Information on EC 3.5.1.15 - aspartoacylase

754252, 754806, 755390

Substrates: -
Products: -

N-acetyl-L-aspartate + H2O

aspartate + acetate

Substrates: enzyme mutations cause the Canavan disease
Products: -

N-acetyl-L-aspartate + H2O

aspartate + acetate

Substrates: deficiency in enzyme activity leads to spongiform degeneration of the white matter of the brain and is the established cause of Canavan disease
Products: -

N-acetyl-L-aspartate + H2O

aspartate + acetate

Substrates: deficiency in enzyme activity leads to spongiform degeneration of the white matter of the brain and is the established cause of Canavan disease
Products: -

N-acetyl-L-aspartate + H2O

L-aspartate + acetate

Substrates: malfunction of the enzyme causes Canavan disease
Products: -

N-acetyl-L-aspartate + H2O

L-aspartate + acetate

Substrates: -
Products: -

N-acetyl-L-aspartate + H2O

L-aspartate + acetate

720276

Substrates: -
Products: -

N-acetyl-L-aspartate + H2O

L-aspartate + acetate

Substrates: -
Products: -

N-acetyl-L-aspartate + H2O

L-aspartate + acetate

Substrates: -
Products: -

N-acetyl-L-aspartate + H2O

L-aspartate + acetate

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

208998, 209001

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

208998, 209000

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Macaca iris

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

208998, 208999, 209000, 209001, 209002, 209007, 209008

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

209002

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetylasparagine + H2O

acetate + aspartate + NH3

Substrates: 10% of the activity towards N-acetylaspartate
Products: product is aspartate, not asparagine, indicating the enzyme catalyzes deacetylation as well as hydrolysis of the beta acid amide

N-acetylasparagine + H2O

acetate + aspartate + NH3

Substrates: 10% of the activity towards N-acetylaspartate
Products: product is aspartate, not asparagine, indicating the enzyme catalyzes deacetylation as well as hydrolysis of the beta acid amide

N-acetylaspartate + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acetylaspartate + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acetylaspartate + H2O

aspartate + acetate

Substrates: -
Products: -

N-acetylaspartate + H2O

aspartate + acetate

Substrates: -
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: enzyme mutations cause the Canavan disease
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: enzyme deficiency causes the Canavan disease, an autosomal-recessive neurodegenerative disorder
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

667727, 668640

Substrates: -
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: 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
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: enzyme deficiency, due to mutations of aspartoacylase II, causes the Canavan disease, which is associated with optical neuropathy
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

667443, 667777

Substrates: -
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: enzyme mutations cause the Canavan disease
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: -
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: the enzyme is involved in negative regulation of brain-derived neurotrophic factor, BDNF, and timing of postnatal oligodendrogenesis, overview
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: restoration of deficient enzyme activity by enzyme expression in CNS neurons does not ameliorate motor deficits and demyelination in a model of Canavan disease, which is caused by elevated levels of N-acetylaspartic acid, NAA, neuronal expression of ASPA can compensate for NAA-mediated neuronal hyperexcitation, but not for oligodebdrocyte dysfunciton, overview
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: -
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: -
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

208998, 209001

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

208998, 209000

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Macaca iris

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

208998, 208999, 209000, 209001, 209002, 209007, 209008

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

209001, 209002

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl L-aspartic acid + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acyl-L-aspartate + H2O

a carboxylate + L-aspartate

769947, 770137

Substrates: -
Products: -

N-acyl-L-aspartate + H2O

a carboxylate + L-aspartate

Substrates: -
Products: -

additional information

Substrates: the enzyme functions in concert with the plasma membrane transporter NaDC3, that specifically transports N-acetylaspartic acid into the cell
Products: -

additional information

Substrates: N-methyl aspartic acid, N-carbamoyl aspartic acid and N-glycyl aspartic acids are no substrates
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

N-acetyl-L-aspartate + H2O

acetate + L-aspartate

5 entries

N-acetyl-L-aspartate + H2O

aspartate + acetate

N-acetyl-L-aspartate + H2O

L-aspartate + acetate

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

17 entries

N-acetylaspartate + H2O

acetate + L-aspartate

N-acetylaspartate + H2O

aspartate + acetate

N-acetylaspartate + H2O

L-aspartate + acetate

Substrates: aspartocylase deficiency results in elevated levels of substrate, brain edema and dysmyelination
Products: -

N-acetylaspartic acid + H2O

aspartate + acetate

681846

Substrates: enzyme mutations cause the Canavan disease and type 2 diabetes
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

8 entries

N-acyl-L-aspartate + H2O

a carboxylate + L-aspartate

additional information

Substrates: the enzyme functions in concert with the plasma membrane transporter NaDC3, that specifically transports N-acetylaspartic acid into the cell
Products: -

