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Ligand N-acetyl-L-aspartate

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (12 results)

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Show Natural Substrate (12 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.15

N-acetyl-L-aspartate + H2O = acetate + L-aspartate

754250, 754480, 754618, 755390, 754252

-

3.5.1.15

N-acetyl-L-aspartate + H2O = aspartate + acetate

678979, 682568

-

3.5.1.15

N-acetyl-L-aspartate + H2O = L-aspartate + acetate

719532, 678338

-

3.5.1.15

N-acetyl-L-aspartic acid + H2O = acetate + aspartic acid

208999, 209001, 209005, 209006, 209007, 209008, 208998, 209000, 209002, 209003, 288852

-

3.5.1.15

N-acetylaspartate + H2O = acetate + L-aspartate

734393, 733213

-

3.5.1.15

N-acetylaspartate + H2O = aspartate + acetate

681524, 679264

-

3.5.1.15

N-acetylaspartate + H2O = L-aspartate + acetate

670342

-

3.5.1.15

N-acetylaspartic acid + H2O = aspartate + acetate

712986, 681846

-

3.5.1.15

N-acetylaspartic acid + H2O = L-asparatate + acetate

668542, 668640, 667777, 667727, 669635, 667443, 670342, 669958

-

3.5.1.15

9 entries

6.3.2.41

ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate

725423, 727869, 728179, 725404

-

6.3.2.42

2 ATP + N-acetyl-L-aspartate + 2 L-glutamate = 2 ADP + 2 phosphate + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate

725423

-

6.3.2.42

ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate

725423

-

6.3.2.42

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (7 results)

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Show Natural Product (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.17

acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartate

-

-

2.3.1.17

acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartic acid

486459, 486456, 486458, , 486457

-

3.4.17.21

N-acetyl-alpha-L-aspartyl-L-glutamate + H2O = N-acetyl-alpha-L-aspartate + L-glutamate

-

-

3.4.17.21

N-acetyl-Asp-Glu + H2O = N-acetyl-Asp + Glu

-

-

3.4.17.21

N-acetyl-alpha L-aspartyl-L-glutamate + H2O = N-acetyl-L-aspartate + L-glutamate

-

-

3.4.17.21

N-acetyl-L-aspartyl-L-glutamate + H2O = L-glutamate + N-acetyl-L-aspartate

-

-

3.4.17.21

N-acetyl-L-aspartyl-L-glutamate + H2O = N-acetyl-L-aspartate + L-glutamate

-

-

2.3.1.17

2 entries

3.4.17.21

5 entries

Substrate in Enzyme-catalyzed Reactions (23 results)

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Show Substrate (23 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.16

N-acetyl-L-aspartate + O2 = ? + H2O2

711324

-

2.7.2.4

ATP + N-acetyl-L-aspartate = ADP + N-acetyl-4-phospho-L-aspartate

642329

-

3.4.17.1

N-acetyl-L-aspartate = acetate + L-aspartate

678979

-

3.5.1.134

N-acetyl-L-aspartate + H2O = acetate + L-aspartate

755043

-

3.5.1.14

N-acetyl-L-Asp + H2O = acetate + L-Asp

711509

-

3.5.1.14

N-acetyl-L-aspartate + H2O = acetate + L-aspartate

713420

-

3.5.1.14

N-alpha-acetyl-L-aspartate + H2O = acetate + L-aspartate

657692

-

3.5.1.15

N-acetyl-L-aspartate + H2O = acetate + L-aspartate

754250, 754252, 754480, 754618, 754806, 755390

-

3.5.1.15

N-acetyl-L-aspartate + H2O = aspartate + acetate

678979, 682568

-

3.5.1.15

N-acetyl-L-aspartate + H2O = L-aspartate + acetate

720100, 719532, 720476, 719318, 720276, 678338

-

3.5.1.15

N-acetyl-L-aspartate + H2O = L-aspartate + acetic acid

697037

-

3.5.1.15

N-acetyl-L-aspartic acid + H2O = acetate + aspartic acid

208999, 209001, 209005, 209006, 209007, 209008, 208998, 209000, 209002, 209003, 288852

