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Ligand D-aspartic acid

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for D-aspartic acid

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (9 results)

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Show Natural Substrate (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.1

D-Asp + H2O + O2 = oxaloacetate + NH3 + H2O2

711718, 712616, 712787, 742035, 742805

-

1.4.3.1

D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2

391716, 711325, 711719, 711722, 743140, 391706, 391712, 391726, 391728, 712818, 723870, 391705, 391707, 391708, 391711, 391717, 391718, 391719, 391720, 391721, 391722, 391723, 391724, 391725, 391727, 725959, 391710, 656415, 391713, 724597, 657350, 391714, 711721, 391715, 742426, 743133, 743350, 743836, 743063, 391709, 677271

-

1.4.3.1

2 entries

1.4.3.15

D-aspartic acid + H2O + O2 = oxaloacetate + NH3 + H2O2

391754, 677271

-

1.4.3.3

D-Asp + H2O + O2 = oxaloacetate + NH3 + H2O2

743827

-

1.4.3.3

D-aspartic acid + H2O + O2 = oxaloacetate + NH3 + H2O2

391830

-

1.4.3.3

2 entries

1.4.3.7

D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2

395288, 395287, 395286

-

2.6.1.21

D-aspartate + 2-oxoglutarate = 2-oxosuccinate + D-glutamate

759235

-

6.3.1.12

ATP + D-aspartate + [beta-GlcNAc-(1,4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n = [beta-GlcNAc-(1,4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate

669439

-

6.3.1.12

ATP + D-aspartate + [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate

727421

-

6.3.1.12

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (4 results)

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Show Natural Product (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.1

D-asparagine + H2O = D-aspartate + NH3

0

1hg1, 3D-view

5.1.1.13

L-Asp = D-Asp

0

-

5.1.1.13

L-aspartate = D-aspartate

0, 652886

-

5.1.1.13

2 entries

5.1.1.18

L-aspartate = D-aspartate

0

-

Substrate in Enzyme-catalyzed Reactions (25 results)

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Show Substrate (25 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.28

D-aspartate + H2O + NAD+ = 2-oxobutanedioate + NH3 + NADH + H+

763366

-

1.4.3.1

D-Asp + H2O + O2 = oxaloacetate + NH3 + H2O2

711718, 712616, 712787, 742035, 742805

-

1.4.3.1

D-aspartate + H2O + O2 = oxaloacetate + H2O2 + NH3

762658, 762748, 762756, 762755

-

1.4.3.1

D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2

391716, 686597, 711325, 711719, 711722, 743140, 391706, 391709, 391712, 391726, 391728, 712818, 723870, 391705, 391707, 391708, 391711, 391717, 391718, 391719, 391720, 391721, 391722, 391723, 391724, 391725, 391727, 725959, 391710, 656415, 391713, 724597, 657350, 391714, 711721, 391715, 655928, 684387, 742426, 743133, 743350, 743836, 687440, 743063, 763008, 684383, 673583, 677271

-

1.4.3.15

D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2

764236

-

1.4.3.15

D-aspartic acid + H2O + O2 = oxaloacetate + NH3 + H2O2

391755, 677271, 391754

-

1.4.3.1

3 entries

1.4.3.15

2 entries

1.4.3.19

D-aspartate + H2O + O2 = ?

689934, 701114

-

1.4.3.3

D-Asp + H2O + O2 = oxaloacetate + NH3 + H2O2

673646, 743827, 654898, 391705, 654786, 684417

-

1.4.3.3

D-aspartate + H2O + O2 = ?

699464

-

1.4.3.3

D-aspartate + H2O + O2 = ? + NH3 + H2O2

696171

-

1.4.3.3

D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2

723920, 687891, 685416, 763089, 685750, 724793

-

1.4.3.3

D-aspartic acid + H2O + O2 = oxaloacetate + NH3 + H2O2

391830

-

1.4.3.3

5 entries

1.4.3.7

D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2

395288, 395287, 395286

-

1.4.99.6

D-Asp + H2O + oxidized 2,6-dichlorophenolindophenol = 2-oxobutanedioate + NH3 + reduced 2,6-dichlorophenolindophenol

695533

-

1.5.99.13

D-aspartate + oxidized 2,6-dichloroindophenol + H2O = oxaloacetate + NH3 + reduced 2,6-dichloroindophenol