N-acetyl-L-aspartate + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acetyl-L-aspartate + H2O

acetate + L-aspartate

754252

Substrates: the enzyme hydrolyzes one of the most abundant amino acid derivatives in the brain, N-acetyl-aspartate
Products: -

N-acetyl-L-aspartate + H2O

acetate + L-aspartate

754480, 754618

Substrates: -
Products: -

N-acetyl-L-aspartate + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acetyl-L-aspartate + H2O

acetate + L-aspartate

N-acetyl-L-aspartate + H2O

aspartate + acetate

Substrates: enzyme mutations cause the Canavan disease
Products: -

N-acetyl-L-aspartate + H2O

aspartate + acetate

Substrates: deficiency in enzyme activity leads to spongiform degeneration of the white matter of the brain and is the established cause of Canavan disease
Products: -

N-acetyl-L-aspartate + H2O

aspartate + acetate

Substrates: deficiency in enzyme activity leads to spongiform degeneration of the white matter of the brain and is the established cause of Canavan disease
Products: -

N-acetyl-L-aspartate + H2O

L-aspartate + acetate

Substrates: malfunction of the enzyme causes Canavan disease
Products: -

N-acetyl-L-aspartate + H2O

L-aspartate + acetate

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

208998, 209001

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

208998, 209000

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Macaca iris

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

208998, 208999, 209000, 209001, 209002, 209007, 209008

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

209002

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetyl-L-aspartic acid + H2O

acetate + aspartic acid

Substrates: -
Products: -

N-acetylaspartate + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acetylaspartate + H2O

acetate + L-aspartate

Substrates: -
Products: -

N-acetylaspartate + H2O

aspartate + acetate

Substrates: -
Products: -

N-acetylaspartate + H2O

aspartate + acetate

Substrates: -
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: enzyme mutations cause the Canavan disease
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: enzyme deficiency causes the Canavan disease, an autosomal-recessive neurodegenerative disorder
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: enzyme deficiency, due to mutations of aspartoacylase II, causes the Canavan disease, which is associated with optical neuropathy
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: enzyme mutations cause the Canavan disease
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: -
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

Substrates: the enzyme is involved in negative regulation of brain-derived neurotrophic factor, BDNF, and timing of postnatal oligodendrogenesis, overview
Products: -

N-acetylaspartic acid + H2O

L-asparatate + acetate

N-acyl-L-aspartate + H2O

a carboxylate + L-aspartate

769947, 770137

Substrates: -
Products: -

N-acyl-L-aspartate + H2O

a carboxylate + L-aspartate

Substrates: -
Products: -

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Ca2+

stimulates activity 20-40%

Mg2+

stimulates activity 20-40%

Mn2+

stimulates activity 20-40%, above 0.1 mM inhibition

Zn2+

13 entries

Zn2+

stimulates activity 20-40%, above 0.1 mM inhibition

Zn2+

required for activity, spectroscopical determination of metal content, the enzyme contains about 1 Zn2+ per enzyme subunit

Zn2+

metallopeptidase, the enzyme contains the conserved H21XXE24(91aa)H116 motif, ligand binding by His21, Glu24, and His116, molecular modeling

Zn2+

essential for activity

Zn2+

one zinc ion per monomer

Zn2+

two zinc ions per enzyme subunit

Zn2+

necessary for activity, coordinated by residues His-21, Glu-24, and His-116 and a phosphate

Zn2+

contains zinc

Zn2+

the enzyme binds one zinc ion per monomer

Zn2+

Zn2+-dependent enzyme

754252

Zn2+

zinc-dependent enzyme

Zn2+

zinc-dependent enzyme. Zn2+ coordination region: His21, Glu24 and His116

Zn2+

necessary for activity

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

aspartic acid

0.002 M, 20-25% inhibition

diisopropyl fluorophosphate

glutamic acid

0.002 M, 20-25% inhibition

Glycyl-L-aspartate

methylphosphonamidate

N-acetyl-aspartate

decrease of the reaction rate at high substrate concentrations. Binding of N-acetyl-aspartate to the allosteric site induces significant rigidity to the protein loops with the amino acid side chains forming gates to the enzyme active site

N-acetyl-L-aspartate

N-acetylaspartic acid

substrate inhibition at concentration above 0.2 mM

N-carbobenzoxy-D-aspartic acid

N-ethylmaleimide

N-phosphonomethyl-L-aspartate

N-tert-butoxycarbonyl-D-aspartic acid-beta-benzyl ester

p-hydroxymercuribenzoate

N-acetyl-L-aspartate

at low N-acetyl-L-aspartate concentrations, sigmoidal shape of kinetic curve is observed, followed by typicalrate growth of the enzyme-catalyzed reaction, whereas at high concentrations of N-acetyl-L-aspartate self-inhibition takes place. N-Acetylaspartate acts as activator at low concentrations, substrate at moderate concentrations, and inhibitor at high concentrations