-

3.5.1.15

N-acetylaspartate + H2O = acetate + L-aspartate

734393, 733213

-

3.5.1.15

N-acetylaspartate + H2O = aspartate + acetate

681524, 679264

-

3.5.1.15

N-acetylaspartate + H2O = L-aspartate + acetate

670342

-

3.5.1.15

N-acetylaspartic acid + H2O = aspartate + acetate

712986, 681846

-

3.5.1.15

N-acetylaspartic acid + H2O = L-asparatate + acetate

667443, 667777, 667727, 668640, 668542, 669635, 670342, 669958

-

3.5.1.14

3 entries

3.5.1.15

10 entries

3.5.1.64

Nalpha-acetyl-L-Asp + H2O = methanol + CO2 + L-Asp

172071

-

3.5.1.68

N-acetyl-L-aspartate + H2O = acetate + L-aspartate

209222, 209224

-

6.3.2.41

ATP + N-acetyl-L-aspartate + citrate = ?

725404

-

6.3.2.41

ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate

725423, 727869, 728179, 725404

-

6.3.2.42

2 ATP + N-acetyl-L-aspartate + 2 L-glutamate = 2 ADP + 2 phosphate + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate

725423

-

6.3.2.42

ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate

725423

-

6.3.2.41

2 entries

6.3.2.42

2 entries

Product in Enzyme-catalyzed Reactions (15 results)

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Show Product (15 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.1

acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartate

486068

-

2.3.1.17

acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartate

-

-

2.3.1.17

acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartic acid

, 486459, 486456, 486458, 486457

-

3.4.17.21

N-acetyl-alpha-L-aspartyl-L-glutamate + H2O = N-acetyl-alpha-L-aspartate + L-glutamate

-

-

3.4.17.21

N-acetyl-Asp-Glu + H2O = N-acetyl-Asp + Glu

-

-

3.4.17.21

N-Acetyl-L-Asp-L-Glu + H2O = N-Acetyl-L-Asp + L-Glu

, 137216, 137217, 137224

-

3.4.17.21

N-acetyl-L-aspartyl-L-glutamate + H2O = N-acetyl-L-Asp + L-Glu

-

-

3.4.17.21

N-acetyl-alpha L-aspartyl-L-glutamate + H2O = N-acetyl-L-aspartate + L-glutamate

-

-

3.4.17.21

N-acetyl-L-aspartyl-L-glutamate + H2O = L-glutamate + N-acetyl-L-aspartate

-

-

3.4.17.21

N-acetyl-L-aspartyl-L-glutamate + H2O = N-acetyl-L-aspartate + L-glutamate

-

-

3.4.17.21

N-acetyl-L-aspartyl-L-glutamate = N-acetyl-L-aspartate + L-glutamate

-

-

3.5.1.1

N-acetyl-L-asparagine + H2O = N-acetyl-L-aspartic acid + NH3

-

-

3.5.1.1

Nalpha-acetyl-L-Asn + H2O = Nalpha-acetyl-L-Asp + NH3

-

-

3.5.1.1

Nalpha-acetyl-L-asparagine + H2O = Nalpha-acetyl-L-aspartate + NH3

-

-

2.3.1.17

2 entries

3.4.17.21

8 entries

3.5.1.1

3 entries

3.5.1.38

N-acetyl-L-asparagine + H2O = N-acetyl-L-aspartate + NH3

209094, 209097

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.15

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

754480

-

Inhibitor in Enzyme-catalyzed Reactions (10 results)

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Show Inhibitors (10 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.1

2 mM, 25% inhibition

486062

-

2.3.1.17

-

702144

-

2.3.1.17

IC50: 0.85 mM

659757

-

2.3.1.17

truncated bisubstrate analog

756429

-

2.3.1.17

3 entries

3.4.17.21

0.1 mM, 38% inhibition

137216

-

3.5.1.15

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

754250

-

3.5.1.15

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

-

3.5.1.15

substrate inhibition at high concentration

755390

-

3.5.1.15

substrate inhibition at concentration above 0.2 mM

667727

-

3.5.1.15

4 entries

4.3.1.1

-

6016

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (13 results)

