable for weeks
-
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recombinant functional and soluble dual His- and MBP-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and amylose affinity chromatography, MBP tag cleavage by 3C protease, method evaluation
-
-
partial
-
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expression in HEK-293T cell
gene nat8l, sequence comparisons, subcloning of the genes for thioredoxin (TRX), glutathione S-transferase (GST) or maltose binding protein (MBP), followed by a linker region (21-68-amino acids) containing various cleavage site sequences, and then connected to the N-terminal of the nat8l gene, without the membrane anchor, recombinant functional and soluble expression of the dual affinity tagged enzyme as MBP-fusion protein in Escherichia coli strain BL21(DE3), method evaluation
overexpressed both as native and as fusion protein with a His6 tag at the C- or the N-terminus in human embryonic kidney-293 cells expressing the large T-antigen of simian virus 40 (HEK-293T cells)
overexpressed both as native and as fusion proteins with a His6 tag at the C- or the N-terminus in human embryonic kidney-293 cells expressing the large T-antigen of simian virus 40 (HEK-293T cells); furthermore expressed as fusion protein in rat embryonal cortical neurons and in Chinese-hamster ovary cells
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expression HEK-293 cell
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medicine
patients with high levels of tumoral N-acetyl-L-aspartate and its biosynthetic enzyme, aspartate N-acetyltransferase (NAT8L), have worse overall survival than patients with low levels of N-acetyl-L-aspartate and NAT8L. The overall survival duration of patients with higher-than-median N-acetyl-L-aspartate levels (3.6 years) is lower than that of patients with lower-than-median N-acetyl-L-aspartate levels (5.1 years). High NAT8L gene expression in other cancers (melanoma, renal cell, breast, colon, and uterine cancers) is associated with worse overall survival. NAT8L silencing reduces cancer cell viability and proliferation. In orthotopic mouse models (ovarian cancer and melanoma), NAT8L silencing reduces tumor growth statistically significantly
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Goldstein, F.B.
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N-acetylaspartate pathway is nutrient responsive and coordinates lipid and energy metabolism in brown adipocytes
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2019
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Design and optimization of aspartate N-acetyltransferase inhibitors for the potential treatment of Canavan disease
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