394966, 684424

-

2.6.1.21

D-aspartate + 2-oxoglutarate = 2-oxosuccinate + D-glutamate

636736, 759235, 636742

-

2.6.1.21

D-aspartate + pyruvate = 2-oxosuccinate + D-alanine

636736, 636738, 636742, 759259

-

2.6.1.21

2 entries

2.6.1.74

D-aspartate + 2-oxoadipate = oxaloacetate + 2-aminoadipate

640195

-

5.1.1.10

D-Asp = L-Asp

2049

-

5.1.1.10

D-aspartate = L-aspartate

715591

-

5.1.1.10

2 entries

5.1.1.13

D-aspartate = L-aspartate

716952, 747720, 746724, 747721

-

6.1.1.12

ATP + D-aspartate + tRNAAsp = AMP + diphosphate + D-aspartyl-tRNAAsp

674863

-

6.3.1.12

ATP + D-aspartate + [beta-GlcNAc-(1,4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n = [beta-GlcNAc-(1,4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate

670324, 669439, 669171

-

6.3.1.12

ATP + D-aspartate + [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate

727421

-

6.3.1.12

2 entries

6.3.2.4

ATP + D-Asp = ADP + phosphate + D-Asp-D-Asp

672685

-

Product in Enzyme-catalyzed Reactions (27 results)

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Show Product (27 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.16

oxaloacetate + NH3 + NADPH + H+ = D-aspartate + NADP+

0

-

3.1.1.43

D-aspartate dimethyl ester + H2O = D-aspartate + methanol

651785

-

3.1.1.96

D-aspartyl-tRNAAsp + H2O = D-aspartate + tRNAAsp

0

-

3.4.13.17

Gly-D-Asp + H2O = Gly + D-Asp

81206

-

3.4.13.19

L-Arg-D-Asp + H2O = L-Arg + D-Asp

0

-

3.5.1.1

D-Asn + H2O = D-Asp + NH3

0

1hg1, 3D-view

3.5.1.1

D-aspartic acid beta-hydroxamate + H2O = D-Asp + hydroxylamine

0

1hg1, 3D-view

3.5.1.1

D-asparagine + H2O = D-aspartate + NH3

0

1hg1, 3D-view

3.5.1.14

N-butyryl-D-aspartate + H2O = butanoate + D-aspartate

0

-

3.5.1.14

N-formyl-D-aspartate + H2O = formate + D-aspartate

0

-

3.5.1.14

N-glycyl-D-aspartate + H2O = glycine + D-aspartate

0

-

3.5.1.14

N-propionyl-D-aspartate + H2O = proipionate + D-aspartate

0

-

3.5.1.2

D-Asn + H2O = D-Asp + NH3

0

-

3.5.1.2

D-Asn + H2O = D-aspartate + NH3

0

-

3.5.1.2

D-asparagine + H2O = D-aspartate + NH3

0

-

3.5.1.1

3 entries

3.5.1.14

4 entries

3.5.1.2

3 entries

3.5.1.38

D-asparagine + H2O = D-aspartate + NH3

0, 209091, 209100, 209101, 209090, 209092, 209097, 209098, 209103

-

3.5.1.77

N-carbamoyl-D-Asp + H2O = D-Asp + NH3 + CO2

0

-

3.5.1.81

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

0

-

3.5.1.83

N-Acetyl-D-Asp + H2O = acetate + D-Asp

0

-

3.5.1.83

N-Butanoyl-D-Asp + H2O = Butanoate + D-Asp

0

-

3.5.1.83

N-Formyl-D-Asp + H2O = Formate + D-Asp

0

-

3.5.1.83

N-glycyl-D-Asp + H2O = Gly + D-Asp

0

-

3.5.1.83

N-Propanoyl-D-Asp + H2O = Propanoate + D-Asp

0

-

3.5.1.83

5 entries

5.1.1.10

L-aspartate = D-aspartate

0

-

5.1.1.13

L-Asp = D-Asp

0, 2075

-

5.1.1.13

L-aspartate = D-aspartate

0, 650892, 650894, 649759, 649148, 652886

-

5.1.1.13

2 entries

5.1.1.18

L-aspartate = D-aspartate

0

-

Activator in Enzyme-catalyzed Reactions (6 results)

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Show Activating Compound (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.38

2 mM, 1.27fold activation

286694

-

1.4.3.1

substrate activation at D-aspartate concentrations above 0.2 mM

687440

-

2.1.3.2

5700% activation

485858

-

2.6.1.31

increases activity

639962

-

3.1.3.5

-

677509

-

4.3.1.1

-

649266

-

Inhibitor in Enzyme-catalyzed Reactions (11 results)

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Show Inhibitors (11 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.2