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Show Turnover Number (13 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.16

0.0035

-

pH 8.0, 25°C, recombinant wild-type enzyme

711324

1.4.3.16

0.0055

-

pH 8.0, 25°C, recombinant mutant E121A

711324

1.4.3.16

2 entries

3.5.1.14

0.1

-

E167R mutant protein, pH not specified in the publication, temperature not specified in the publication

713420

3.5.1.15

0.083

-

pH and temperature not specified in the publication

755390

3.5.1.15

0.083

-

pH 7.2, recombinant Escherichia coli-expressed enzyme

667727

3.5.1.15

0.52

-

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

668640

3.5.1.15

1.48

-

pH 7.4, 37°C, recombinant mutant E178D

668640

3.5.1.15

12.7

-

pH 7.2, recombinant Pichia pastoris-expressed enzyme

667727

3.5.1.15

14.22

-

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

668640

3.5.1.15

37.5

-

-

679264

6.3.2.41

2.6

-

at pH 8.0 and 37°C

725404

6.3.2.41

2.6

-

pH 8.0, 30°C

725404

6.3.2.41

3

-

pH 8.0, 30°C

725404

3.5.1.15

7 entries

6.3.2.41

3 entries

K_M Value (16 results)

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Show KM Value (16 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.16

3.2

-

pH 8.0, 25°C, recombinant mutant E121A

711324

1.4.3.16

17

-

pH 8.0, 25°C, recombinant wild-type enzyme

711324

1.4.3.16

2 entries

2.7.2.4

48

-

pH 8.0, 25°C, aspartokinase III

642329

3.5.1.14

5

-

pH 7.0, 30°C

657692

3.5.1.15

0.1

-

-

208998

3.5.1.15

0.12

-

pH 7.2, recombinant Pichia pastoris-expressed enzyme

667727

3.5.1.15

0.163

-

-

679264

3.5.1.15

0.2

-

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

668640

3.5.1.15

0.22

-

pH 7.4, 37°C, recombinant mutant E178D

668640

3.5.1.15

0.36

-

pH and temperature not specified in the publication

755390

3.5.1.15

0.36

-

pH 7.2, recombinant Escherichia coli-expressed enzyme

667727

3.5.1.15

1.69

-

ASPA isolated from cytosol

681524

3.5.1.15

3.7

5

ASPA isolated from myelin

681524

6.3.2.41

1.48

-

at pH 8.0 and 37°C

725404

6.3.2.41

1.48

-

pH 8.0, 30°C

725404

6.3.2.41

4.59

-

pH 8.0, 30°C

725404

3.5.1.15

9 entries

6.3.2.41

3 entries

K_i Value (2 results)

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Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.1.17

0.56

-

-

702144

2.3.1.17

1.6

-

pH not specified in the publication, temperature not specified in the publication

756429

2.3.1.17

2 entries

IC₅₀ Value (1 result)

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Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

2.3.1.17

0.85

-

IC50: 0.85 mM

659757

References & Links

Literature References (68)

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Show Reference (68 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

6016

2853974

L-Aspartase from Escherichia coli: substrate specificity and role of divalent metal ions

1988

Falzone, C.J.; Karsten, W.E.; Conley, J.D.; Viola, R.E.

Biochemistry

27

9089-9093

137216

3667587

Hydrolysis of the brain dipeptide N-acetyl-L-aspartyl-L-glutamate

1987

Robinson, M.B.; Blakely, R.D.; Couto, R.; Coyle, J.T.

J. Biol. Chem.

262

14498-14506

137217

8558536

Design, synthesis and biological activity of a potent inhibitor of the neuropeptidase N-acetylated alpha-linked acidic dipeptidase

1996

Jackson, P.F.; Cole, D.C.; Slusher, B.S.; Stetz, S.L.; Ross, L.E.; Donzanti, B.A.; Trainor, D.A.

