Information on EC 6.3.2.41 - N-acetylaspartylglutamate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.3.2.41
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RECOMMENDED NAME
GeneOntology No.
N-acetylaspartylglutamate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
N-acetyl-L-aspartate:L-glutamate ligase (ADP, N-acetyl-L-aspartyl-L-glutamate-forming)
The enzyme, found in animals, produces the neurotransmitter N-acetyl-L-aspartyl-L-glutamate. One isoform also has the activity of EC 6.3.1.17, beta-citrylglutamate synthase [2], while another isoform has the activity of EC 6.3.2.42, N-acetylaspartylglutamylglutamate synthase [3].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + N-acetyl-L-aspartate + citrate
?
show the reaction diagram
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?
ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
stimulates; stimulates; the enzyme is markedly stimulated by dithiothreitol, which increases the activity by about 5fold
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0096 - 0.065
ATP
0.87
citrate
at pH 8.0 and 37C
0.73 - 0.88
L-glutamate
1.48 - 4.59
N-acetyl-L-aspartate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6 - 3
N-acetyl-L-aspartate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.09
pH 8.0, 30C, formation of N-acetyl-L-aspartyl-L-glutamate
1.4
pH 8.0, 30C, formation of N-acetyl-L-aspartyl-L-glutamate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at; assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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cerebellar glia cell
Manually annotated by BRENDA team
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very low expression
Manually annotated by BRENDA team
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cerebellar neuron
Manually annotated by BRENDA team
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very low expression
Manually annotated by BRENDA team
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very low expression
Manually annotated by BRENDA team
additional information
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the enzyme is undetectable in liver
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
x * 43000, contains at least six subunits, SDS-PAGE; x * 43000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, and S-200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as FLAG epitope-tagged protein in HEK-293T and CHO-K1 cells
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expressed in bacteria or HEK293T cells; expressed in Escherichia coli; expressed in Escherichia coli BL21(DE3)pLysS cells and in HEK-293T cells
expressed in CHO-K1 and HEK-293T cells
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