754480

N-acetyl-L-aspartate

substrate inhibition at high concentration

show all columns Go to Activating Compound Search

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

chloroacetylamino acids

dithiothreitol

enhances activity

N-acetylaspartate

N-acetylaspartate acts as activator at low concentrations, substrate at moderate concentrations, and inhibitor at high concentrations

NP-40

enhances activity

Triton X-100

Tween-20

enhances activity

additional information

upregulation of aspartoacylase activity in the duodenum of obesity induced diabetes mouse

chloroacetylamino acids

chloroacetylamino acids

chloroacetylamino acids

chloroacetylamino acids

Macaca iris

chloroacetylamino acids

chloroacetylamino acids

chloroacetylamino acids

chloroacetylamino acids

chloroacetylamino acids

chloroacetylamino acids

Triton X-100

increases activity of the enzyme

209001, 209005

Triton X-100

increases activity of the enzyme

Triton X-100

increases activity of the enzyme

Triton X-100

Macaca iris

increases activity of the enzyme

Triton X-100

increases activity of the enzyme

Triton X-100

increases activity of the enzyme

Triton X-100

increases activity of the enzyme

Triton X-100

increases activity of the enzyme

Triton X-100

increases activity of the enzyme

Triton X-100

increases activity of the enzyme

Show Disease (243 entries)

Go to Disease Search

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.36

N-acetyl-L-aspartate

pH and temperature not specified in the publication

0.1

N-acetyl-L-aspartic acid

0.163 - 5

N-acetylaspartate

0.12 - 0.36

N-acetylaspartic acid

0.2

N-acyl L-aspartic acid

0.3 - 0.5

N-acyl-aspartic acid

recombinant enzyme, purified from bacteria

0.85 - 5.1

N-acyl-L-aspartic acid

0.59

N-Chloroacetyl-L-aspartate

pH and temperature not specified in the publication

0.23

N-dichloroacetyl-L-aspartate

pH and temperature not specified in the publication

0.95

N-formyl-L-aspartate

pH and temperature not specified in the publication

0.21

N-trifluoroacetyl-L-aspartate

pH and temperature not specified in the publication

0.15 - 0.21

N-trifluoroacetylaspartic acid

additional information

the enzyme shows sigmoidal behaviour and cooperative substrate bindng at low substrate concentration of 0.05-0.2 mM

