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Information on EC 2.3.1.17 - aspartate N-acetyltransferase and Organism(s) Mus musculus and UniProt Accession Q3UGX3

for references in articles please use BRENDA:EC2.3.1.17
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This record set is specific for:
Mus musculus
UNIPROT: Q3UGX3 not found.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
nat8l, aspartate n-acetyltransferase, l-aspartate n-acetyltransferase, aspartate acetyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyltransferase, aspartate
-
-
-
-
aspartate acetyltransferase
-
-
-
-
aspartate N-acetyltransferase
-
-
aspartic acetylase
-
-
-
-
L-aspartate N-acetyltransferase
-
-
-
-
NAT8L
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-aspartate N-acetyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9029-99-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
show the reaction diagram
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamic acid
show the reaction diagram
less than 1% of the activity with L-aspartate
-
-
?
acetyl-CoA + glutamate
CoA + N-acetylglutamate
show the reaction diagram
-
[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-aspartic acid
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutamate
-
Glutamate is a competitive inhibitor. No inhibition is observed with other amino acids, indicating that the enzyme is specific.
N-acetyl-L-aspartate
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009 - 0.013
acetyl-CoA
5
glutamate
-
-
0.09
L-aspartate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.1
glutamate
-
-
0.56
N-acetyl-L-aspartate
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
In PCR, no specific amplification was observed with liver, kidney, lung, skeletal muscle, testis and heart cDNA of mice.
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
not in mitochondria
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NAT8L_MOUSE
299
1
32777
Swiss-Prot
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 33000-35000, SDS-PAGE of recombinant His-tagged protein
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression HEK-293 cell
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Homo sapiens (Q8N9F0), Homo sapiens, Mus musculus
Manually annotated by BRENDA team
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
Homo sapiens (Q8N9F0), Homo sapiens, Mus musculus (Q3UGX3)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team