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Enzyme Nomenclature
Information on EC 2.3.1.17 - aspartate N-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.17
Word Map on EC 2.3.1.17
- 2.3.1.17
- n-acetylaspartate
- aspartoacylase
- canavan
-
myelin
- leukodystrophy
- n-acetyl-l-aspartate
- methamphetamine
-
8-like
- oligodendrocytes
-
spongiform
-
neuron-specific
- n-acetylaspartylglutamate
-
atlas
- naags
-
meth-induced
-
methamphetamine-induced
-
meth
-
accumbens
-
hyperlocomotion
-
locomotor
-
dysmyelination
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.3.1.17
-
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RECOMMENDED NAME
GeneOntology No.
aspartate N-acetyltransferase
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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
Acyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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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 + 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
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highly specific
-
?
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
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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
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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
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-
-
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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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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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INHIBITORS
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-methyl-N-nonanoyl-beta-D-glucosylamine
-
Mega-9, high inhibition at CMC concentration
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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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
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pH 7.4, temperature not specified in the publication
0.8 - 1.06
acetyl-CoA
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pH 7.0, 37°C, slightly varying Km depending on source organelle
0.166 - 0.174
L-aspartate
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pH 7.0, 37°C, slightly varying Km depending on source organelle
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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
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
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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
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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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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.
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
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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
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membrane-associated, the enzyme contains a membrane anchor region
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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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SUBUNITS
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
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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
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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
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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)
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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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ENGINEERING
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
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
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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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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.17)
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