90% activity in the presence of 10 mM D-aspartate

692832

-

1.4.3.16

-

711324

-

1.4.3.16

weak inhibition; weak inhibition

721394

-

1.4.3.16

2 entries

2.6.1.21

inhibition of D- and L-transamination of D-alanine to 2-oxoglutarate, weak

636737

-

2.6.1.5

weak inhibition

640098

-

3.5.1.1

-

208940

1hg1, 3D-view

4.3.1.1

competitive

5998, 6000, 6009

-

6.3.1.4

-

949

-

6.3.2.9

weak

1293

-

6.3.4.5

-

1574

-

6.3.5.4

weak

1713

-

3D Structure of Enzyme-Ligand-Complex (PDB) (13 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (13 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.3.2.13

4kty, 3D-view

2.7.11.1

6spw, 3D-view

2.7.11.1

6spx, 3D-view

2.7.11.1

6spw, 3D-view

2.7.11.1

6spx, 3D-view

2.7.11.1

6spw, 3D-view

2.7.11.1

6spx, 3D-view

2.7.11.1

6spw, 3D-view

2.7.11.1

6spx, 3D-view

2.7.11.1

8 entries

3.4.21.4

1an1, 3D-view

3.4.24.27

1ks7, 3D-view

3.5.1.1

1hg1, 3D-view

3.5.1.98

6wi3, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (53 results)

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Show Turnover Number (53 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.1