0.1

N-acetyl-L-aspartic acid

0.1

N-acetyl-L-aspartic acid

0.163

N-acetylaspartate

1.69

N-acetylaspartate

ASPA isolated from cytosol

3.7 - 5

N-acetylaspartate

ASPA isolated from myelin

0.12

N-acetylaspartic acid

pH 7.2, recombinant Pichia pastoris-expressed enzyme

0.2

N-acetylaspartic acid

pH 7.4, 37°C, recombinant wild-type enzyme

0.22

N-acetylaspartic acid

pH 7.4, 37°C, recombinant mutant E178D

0.36

N-acetylaspartic acid

pH 7.2, recombinant Escherichia coli-expressed enzyme

0.2

N-acyl L-aspartic acid

209000, 209001

0.2

N-acyl L-aspartic acid

brain enzyme

209000, 209001

0.85

N-acyl-L-aspartic acid

1.8 - 2

N-acyl-L-aspartic acid

209008

5.1

N-acyl-L-aspartic acid

0.15

N-trifluoroacetylaspartic acid

pH 7.2, recombinant Pichia pastoris-expressed enzyme

0.21

N-trifluoroacetylaspartic acid

pH 7.2, recombinant Escherichia coli-expressed enzyme

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.083

N-acetyl-L-aspartate

pH and temperature not specified in the publication

37.5

N-acetylaspartate

0.083 - 14.22

N-acetylaspartic acid

5 entries

0.62

N-Chloroacetyl-L-aspartate

pH and temperature not specified in the publication

0.77

N-dichloroacetyl-L-aspartate

pH and temperature not specified in the publication

0.25

N-formyl-L-aspartate

pH and temperature not specified in the publication

1.2

N-trifluoroacetyl-L-aspartate

pH and temperature not specified in the publication

1.2 - 116

N-trifluoroacetylaspartic acid

0.083

N-acetylaspartic acid

pH 7.2, recombinant Escherichia coli-expressed enzyme

0.52

N-acetylaspartic acid

pH 7.4, 37°C, recombinant wild-type enzyme

1.48

N-acetylaspartic acid

pH 7.4, 37°C, recombinant mutant E178D

12.7

N-acetylaspartic acid

pH 7.2, recombinant Pichia pastoris-expressed enzyme

14.22

N-acetylaspartic acid

pH 7.4, 37°C, recombinant wild-type enzyme

1.2

N-trifluoroacetylaspartic acid

pH 7.2, recombinant Escherichia coli-expressed enzyme

116

N-trifluoroacetylaspartic acid

pH 7.2, recombinant Pichia pastoris-expressed enzyme

show all columns Go to kcat/KM Value Search

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.23

N-acetyl-L-aspartate

pH and temperature not specified in the publication

N-Chloroacetyl-L-aspartate

pH and temperature not specified in the publication

3.4

N-dichloroacetyl-L-aspartate

pH and temperature not specified in the publication

0.26

N-formyl-L-aspartate

pH and temperature not specified in the publication

5.8

N-trifluoroacetyl-L-aspartate

pH and temperature not specified in the publication

show all columns Go to Ki Value Search

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.3

N-phosphonomethyl-L-aspartate

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.019 - 0.02

0.25

0.29

0.3

0.42

0.45

0.47

0.98

1557

purified recombinant wild-type enzyme

300

purified recombinant mutant E178D

recombinant enzyme expressed from Escherichia coli, pH and temperature not specified in the publication

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

7.2

assay at

7.4

assay at

7.5 - 8.5

8.5

assay at

assay at

8.5

8.5

N-acetyl-L-aspartate as substrate

show all columns Go to pH Range Search

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

3 - 10

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

assay at

assay at

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

bovine

brenda

goldfish

brenda

guinea pig, strain Hartley

brenda

pigeon

brenda

cat

brenda

Macaca iris

java monkey

brenda

rhesus monkey

brenda

hamster

brenda

no activity in Cavia porcellus

rabbit

brenda

Prochlorococcus marinus

brenda

6 entries

209001, 209002

brenda

brenda

pig

brenda

brenda

chicken, no activity in chick embryos up to 14 days

brenda

667727, 668640, 670342

brenda

678338, 678979

Uniprot

brenda

brenda

Uniprot

brenda

brenda

Uniprot

brenda

brenda

Uniprot

brenda

brenda

754250, 754252, 754480, 754618, 754806, 755390, 769947, 770137, 774656, 775283

Uniprot

brenda

gene acy2 or ASPA

Uniprot

brenda

gene ASPA

733213, 733353

Uniprot

brenda

human

brenda

667443, 667777, 681524, 712823, 720100

brenda

gene ASPA

Uniprot

brenda

mouse

brenda

mouse

Uniprot

brenda

no activity in Cavia porcellus

guinea pig

brenda

no activity in Cavia porcellus

male albino

brenda

208999, 209000, 209001, 209002, 209007, 209008, 670342, 681846, 682568, 697037

brenda

Uniprot

brenda

female wild-type Kyoto-Wistar and tremor rats

Uniprot

brenda

male sprague-dawley rats

brenda

rat

brenda

Sprague-Dawley rat pups

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

amygdala

central nucleus of amygdala

brenda

31 entries

central nervous system

immunohistochemical localization analysis, high enzyme content in oligodendrocytes along with CC1, and in white matter, including the corpus callosum and the cerebellar white matter, less abundant enzyme content in grey matter, including cerebral cortex, descending neuronal fibers, and microglial cells, no enzyme in astroyctes and forebrain, overview

brenda

cerebral white matter

brenda

brenda

circular smooth muscle

brenda

in situ immunostaining of the enzyme in duodenum of healthy and diabetic mice, overview

brenda

eye

neuron-oligodendrocyte co-culture

ocular tissue, enzyme expression pattern

brenda

brenda

brenda

brenda

brenda

brenda

resident peritoneal

brenda

retinal pigment epithelium

neurons from wild-type embryos are co-cultured with oligodendrocytes prepared from either wild-type or tremor rats

brenda

brenda

brenda

brenda

brenda

brenda

brenda

additional information

brenda

brenda

brenda

brenda

brenda

brenda

209005, 209006, 209007, 667727, 668640, 679264

brenda

brenda

brenda

720276, 719318, 733353, 734698, 733213

brenda

brenda

brenda

most important site of aspartoacylase expression is the brain white matter

brenda

Macaca iris

brenda

brenda

brenda

brenda

brenda

brenda

expression of full-length ASPA at embryonic day 12.5, when oligodendrocyte progenitors first appear during development

brenda

brenda

brenda

brenda

208998, 208999, 209000, 209001, 209002

brenda

enzyme activity expressed only in oligodendrocytes

brenda

brenda

in situ hybridization, quantitative expression analysis in brain of wild-type and tremor rats, overview

brenda

brenda

brenda

brenda

209000, 209001, 209002

brenda

brenda

brenda

brenda

brenda

brenda

brenda

208998, 208999, 209000, 209002

brenda

abundant expression, especially in proximal tubules

brenda

brenda

brenda

209000, 209002, 209003, 288852

brenda

brenda

208998, 209000, 209002

brenda

liver

brenda

brenda

brenda

brenda

brenda

brenda

brenda

primary cortical neuron culture

brenda

brenda

ASPA is an oligodendrocyte-specific enzyme, most active in immature oligodendrocytes

brenda

brenda

high expression level

brenda

primary cell culture

brenda

brenda

additional information

co-localization with plasma membrane transporter NaDC3 in the optic system, in situ hybridization, overview

brenda

additional information

immunocolorimetric analysis of enzyme distribution in the brain, enzyme staining does not colocalize with CC1