J. Med. Chem.

39

619-622

137224

2355230

Competitive inhibition of N-acetylated-alpha-linked acidic dipeptidase activity by N-acetyl-L-aspartyl-beta-linked L-glutamate

1990

Serval, V.; Barbeito, L.; Pittaluga, A.; Cheramy, A.; Lavielle, S.; Glowinski, J.

J. Neurochem.

55

39-46

172071

-

A novel enzyme, Nalpha-benzyloxycarbonyl amino acid urethane hydrolase IV

1985

Matsumura, E.; Shin, T.; Murao, S.; Sakaguchi, M.; Kawano, T.

Agric. Biol. Chem.

49

3643-3645

208998

703517

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

1978

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

Life Sci.

23

791-796

208999

720621

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

1978

Endo, Y.

FEBS Lett.

95

281-283

209000

19559

N-Acetyl-aspartate amidohydrolase: Purification and properties

1977

D'Adamo, A.F.; Peisach, J.; Manner, G.; Weiler, C.T.

J. Neurochem.

28

739-744

209001

1255182

Amidohydrolases of brain; enzymatic hydrolysis of N-acetyl-L-aspartate and other N-acyl-L-amino acids

1976

Goldstein, F.B.

J. Neurochem.

26

45-49

209002

4697888

The occurrence of N-acetylaspartate amidohydrolase (aminoacylase II) in the developing rat

1973

D'Adamo, A.F.; Smith, J.C.; Weiler, C.

J. Neurochem.

20

1275-1278

209003

-

Aminoacylase amino acid acylases I and II from hog kidney

1955

Birnbaum, S.M.

Methods Enzymol.

2

115-119

209005

1987315

Purification, characterization, and localization of aspartoacylase from bovine brain

1991

Kaul, R.; Casanova, J.; Johnson, A.B.; Tang, P.; Matalon, R.

J. Neurochem.

56

129-135

209006

10837925

Murine aspartoacylase: cloning, expression and comparison with the human enzyme

2000

Namboodiri, M.A.A.; Corigliano-Murphy, A.; Jiang, G.; Rollag, M.; Provencio, I.

Mol. Brain Res.

77

285-289

209007

10691291

Expression of aspartoacylase activity in cultured rat macroglial cells is limited to oligodendrocytes

1999

Baslow, M.H.; Suckow, R.F.; Sapirstein, V.; Hungund, B.L.

J. Mol. Neurosci.

13

47-53

209008

1756590

A radiometric assay for aspartoacylase activity in human fibroblasts: application for the diagnosis of canavan's disease

1991

Barash, V.; Flhor, D.; Morag, B.; Boneh, A.; Elpeleg, O.N.; Gilon, C.

Clin. Chim. Acta

201

175-182

209094

-

Characterization of an extracellular asparaginase of Rhodosporidium toruloides CBS14 exhibiting unique physicochemical properties

1996

Ramakrishnan, M.S.; Joseph, R.

Can. J. Microbiol.

42

316-325

209097

845119

Purification and properties of an L-glutaminase-L-asparaginase from Pseudomonas acidovorans

1977

Davidson, L.; Brear, D.R.; Wingard, P.; Hawkins, J.; Kitto, G.B.

J. Bacteriol.

129

1379-1386

209222

6414521

A beta-citryl-L-glutamate-hydrolysing enzyme in rat testes

1983

Miyake, M; Innami, T; Kakimoto, Y.

Biochim. Biophys. Acta

760

206-214

209224

7612651

Purification and properties of beta-citryl-L-glutamate-hydrolysing enzyme from rat testis particulate

1995

Asakura, M; Nagahashi, Y.; Hamada, M.; Kawai, M.; Kadobayashi, K.; Narahara, M.; Nakagawa, S.; Kawai, Y.; Hama, T.; Miyake, M.

Biochim. Biophys. Acta

1250

35-42

288852

14927637

Specificity of amino acid acylases

1952

Birnbaum, S.M.; Levintow, L.; Kingsley, R.B.; Greenstein, J.P.

J. Biol. Chem.

194

455-470

486062

25771

N-Acetylglutamate synthetase from rat-liver mitochondria. Partial purification and catalytic properties

1978

Shigesada, K.; Tatibana, M.

Eur. J. Biochem.