0.183

-

-

391721

1.4.3.1

0.183

-

50 mM potassium phosphate buffer, 0.3 mM EDTA, pH 7.4, 4°C

391719

1.4.3.1

0.725

-

50 mM potassium phosphate buffer, 0.3 mM EDTA, pH 7.4, 25°C

391721

1.4.3.1

1.3

-

pH 7.0, 20°C, recombinant mutant R243E

712787

1.4.3.1

1.4

-

pH 7.0, 20°C, recombinant mutant R243K

712787

1.4.3.1

2.51

-

pH 8.3, 37°C, recombinant DDO-3

711718

1.4.3.1

3.07

-

37°C, pH 8.3, F18E3.7a gene product

673583

1.4.3.1

3.13

-

37°C, pH 8.3, C47A10.5 gene product

673583

1.4.3.1

9.49

-

pH 8.3, 37°C, recombinant DDO-2

711718

1.4.3.1

9.83

-

at pH 8.3 and 37°C

742035

1.4.3.1

26.1

-

pH 8.3, 37°C, recombinant DDO-1

711718

1.4.3.1

27.9

-

pH and temperature not specified in the publication

724597

1.4.3.1

31.1

-

at pH 8.3 and 37°C

742035

1.4.3.1

50.9

-

mutant F248Y, pH 7, 60°C

762658

1.4.3.1

58.4

-

pH 8.3, 25°C

762756

1.4.3.1

62.6

-

pH 7.0, 20°C, recombinant mutant R243M

712787

1.4.3.1

68.4

-

at pH 8.3 and 37°C

742035

1.4.3.1

74.5

-

pH 7.0, 20°C, recombinant wild-type enzyme

712787

1.4.3.1

74.5

-

wild type enzyme, at pH 7.5 and 37°C

742805

1.4.3.1

81.3

-

wild-type, pH 8.3, 25°C

763008

1.4.3.1

82.6

-

37°C, pH 7.5

655928

1.4.3.1

121

-

pH 7.0, 20°C, recombinant mutant R243D

712787

1.4.3.1

123

-

wild-type, pH 7, 60°C

762658

1.4.3.3

0.09

-

mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

0.26

-

mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

0.37

-

mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

0.5

-

mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

0.5

-

wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

0.56

-

mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

0.67

-

mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

0.9

-

mutant enzyme Y223S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

0.95

-

at pH 8.0 and 37°C

743827

1.4.3.3

1

-

mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

2.5

-

mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

3.2

-

mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

3.9

-

mutant enzyme M213R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

6

-

mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

6.7

-

pH 8.5, 25°C

673646

1.4.3.3

6.7

-

at pH 7.0 and 25°C

723920

1.4.3.3

29

-

pH 8.5, 25°C, wild-type enzyme

391705

1.4.3.3

235

-

pH 8.5, 25°C, mutant enzyme M213R

391705

1.4.3.3

1665

-

pH 8.5, 25°C, mutant enzyme M213R/Y238R

391705

5.1.1.13

0.0322

-

recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C

746724

5.1.1.13

6.4

-

pH 5.53, 2 mM ATP

650894

5.1.1.13

9.3

-

pH 5.53, 1 mM ATP

650894

5.1.1.13

13.1

-

recombinant His-tagged wild-type enzyme, pH 8.0, 30°C

746724

5.1.1.13

14.7

-

pH 5.53

650894

5.1.1.13

17.8

-

recombinant His-tagged mutant P150S, pH 8.0, 30°C

746724

5.1.1.13

25.3

-

recombinant His-tagged wild-type enzyme, pH 8.0, 30°C

746724

5.1.1.13

27.6

-

recombinant His-tagged wild-type enzyme, pH 8.0, 30°C

746724

5.1.1.13

28.2

-

pH 5.53, 2 mM AMP

650894

5.1.1.13

42.9

-

pH 5.53, 4 mM AMP

650894

5.1.1.13

610000

-

recombinant enzyme, pH 8.0, 90°C

747721

1.4.3.1

23 entries

1.4.3.3

19 entries

5.1.1.13

11 entries

K_M Value (84 results)

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Show KM Value (84 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.1