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

brenda

brenda

additional information

brenda

brenda

brenda

209000, 209002, 209008, 670342

brenda

cytosol

brenda

brenda

brenda

additional information

synthesis and storage in neuron, hydrolytic cleavage in the oligodendrocyte

brenda

additional information

immunohistochemical localization analysis

brenda

additional information

subcellular localization analysis, the enzyme is active in cytoplasm and in nucleus

brenda

top hide

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

drug target

malfunction

9 entries

metabolism

physiological function

7 entries

additional information

drug target

Canavan disease is caused by a deficiency of the cytosolic aspartoacylase. Gene therapy is one of the more promising attempts at curing Canavan disease

drug target

increasing aspartoacylase to hydrolyze N-acyl-L-aspartate in central nucleus of amygdala is a common mechanism of gastroprotective effects against stress exerted by monoamine-based antidepressants

malfunction

the defect of aspartoacylase is the cause of Canavan disease

malfunction

mutations in the ASPA gene cause the Canavan disease, a fatal, childhood neurological disorder leading to catalytic deficiencies in the aspartoacylase (ASPA) enzyme and impaired N-acetyl-l-aspartic acid metabolism in the brain. The mutant enzymes each have overall structures similar to that of the wild-type ASPA enzyme, but with varying degrees of alterations that offer explanations for the respective loss of catalytic activity

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

malfunction

mutations in the ASPA gene cause the Canavan disease, a fatal, childhood neurological disorder leading to catalytic deficiencies in the aspartoacylase enzyme and impaired N-acetyl-L-aspartic acid metabolism in the brain. Enzyme replacement therapy can potentially be used to overcome these defects if a stable enzyme form that can gain access to the appropriate neural cells can be produced. Achieving the proper cellular targeting requires a modified form of aspartoacylase that can traverse the blood-brain barrier

malfunction

defects in the ASPA gene that codes for aspartoacylase causes a dramatic elevation in N-acetyl-L-aspartate1 levels, depletion of brain acetate, and leads to demyelination in neuronal cellsenzyme deficiency lead to a loss of activity and the symptoms of a fatal neurological disorder called Canavan disease

malfunction

mutations in the ASPA gene are associated with the development of Canavan disease (CD), leading to the deficiency of ASPA activity. Patients with CD are characterized by degeneration of the white matter of the brain

malfunction

catalytic deficiency of aspartoacylase is associated with several neurodegenerative disorders. The Canavan disease occurs most frequently in Ashkenazi Jews, with more than 96% of cases being associated with two point mutations: Glu285Ala and Tyr231X. The Canavan disease in other ethnic groups is associated with a more diverse range of mutations, the Ala305Glu replacement being the most frequent

malfunction

Canavan disease is caused by a deficiency of the cytosolic aspartoacylase. Canavan disease is an autosomal recessive and lethal neurological disorder, characterized by the spongy degeneration of the white matter in the brain

malfunction

aspartoacylase variants are linked to Canavan disease, a lethal neurological disorder

774656

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

metabolism

the enzyme plays an essential role in N-acetyl-aspartate catabolism

physiological function

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

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

aspartoacylase catalyzes the selective breakdown of N-acetyl-L-aspartate to release acetate in the brain. The acetate provides the building blocks required for fatty acid biosynthesis

physiological function

aspartoacylase is a key enzyme in the human central nervous system

physiological function

aspartoacylase promotes the process of tumour development and is associated with immune infiltrates in gastric cancer

769947

physiological function

the enzyme plays an essential role in N-acetyl-aspartate catabolism

physiological function

overexpressing aspartoacylase in central nucleus of amygdala alleviates stress ulcers

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

712823

additional information

homology modeling of the N117Q human aspartoacylase mutant using the native structure, PDB ID 2O53, as the template

additional information

homology modeling of the N117Q human aspartoacylase mutant using the native structure, PDB ID 2O53, as the template

additional information

enzyme deficiency is involved in Canavan disease and type 2 diabetes, high levels of N-acetylaspartic acid induce inflammatory agents TNFalpha, p38MAPK, iNOS, PKC, COX2 and ICAM3, and alters proteins levels and smooth muscle contractility, which contributes to the gastrointestinal disorder, overview

681846

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

Show AA Sequence and Transmembrane Helices (781 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.

