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Information on EC 3.5.1.15 - aspartoacylase and Organism(s) Mus musculus and UniProt Accession Q8R3P0
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3.5.1.15 aspartoacylaseSpecify your search results
Word Map
- 3.5.1.15
- canavan
- n-acetylaspartate
- leukodystrophy
- matter
- myelin
- oligodendrocyte
-
spongy
- n-acetyl-l-aspartate
-
spongiform
- macrocephaly
- tremor
-
ashkenazi
-
jewish
-
non-jewish
-
dysmyelination
- nutrition
- medicine
- pharmacology
- n-acetylaspartylglutamate
- triacetate
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aspartoacylase, human aspa, haspa, aspartoacylase ii, murine aspartoacylase, aminoacylase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl-aspartic deaminase
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-
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Acylase II
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-
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Aminoacylase II
-
-
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N-Acetyl-L-aspartate amidohydrolase
N-Acetylaspartate amidohydrolase
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-
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N-Acetyl-L-aspartate amidohydrolase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of amide bond
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-
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
N-acyl-L-aspartate amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9031-86-1
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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
N-acetylalanine + H2O
acetate + alanine
poor substrate, 0.1% of the activity towards N-acetyl-aspartate
-
-
?
N-acetylarginine + H2O
acetate + arginine
poor substrate, 0.1% of the activity towards N-acetyl-aspartate
-
-
?
N-acetylasparagine + H2O
acetate + aspartate + NH3
10% of the activity towards N-acetylaspartate
product is aspartate, not asparagine, indicating the enzyme catalyzes deacetylation as well as hydrolysis of the beta acid amide
?
N-acetylcysteine + H2O
acetate + cysteine
poor substrate, 0.1% of the activity towards N-acetyl-aspartate
-
-
?
N-acetylglutamate + H2O
acetate + glutamate
poor substrate, 0.1% of the activity towards N-acetyl-aspartate
-
-
?
N-acetylglutamine + H2O
acetate + glutamine
poor substrate, 0.1% of the activity towards N-acetyl-aspartate
-
-
?
N-acetylleucine + H2O
acetate + leucine
poor substrate, 0.1% of the activity towards N-acetyl-aspartate
-
-
?
N-acetyllysine + H2O
acetate + lysine
poor substrate, 0.1% of the activity towards N-acetyl-aspartate
-
-
?
N-acetylmethionine + H2O
acetate + methionine
poor substrate, 0.1% of the activity towards N-acetyl-aspartate
-
-
?
N-acetylphenylalanine + H2O
acetate + phenylalanine
poor substrate, 0.1% of the activity towards N-acetyl-aspartate
-
-
?
N-acetylproline + H2O
acetate + proline
poor substrate, 0.1% of the activity towards N-acetyl-aspartate
-
-
?
N-acetyltyrosine + H2O
acetate + tyrosine
poor substrate, 0.1% of the activity towards N-acetyl-aspartate
-
-
?
additional information
?
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the enzyme functions in concert with the plasma membrane transporter NaDC3, that specifically transports N-acetylaspartic acid into the cell
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?
N-acetylaspartic acid + H2O
L-asparatate + acetate
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enzyme deficiency, due to mutations of aspartoacylase II, causes the Canavan disease, which is associated with optical neuropathy
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-
?
N-acetylaspartic acid + H2O
L-asparatate + acetate
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hydrolysis of N-acetylaspartic acid is important to maintain healthy neurons, the enzyme is upregulated in duodenum of obesity-induced diabetic mice, which might be responsible for diabetic neuropathy, overview
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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
additional information
?
-
-
the enzyme functions in concert with the plasma membrane transporter NaDC3, that specifically transports N-acetylaspartic acid into the cell
-
-
?
N-acetylaspartic acid + H2O
L-asparatate + acetate
-
enzyme deficiency, due to mutations of aspartoacylase II, causes the Canavan disease, which is associated with optical neuropathy
-
-
?
