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Information on EC 2.3.1.17 - aspartate N-acetyltransferase
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EC Tree
2.3.1.17 aspartate N-acetyltransferaseSpecify your search results
Word Map
- 2.3.1.17
- n-acetylaspartate
- aspartoacylase
- canavan
- n-acetyl-l-aspartate
- leukodystrophy
- oligodendrocytes
- methamphetamine
-
8-like
-
myelin
-
spongiform
-
lipolysis
- medicine
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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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ANAT
aspartate N-acetyltransferase
NAT
NAT8L
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-aspartate N-acetyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9029-99-6
-
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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
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-glutamate
CoA + N-acetyl-L-glutamate
reaction of EC 2.3.1.1
-
?
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
-
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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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
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutamate
-
Glutamate is a competitive inhibitor. No inhibition is observed with other amino acids, indicating that the enzyme is specific.
N-(2,6-dibromo-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
-
N-(2,6-dichloro-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
-
N-acetyl-(dimethyl)aspartyl-conjugated CoA
coenzyme A coupled to methylated N-acetyl aspartate, bisubstrate inhibitor
N-acetylaspartyl-conjugated CoA
coenzyme A coupled to N-acetyl aspartate, bisubstrate inhibitor
N-methyl-N-nonanoyl-beta-D-glucosylamine
Mega-9, high inhibition at CMC concentration
N-propionyl-(dimethyl)aspartyl-conjugated CoA
coenzyme A coupled to N-propionyl aspartate, bisubstrate inhibitor
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
Nervous System Diseases
Structure of the Brain N-Acetylaspartate Biosynthetic Enzyme NAT8L Revealed by Computer Modeling.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.8 - 1.06
acetyl-CoA
-
pH 7.0, 37°C, slightly varying Km depending on source organelle
0.166 - 0.174
L-aspartate
-
pH 7.0, 37°C, slightly varying Km depending on source organelle
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
recombinant enzyme, pH 7.4, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
membrane-associated, the enzyme contains a membrane anchor region
brenda
enzyme is present in both cytoplasm and mitochondria
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 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)
A0A1S2X6C5_SALSA
90
0
10091
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2K8W1D4_9GAMM
170
0
18387
TrEMBL
-
A0A482ZQH8_9GAMM
165
0
18299
TrEMBL
-
A0A076LLY5_9GAMM
167
0
18060
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression HEK-293 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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goldstein, F.B.
Biosynthesis of N-acetyl-L-aspartic acid
J. Biol. Chem.
234
2702-2706
1959
Rattus norvegicus
-
brenda
Knizley, H.Jr.
The enzymatic synthesis of N-acetyl-L-aspartic acid by a water-insoluble preparation of a cat brain acetone powder
J. Biol. Chem.
242
4619-4622
1967
Felis catus
brenda
Truckenmiller, M.E.; Namboodiri, M.A.A.; Brownstein, M.J.; Neale, J.H.
N-Acetylation of L-aspartate in the nervous system: differential distribution of a specific enzyme
J. Neurochem.
45
1658-1662
1985
Rattus norvegicus
brenda
Moreno, A.; Ross, B.D.; Bluml, S.
Direct determination of the N-acetyl-L-aspartate synthesis rate in the human brain by (13)C MRS and [1-(13)C]glucose infusion
J. Neurochem.
77
347-350
2001
Homo sapiens
brenda
Lu, Z.H.; Chakraborty, G.; Ledeen, R.W.; Yahya, D.; Wu, G.
N-Acetylaspartate synthase is bimodally expressed in microsomes and mitochondria of brain
Brain Res. Mol. Brain Res.
122
71-78
2004
Rattus norvegicus
brenda
Madhavarao, C.N.; Chinopoulos, C.; Chandrasekaran, K.; Namboodiri, M.A.
Characterization of the N-acetylaspartate biosynthetic enzyme from rat brain
J. Neurochem.
86
824-835
2003
Rattus norvegicus
brenda
Wiame, E.; Tyteca, D.; Pierrot, N.; Collard, F.; Amyere, M.; Noel, G.; Desmedt, J.; Nassogne, M.C.; Vikkula, M.; Octave, J.N.; Vincent, M.F.; Courtoy, P.J.; Boltshauser, E.; van Schaftingen, E.
Molecular identification of aspartate N-acetyltransferase and its mutation in hypoacetylaspartia
Biochem. J.
425
127-136
2010
Danio rerio, Mus musculus, Homo sapiens (Q8N9F0), Homo sapiens
brenda
Tahay, G.; Wiame, E.; Tyteca, D.; Courtoy, P.J.; Van Schaftingen, E.
Determinants of the enzymatic activity and the subcellular localization of aspartate N-acetyltransferase
Biochem. J.
441
105-112
2012
Homo sapiens (Q8N9F0)
brenda
Ariyannur, P.S.; Moffett, J.R.; Manickam, P.; Pattabiraman, N.; Arun, P.; Nitta, A.; Nabeshima, T.; Madhavarao, C.N.; Namboodiri, A.M.
Methamphetamine-induced neuronal protein NAT8L is the NAA biosynthetic enzyme: implications for specialized acetyl coenzyme A metabolism in the CNS
Brain Res.
1335
1-13
2010
Mus musculus (Q3UGX3), Homo sapiens (Q8N9F0), Homo sapiens
brenda
Wang, Q.; Zhao, M.; Parungao, G.G.; Viola, R.E.
Purification and characterization of aspartate N-acetyltransferase: a critical enzyme in brain metabolism
Protein Expr. Purif.
119
11-18
2016
Homo sapiens (Q8N9F0), Homo sapiens
brenda
Huber, K.; Hofer, D.C.; Trefely, S.; Pelzmann, H.J.; Madreiter-Sokolowski, C.; Duta-Mare, M.; Schlager, S.; Trausinger, G.; Stryeck, S.; Graier, W.F.; Kolb, D.; Magnes, C.; Snyder, N.W.; Prokesch, A.; Kratky, D.; Madl, T.; Wellen, K.E.; Bogner-Strauss, J.G.
N-acetylaspartate pathway is nutrient responsive and coordinates lipid and energy metabolism in brown adipocytes
Biochim. Biophys. Acta
1866
337-348
2019
Mus musculus (Q3UGX3)
brenda
Thangavelu, B.; Mutthamsetty, V.; Wang, Q.; Viola, R.E.
Design and optimization of aspartate N-acetyltransferase inhibitors for the potential treatment of Canavan disease
Bioorg. Med. Chem.
25
870-885
2017
Homo sapiens (Q8N9F0), Homo sapiens
brenda
Mutthamsetty, V.; Dahal, G.P.; Wang, Q.; Viola, R.E.
Development of bisubstrate analog inhibitors of aspartate N-acetyltransferase, a critical brain enzyme
Chem. Biol. Drug Des.
95
48-57
2020
Homo sapiens (Q8N9F0), Homo sapiens
brenda
Zand, B.; Previs, R.A.; Zacharias, N.M.; Rupaimoole, R.; Mitamura, T.; Nagaraja, A.S.; Guindani, M.; Dalton, H.J.; Yang, L.; Baddour, J.; Achreja, A.; Hu, W.; Pecot, C.V.; Ivan, C.; Wu, S.Y.; McCullough, C.R.; Gharpure, K.M.; Shoshan, E.; Pradeep, S.; Mangala, L.S.; Rodriguez-Aguayo, C.; Wang, Y.; Nick, A.M.
Role of increased N-acetylaspartate levels in cancer
J. Natl. Cancer Inst.
108
djv426
2016
Homo sapiens (Q8N9F0), Homo sapiens
brenda
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