Go to PDB and Structure Links Search

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PDB

SCOP

CATH

UNIPROT

ORGANISM

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

35000

36000

37000

determined by SDS-PAGE

38000

1 * 38000, SDS-PAGE

58000

SDS-PAGE

60000

recombinant mASPA fusion protein, SDS-PAGE

70000

dimer

73000

dynamic light scattering study

35000

immunoblot analysis

35000

x * 35000, SDS-PAGE

36000

about, gel filtration

36000

36000

x * 36000, recombinant enzyme, SDS-PAGE

36000

2 * 36000, recombinant enzyme, SDS-PAGE

show all columns Go to Subunit Search

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dimer

2 * 36000, recombinant enzyme, SDS-PAGE

homodimer

monomer

additional information

x * 36000, recombinant enzyme, SDS-PAGE

x * 35000, SDS-PAGE

homodimer

homodimer

extensive contact surface area between the two subunits

homodimer

682568, 755390, 770137

monomer

1 * 58000, SDS-PAGE, reducing conditions

monomer

1 * 38000, SDS-PAGE

additional information

quarternary structure, dynamic light scattering

additional information

the enzyme belongs to the carboxypeptidase metalloprotein family with the conserved H21XXE24(91aa)H116 motif

show all columns Go to Posttranslational Modification Search

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

glycoprotein

glycoprotein

carbohydrate determination by mass spectrometry, overview, the N-glycosylation site is N117

glycoprotein

presence of a glycan at Asn117 that plays an essential role in the stability and catalytic activity of mammalian aspartoacylase. Although recombinantly-expressed human aspartoacylase is not glycosylated, mass spectrometric analysis, overview. The recombinant enzyme is still fully functional and stable, even when produced from a bacterial expression system

Go to Crystallization (commentary) Search

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

2.8 angstrom resolution

crystallization in complex with inhibitor N-phosphonomethyl-L-aspartate, crystallization conditions: 50 mM sodium citrate (pH 6.0), 300 mM K2HPO4, and 15-19% polyethylene glycol 3350

resolution 2.8 Angstrom

resolution 1.8 angstrom

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

A305E

A57T

Canavan disease mutation, undetectable enzyme activity

C152R

0.5% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease

C152W

D249V

Canavan disease mutation, undetectable enzyme activity

D68A

Canavan disease mutation, undetectable enzyme activity

E178A

undetectable ASPA activity

E178D

E178Q

site-directed mutagenesis, inactive mutant

E214X

Canavan disease mutation, undetectable enzyme activity

E24A

E24D

E24G

E285A

E285A/P181T

32% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease

F295S

G274R

Canavan disease mutation, undetectable enzyme activity

H116A

H116G

putative zinc ion binding sites, undetectable ASPA activity

H21A

H21G

putative zinc ion binding sites, undetectable ASPA activity

H21P

Canavan disease mutation, undetectable enzyme activity

I143T

Canavan disease mutation, undetectable enzyme activity

I143V

the pathogenicity, stability, conservation, change in structural pattern, influence of the mutations on substrate binding of the crystallized mutations (K213E, Y231C, E285A, F295S, I143V and V186D) is compared. The binding affinity to the substrate, hydrogen bond interactions and metal interactions are found to be highly disturbed due to the mutant V186D than the mutant I143V

I143V/V186D

patients with severe form of Canavan disease (CD) have both missense mutations in the ASPA: c.427 A > G; p. I143V and c.557 T > A; p. V186D. Patient 1 harbors both mutations (p.I143V and p.V186D) in a heterozygous form together with four other mutations, and patient 2 has both mutations in homozygous form

I226T

mutant shows no catalytic activity, mutation may be responsible in homozygosis for the phenotype corresponding to Canavan disease.

K213E

M195R

Canavan disease mutation, undetectable enzyme activity

N117Q

P183H

Canavan disease mutation, undetectable enzyme activity

R63N

R71H

11% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease

R71N

undetectable ASPA activity

V186D

Y231C

Y88X

the mutation is associated with Canavan disease

additional information

6 entries

A305E

Canavan disease mutation, undetectable enzyme activity

A305E

10% activity compared to native enzyme form, mutation responsible for the Canavan disease

C152W

Canavan disease mutation, undetectable enzyme activity

C152W

1% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease

C152W

Canavan disease is a severe progressive neurodegenerative disorder that is characterized by swelling and spongy degeneration of brain white matter. The disease is genetically linked to polymorphisms in the aspartoacylase gene, including the substitution C152W. ASPA C152W is associated with greatly reduced protein levels in cells. A decreased steady state compared to wild-type aspartoacylase is found as a result of increased proteasomal degradation