N-acetylaspartic acid + H2O
L-asparatate + acetate
-
hydrolysis of N-acetylaspartic acid is important to maintain healthy neurons, the enzyme is upregulated in duodenum of obesity-induced diabetic mice, which might be responsible for diabetic neuropathy, overview
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
upregulation of aspartoacylase activity in the duodenum of obesity induced diabetes mouse
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3 - 0.5
N-acyl-aspartic acid
recombinant enzyme, purified from bacteria
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in situ immunostaining of the enzyme in duodenum of healthy and diabetic mice, overview
additional information
-
co-localization with plasma membrane transporter NaDC3 in the optic system, in situ hybridization, overview
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expression of full-length ASPA at embryonic day 12.5, when oligodendrocyte progenitors first appear during development
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ASPA is an oligodendrocyte-specific enzyme, most active in immature oligodendrocytes
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
synthesis and storage in neuron, hydrolytic cleavage in the oligodendrocyte
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
mutations in gene Aspa lead to Canavan disease characterized by defective synthesis of myelin. Loss of expression of aspartoacylase does not lead to macrophage polarization
metabolism
enzyme substrate N-acetylaspartate is the second-most abundant metabolite in the brain, being produced by neurons and used by oligodendrocytes to coordinate their differentiation, energy production, and lipid synthesis
physiological function
Aspa might be relevant to the loss of viable macrophages in the peritoneum, transcription factor Gata6 regulates aspartoacylase expression in resident peritoneal macrophages and controls their survival, perturbed metabolic regulator aspartoacylase facilitates generation of acetyl CoA, gene expression profiling and phenotype, overview. Mutant mice lacking functional Aspa phenocopy the higher propensity to death leading to a contraction of resident peritoneal macrophages
physiological function
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aspartoacylase activity supports adenosine triphosphate synthesis in oligodendrocytes during hypoglycemia in vitro. The loss of enzyme function during the early stages of postnatal development significantly compromises oligodendrocyte oxidative integrity
additional information
-
lack of aspartoacylase activity disrupts survival and differentiation of neural progenitors and oligodendrocytes in a mouse model of Canavan disease. ASPA knockout leads to degeneration of white matter
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). ACY2_MOUSE
312
0
35345
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Gata6flox/flox mice on a mixed 129S1/SvImJ and CD-1 background are bred with Lyz2-Cre+/- on a C57BL/6 background to yield Cre+/-Gata6-Mac mice and Cre-/- Gata6flox/flox littermate control mice. Nur7 mice bearing mutant Aspa alleles are on a C57BL/6J background and compared with C57BL/6J mice
additional information
-
knockout of aspartoacylase activity leads to sponginess and loss of white matter in Canavan disease, and to increased expression/activity of cdk2, NCAM, nestin, vimentin, and NG2. Differentiation of neuronal progenitor cells is arrested, phenotype, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene identified with human cDNA, cloned into a thioredoxin fusion vector and overexpressed in bacteria
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is decreased during the early stages of postnatal development
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goldstein, F.B.
Amidohydrolases of brain; enzymatic hydrolysis of N-acetyl-L-aspartate and other N-acyl-L-amino acids
J. Neurochem.
26
45-49
1976
Bos taurus, Columba sp., Felis catus, Macaca iris, Macaca mulatta, Mesocricetus auratus, Mus musculus, no activity in Cavia porcellus, Oryctolagus cuniculus, Rattus norvegicus, Rattus norvegicus Sprague Dawley, Sus scrofa
Namboodiri, M.A.A.; Corigliano-Murphy, A.; Jiang, G.; Rollag, M.; Provencio, I.
Murine aspartoacylase: cloning, expression and comparison with the human enzyme
Mol. Brain Res.
77
285-289
2000
Bos taurus, Homo sapiens, Mus musculus (Q8R3P0), Mus musculus, Prochlorococcus marinus
Surendran, S.; Matalon, R.; Tyring, S.K.
Upregulation of aspartoacylase activity in the duodenum of obesity induced diabetes mouse: implications on diabetic neuropathy
Biochem. Biophys. Res. Commun.
345
973-975
2006
Mus musculus
George, R.L.; Huang, W.; Naggar, H.A.; Smith, S.B.; Ganapathy, V.
Transport of N-acetylaspartate via murine sodium/dicarboxylate cotransporter NaDC3 and expression of this transporter and aspartoacylase II in ocular tissues in mouse
Biochim. Biophys. Acta
1690
63-69
2004
Mus musculus
Wang, J.; Matalon, R.; Bhatia, G.; Wu, G.; Li, H.; Liu, T.; Lu, Z.H.; Ledeen, R.W.
Bimodal occurrence of aspartoacylase in myelin and cytosol of brain
J. Neurochem.
101
448-457
2007
Mus musculus
Kumar, S.; Biancotti, J.C.; Matalon, R.; de Vellis, J.
Lack of aspartoacylase activity disrupts survival and differentiation of neural progenitors and oligodendrocytes in a mouse model of Canavan disease
J. Neurosci. Res.
87
3415-3427
2009
Mus musculus
Francis, J.S.; Strande, L.; Markov, V.; Leone, P.
Aspartoacylase supports oxidative energy metabolism during myelination
J. Cereb. Blood Flow Metab.
32
1725-1736
2012
Mus musculus
Gautier, E.; Ivanov, S.; Williams, J.; Huang, S.; Marcelin, G.; Fairfax, K.; Wang, P.; Francis, J.; Leone, P.; Wilson, D.; Artyomov, M.; Pearce, E.; Randolph, G.
Gata6 regulates aspartoacylase expression in resident peritoneal macrophages and controls their survival
J. Exp. Med.
211
1525-1531
2014
Mus musculus (Q8R3P0)
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