84

285-291

486068

7287652

Subcellular localization and properties of N-acetylglutamate synthase in rat small intestinal mucosa

1981

Uchiyama, C.; Mori, M.; Tatibana, M.

J. Biochem.

89

1777-1786

486456

-

Biosynthesis of N-acetyl-L-aspartic acid

1959

Goldstein, F.B.

J. Biol. Chem.

234

2702-2706

486457

6061408

The enzymatic synthesis of N-acetyl-L-aspartic acid by a water-insoluble preparation of a cat brain acetone powder

1967

Knizley, H.Jr.

J. Biol. Chem.

242

4619-4622

486458

4045470

N-Acetylation of L-aspartate in the nervous system: differential distribution of a specific enzyme

1985

Truckenmiller, M.E.; Namboodiri, M.A.A.; Brownstein, M.J.; Neale, J.H.

J. Neurochem.

45

1658-1662

486459

11279290

Direct determination of the N-acetyl-L-aspartate synthesis rate in the human brain by (13)C MRS and [1-(13)C]glucose infusion

2001

Moreno, A.; Ross, B.D.; Bluml, S.

J. Neurochem.

77

347-350

642329

8914836

Specificity of aspartokinase III from Escherichia coli and an examination of important catalytic residues

1996

Keng, Y.F.; Viola, R.E.

Arch. Biochem. Biophys.

335

73-81

657692

12682714

Purification and characterisation of a lactococcal aminoacylase

2003

Curley, P.; van der Does, C.; Driessen, A.J.; Kok, J.; van Sinderen, D.

Arch. Microbiol.

179

402-408

659757

12887681

Characterization of the N-acetylaspartate biosynthetic enzyme from rat brain

2003

Madhavarao, C.N.; Chinopoulos, C.; Chandrasekaran, K.; Namboodiri, M.A.

J. Neurochem.

86

824-835

667443

16707098

Upregulation of aspartoacylase activity in the duodenum of obesity induced diabetes mouse: implications on diabetic neuropathy

2006

Surendran, S.; Matalon, R.; Tyring, S.K.

Biochem. Biophys. Res. Commun.

345

973-975

667727

16669630

Characterization of human aspartoacylase: the brain enzyme responsible for Canavan disease

2006

Le Coq, J.; An, H.J.; Lebrilla, C.; Viola, R.E.

Biochemistry

45

5878-5884

667777

15337171

Transport of N-acetylaspartate via murine sodium/dicarboxylate cotransporter NaDC3 and expression of this transporter and aspartoacylase II in ocular tissues in mouse

2004

George, R.L.; Huang, W.; Naggar, H.A.; Smith, S.B.; Ganapathy, V.

Biochim. Biophys. Acta

1690

63-69

668542

16935940

Aspartoacylase is a regulated nuclear-cytoplasmic enzyme

2006

Hershfield, J.R.; Madhavarao, C.N.; Moffett, J.R.; Benjamins, J.A.; Garbern, J.Y.; Namboodiri, A.

FASEB J.

20

2139-2141

668640

17027983

Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease

2006

Herga, S.; Berrin, J.G.; Perrier, J.; Puigserver, A.; Giardina, T.

FEBS Lett.

580

5899-5904

669635

15065127

Immunohistochemical localization of aspartoacylase in the rat central nervous system

2004

Madhavarao, C.N.; Moffett, J.R.; Moore, R.A.; Viola, R.E.; Namboodiri, M.A.; Jacobowitz, D.M.

J. Comp. Neurol.

472

318-329

669958

16634055

Novel role for aspartoacylase in regulation of BDNF and timing of postnatal oligodendrogenesis

2006

Francis, J.S.; Olariu, A.; McPhee, S.W.; Leone, P.

J. Neurosci. Res.

84

151-169

670342

15851013

Restoration of aspartoacylase activity in CNS neurons does not ameliorate motor deficits and demyelination in a model of Canavan disease

2005

Klugmann, M.; Leichtlein, C.B.; Symes, C.W.; Serikawa, T.; Young, D.; During, M.J.

Mol. Ther.

11

745-753

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