775283

E178D

site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme

E178D

10% activity of native enzyme

E24A

site-directed mutagenesis, inactive mutant

E24A

no detectable activity

E24D

no detectable activity

E24D

putative zinc ion binding sites, undetectable ASPA activity

E24G

no protein expression

E24G

putative zinc ion binding sites, undetectable ASPA activity

E24G

Canavan disease mutation, undetectable enzyme activity

E285A

Canavan disease mutation, undetectable enzyme activity

E285A

a naturally occuring missense mutation associated with the Canavan disease, the mutant shows loss of hydrogen bonding interactions with the carboxylate side chain of Glu285, which disturbs the active site architecture leading to altered substrate binding and lower catalytic activity

E285A

the pathogenicity, stability, conservation, change in structural pattern, influence of the mutations on substrate binding of the crystallized mutations (K213E, Y231C, E285A, F295S, I143V and V186D) is compared. Of the crystallized mutations, the mutant E285A is found to be highly conserved as well as affecting the substrate binding with lesser number of overall hydrogen bonds

E285A

0.3% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease

F295S

Canavan disease mutation, undetectable enzyme activity

F295S

a naturally occuring missense mutation associated with the Canavan disease, the mutant shows loss of van der Waals contacts

F295S

the decreased availability of the active site for substrate molecules in the mutated enzymes explains their diminishing activity observed in clinical experiments. The variant is associated with the mild or variable form of Canavan disease

F295S

F295S

10% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease

H116A

site-directed mutagenesis, inactive mutant

H116A

no detectable activity

H21A

site-directed mutagenesis, inactive mutant

H21A

no detectable activity

K213E

Canavan disease mutation, undetectable enzyme activity

K213E

a naturally occuring missense mutation associated with a mild phenotype of Canavan disease, a nonconservative mutant, has minimal structural differences compared to the wild-type enzyme

K213E

the pathogenicity, stability, conservation, change in structural pattern, influence of the mutations on substrate binding of the crystallized mutations (K213E, Y231C, E285A, F295S, I143V and V186D) is compared. The mutant K213E is found to be least conserved, and the substrate binding affinity is found to be minimal

K213E

the point mutation does not affect the catalytic function of the enzyme

754806

N117Q

site-directed mutagenesis, the mutant enzyme is less stable than the wild-type enzyme, while it shows similar catalytic properties and substrate specificity

N117Q

homology modeling of the N117Q human aspartoacylase mutant using the native structure, PDB ID 2O53, as the template

R63N

undetectable ASPA activity

R63N

the mutation results in undetectable activity

Y231C

a naturally occuring missense mutation associated with the Canavan disease, the mutant shows loss of hydrophobic and hydrogen bonding interactions. The mutation leads to a local collapse of the hydrophobic core structure in the carboxyl-terminal domain, contributing to a decrease in protein stability

Y231C

Y231C

Y231C

24% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease

additional information

Canavan disease is a rare recessive genetic neurodegenerative brain disorder that is associated with many different mutations in the gene encoding aspartoacylase

700434

additional information

synthesis of PEGylated enzyme by treatment of enzyme samples with amethoxy-PEG reagent containing terminal activating aldehyde or ester groups attached with a carboxymethyl linker, purification of the protein-PEG conjugates by anion exchange chromatography, labeling with a covalently attached fluorescent tag, method optimization, overview

additional information

deep mutational scanning reveals a correlation between degradation and toxicity of thousands of aspartoacylase variants

774656

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

712823

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

restoration of deficient enzyme activity in CNS neurons does not ameliorate motor deficits and demyelination in a model of Canavan disease, which is caused by elevated levels of N-acetylaspartic acid, NAA, neuronal expression of ASPA can compensate for NAA-mediated neuronal hyperexcitation, but not for oligodebdrocyte dysfunciton, phenotypes, overview

show all columns Go to Temperature Stability Search

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Go to General Stability Search

rapidly denatures above

stable at

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

PEGylated forms of aspartoacylase (modified with PEG of 2 kDa, 5 kDa, 10 kDa, 20 kDa or 40 kDa) show similar activities to that of the native enzyme. The activity of PEGylated enzyme samples is monitored for 72 hours without observing a substantial loss in activity

pure enzyme extremely unstable

the Escherichia coli-expressed enzyme form is quite unstable, losing a significant fraction of its catalytic activity within 24 h

Go to Oxidation Stability Search

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OXIDATION STABILITY

ORGANISM

UNIPROT

LITERATURE

the Pichia pastoris-expressed enzyme shows sensitivity to oxidation over time and will precipitate if not kept under the proper reducing conditions, addition of 1 mM DTT reverses the precipitated state of the enzyme with no significant loss of activity

667727

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-20°C, frozen storage of undialyzed enzyme for a few days leads to a complete disappearance of activity following a single thaw

-70°C, kept for up to 4 weeks without loss of activity

209008

4°C, purified wild-type enzyme, expressed

the purified enzyme expressed in Pichia pastoris is significantly more stable than the Escherichia coli-expressed enzyme, losing less than 10% of its catalytic activity after 2 weeks when stored under conditions where the Escherichia coli-expressed enzyme becomes completely inactivated within 24 h, the Pichia pastoris-expressed enzyme shows sensitivity to oxidation over time and will precipitate if not kept under the proper reducing conditions

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

affinity chromatography

anion exchange chromatography followed by size exclusion chromatography

native enzyme from brain by subcellular fractionation, and anion exchange chromatography

nickel Sepharose column chromatography and Source 15Q column chromatography

One-step nickel-affinity chromatography

partial

recombinant enzyme by metal affinity chromatography, dialysis, and anion exchange chromatography

recombinant enzyme, overexpressed in bacteria

recombinant His-tagged enzyme from Pichia pastoris strain KM71H by nickel affinity chromatography, dialysis, and anion exchange chromatography

recombinant wild-type and mutant GST-fusion enzymes from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography

partial

partial

recombinant enzyme, overexpressed in bacteria

Go to Cloned (commentary) Search

recombinant enzyme, overexpressed in bacteria

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Pichia pastoris

expression in Escherichia coli

expression in Pichia pastoris

expression of mutant enzyme C152W in Saccharomyces cerevisiae. A decreased steady state compared to wild-type aspartoacylase is found as a result of increased proteasomal degradation

775283

expression of the GFP-tagged enzyme in COS-7 cells in cytoplasm, nucleoplasm, and nuclei

expression of wild-type and mutant enzymes as GST-fusion proteins in Escherichia coli strain BL21(DE3)

gene acy2 or ASPA, recombinant expression of His-tagged enzyme in Pichia pastoris strain KM71H and in Escherichia coli. Recombinantly-expressed human aspartoacylase is not glycosylated, but is still fully functional and stable even when produced from a bacterial expression system

gene acy2, recombinant expressionin Pichia pastoris strain KM71H

gene Aspa, expression analysis

gene for the production of aspartoacylase is located on chromosome 17

gene identified with human cDNA, cloned into a thioredoxin fusion vector and overexpressed in bacteria

hASPA gene cloned and overexpressed in bacteria

putative aspartoacylase identified, homologous to human ASPA

Prochlorococcus marinus

quantitative expression analysis in brain of wild-type and tremor rats

stable expression of wild-type and mutant enzyme in Pichia pastoris, expression in Escherichia coli strain XL10 primarily in inclusion bodies, while the expression yields are lower in Pichia pastoris than in Escherichia coli, the purified enzyme is significantly more stable, the enzyme form has the same substrate specificity but is 150fold more active than the Escherichia coli-expressed enzyme

expression in Escherichia coli

expression in Escherichia coli

678338, 682568

expression in Escherichia coli

expression in Escherichia coli

Go to Expression Search

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EXPRESSION

ORGANISM

UNIPROT

LITERATURE

aspartoacylase is the only enzyme downregulated by 0.5 h water-immersion restraint stress

aspartoacylase is the only enzyme upregulated by duloxetine

enzyme expression is decreased during the early stages of postnatal development

expression of aspartoacylase in gastric cancer is associated with immune infiltration

Go to Renatured Search

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

the Pichia pastoris-expressed wild-type enzyme shows sensitivity to oxidation over time and will precipitate if not kept under the proper reducing conditions, addition of 1 mM DTT reverses the precipitated state of the enzyme with no significant loss of activity

show all columns Go to Application Search

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

diagnostics

aspartoacylase can promote the occurrence and development of gastric cancer and presents a promising predictive biomarker for the disease since it is favourably connected with immune infiltrates and negatively correlated with prognosis

769947

medicine

nutrition

development of a general and simple procedure for the resolution of racemic amino acids

288852

pharmacology

the enzyme is the taget for treatment of Canavan disease, enzyme replacement therapy can potentially be used to overcome these defects if a stable enzyme form that can gain access to the appropriate neural cells can be produced. PEGylated form of aspartoacylase are able to traverse the blood-brain barrier and show dramatic enhancement in brain tissue access and distribution, overview. Examination of the effect of enzyme administration on the immunological response

medicine

diagnosis of Canavan disease, an autosomal recessive neurodegenerative disorder characterized by aspartoacylase deficiency, technique for prenatal diagnosis

medicine

mutations in the aspartoacylase aspA gene are implicated as the cause of Canavan Disease

top print hide References Search

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

D'Adamo, A.F.; Wertman, E.; Foster, F.; Schneider, H.

A radiochemical assay for N-acetyl-L-aspartate amidohydrolase (EC 3.5.1.15) and its occurrence in the tissues of the chicken

Life Sci.

791-796

1978

Gallus sp., Rattus norvegicus, Columba sp., no activity in Cavia porcellus

703517

brenda

Endo, Y.

Deacetylation and deformylation of N-acyl amino acids by kidney acylases

FEBS Lett.

281-283

1978

Cavia porcellus, Rattus norvegicus, Rattus norvegicus Wistar

720621

brenda

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