0.38

-

37°C, pH 8.3, F18E3.7a gene product

673583

1.4.3.1

0.86

-

O2 as acceptor

391727

1.4.3.1

0.87

-

mutant F248Y, pH 7, 60°C

762658

1.4.3.1

1

-

pH 7.0, 20°C, recombinant mutant R243D

712787

1.4.3.1

1.05

-

wild-type, pH 8.3, 25°C

763008

1.4.3.1

1.2

-

mutant enzyme S308G fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

684387

1.4.3.1

1.3

-

pH and temperature not specified in the publication

724597

1.4.3.1

1.6

-

at 25°C

391721

1.4.3.1

1.78

-

mutant enzyme S308A fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

684387

1.4.3.1

2

-

pH 7.0, 20°C, recombinant mutant R243E

712787

1.4.3.1

2.02

-

37°C, pH 8.3, C47A10.5 gene product

673583

1.4.3.1

2.1

-

at pH 8.3 and 37°C

742035

1.4.3.1

2.1

-

pH 8.3, 25°C

762756

1.4.3.1

2.2

-

at 4°C

391719

1.4.3.1

2.26

-

at pH 8.3 and 37°C

742035

1.4.3.1

2.37

-

His-tagged mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

684387

1.4.3.1

2.5

-

pH 7.0, 20°C, recombinant wild-type enzyme

712787

1.4.3.1

2.5

-

wild type enzyme, at pH 7.5 and 37°C

742805

1.4.3.1

2.5

-

at pH 8.3

391723

1.4.3.1

2.7

-

-

391712, 391705

1.4.3.1

2.9

-

37°C, pH 7.5

655928

1.4.3.1

3.7

-

-

391707, 391713

1.4.3.1

3.8

-

pH 7.0, 20°C, recombinant mutant R243M

712787

1.4.3.1

3.81

-

pH 8.3, 37°C, recombinant DDO-3

711718

1.4.3.1

4.2

-

pH 8.3, 37°C, recombinant DDO-2

711718

1.4.3.1

4.22

-

pH 8.2, 37°C, kidney

712616

1.4.3.1

4.26

-

pH 8.2, 37°C, brain

712616

1.4.3.1

4.3

-

-

391714

1.4.3.1

4.41

-

pH 8.2, 37°C, liver

712616

1.4.3.1

4.5

-

-

391717

1.4.3.1

4.87

-

wild type enzyme fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

684387

1.4.3.1

5.19

-

-

656415

1.4.3.1

5.2

-

ferricyanide as acceptor

391727

1.4.3.1

5.5

-

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

711722

1.4.3.1

5.54

-

pH 8.3, 37°C, recombinant DDO-1

711718

1.4.3.1

5.7

-

at pH 7.4

391723

1.4.3.1

5.8

-

-

391717

1.4.3.1

7.3

-

His-tagged wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

684387

1.4.3.1

7.37

-

at pH 8.3 and 37°C

742035

1.4.3.1

7.5

-

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

711722

1.4.3.1

7.63

-

mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

684387

1.4.3.1

7.7

-

-

391725

1.4.3.1

8.77

-

wild-type, pH 7, 60°C

762658

1.4.3.1

10.3

-

pH 7.0, 20°C, recombinant mutant R243K

712787

1.4.3.1

13.4

-

pH 7.0, 20°C, recombinant mutant R243A

712787

1.4.3.3

2

-

pH 8.5, 25°C, mutant enzyme M213R

391705

1.4.3.3

2

-

mutant enzyme M213R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

5.2

-

mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

15

-

mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

15

-

mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

17

-

mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

18

-

pH 8.5, 25°C, wild-type enzyme

654898, 391705

1.4.3.3

18

-

wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

28

-

pH 8.5, 25°C, mutant enzyme M213R/Y238R

391705

1.4.3.3

30

-

pH 8.5, 25°C, mutant enzyme S335G

654898

1.4.3.3

30

-

mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

33

-

mutant enzyme Y223S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

43

-

at pH 8.0 and 37°C

743827

1.4.3.3

53

-

mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

61

-

mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

72

-

mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

98

-

mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

150

-

mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

685416

1.4.3.3

2000

-

pH 8.5, 25°C

673646

1.4.3.3

2000

-

at pH 7.0 and 25°C

723920

1.4.3.7

4.5

-

-

395288

1.4.3.7

5.4

-

-

395287

1.4.3.1

45 entries

1.4.3.3

20 entries

1.4.3.7

2 entries

5.1.1.10

94

-

in 50 mM Tris-HCl buffer, pH 8.0, at 30°C

715591

5.1.1.13

0.94

-

-

661647

5.1.1.13

1.37

-

recombinant His-tagged wild-type enzyme, pH 8.0, 30°C

746724

5.1.1.13

4.55

-

recombinant His-tagged mutant P150S, pH 8.0, 30°C

746724

5.1.1.13

6.21

-

recombinant His-tagged wild-type enzyme, pH 8.0, 30°C

746724

5.1.1.13

8.7

-

-

2076, 2078

5.1.1.13

9.86

-

recombinant His-tagged wild-type enzyme, pH 8.0, 30°C

746724

5.1.1.13

11.11

-

pH 4.6, 60°C, recombinant enzyme

747720

5.1.1.13

17.2

-

-

674359

5.1.1.13

60.4

-

37°C, pH 8

650892

5.1.1.13

80.6

-

recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C

746724

5.1.1.13

136

-

recombinant enzyme, pH 8.0, 90°C

747721

5.1.1.13

159

-

pH 5.53, 1 mM ATP or no addings

650894

5.1.1.13

160

-

pH 5.53, 2 mM ATP

650894

5.1.1.13

162

-

pH 5.53, 2 mM AMP

650894

5.1.1.13

164

-

pH 5.53, 4 mM AMP

650894

5.1.1.13

15 entries

6.3.1.12

2

-

-

669171

References & Links

Literature References (139)

top print hide

Show Reference (139 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

949

-

Biosynthesis of asparagine

1961

AlDawody, A.; Varner, J.E.

Fed. Proc.

20

10C

1293

3301347

Partial purification and specificity studies of the D-glutamate-adding and D-alanyl-D-alanine-adding enzymes from Escherichia coli K12

1987

Michaud, C.; Blanot, D.; Flouret, B.; van Heijenoort, J.

Eur. J. Biochem.

166

631-637

1574

4355767

Enzymes of arginine and urea synthesis

1973

Ratner, S.

Adv. Enzymol. Relat. Areas Mol. Biol.

39

1-90

1713

5076775

Glutamine-dependent asparagine synthetase from leukemia cells. Chloride dependence mechanism of action and inhibition

1972

Horowitz, B.; Meister, A.

J. Biol. Chem.

247

6708-6719

2049

-

Amino acid racemase with broad substrate specificity, its properties and use in phenylalanine racemization

1988

Asano, Y.; Endo, K.

Appl. Microbiol. Biotechnol.

29

523-527

2075

4626916

Partial purification and characterization of an aspartate racemase from Streptococcus faecalis

1972

Lamont, H.C.; Staudenbauer, W.L.; Strominger, J.L.

J. Biol. Chem.

247

5103-5106

2076

1526977

Properties of aspartate racemase, a pyridoxal 5'-phosphate-independent amino acid racemase

1992

Yamaguchi, T.; Choi, S.Y.; Okada, H.; Yohda, M.; Kumagai, H.; Esaki, N.; Soda, K.

J. Biol. Chem.

267

18361-18364

2078

-

PLP-dependent and independent amino acid racemase

1991

Soda, K.

Enzymes Depend. Pyridoxal Phosphate Other Carbonyl Comp. Cofactors (Proc. Int. Symp. Vitam. B6 Carbonyl Catal. , Meeting Date 1990, Fukui T. , ed. ) Pergamon, Oxford

8

29-34

5998

4584395

Purification and molecular properties of aspartate from Escherichia coli

1973

Suzuki, S.; Yamaguchi, J.; Tokushige, M.

Biochim. Biophys. Acta

321

369-381

6000

240429

Role of sulfhydryl groups in aspartase from Escherichia coli

1975

Mizuta, K.; Tokushige, M.

Biochim. Biophys. Acta

403

221-231

6009

3003513

Aspartate ammonia-lyase

1985

Tokushige, M.

Methods Enzymol.

113

618-627

81206

6444201

Peptidyl-D-amino acid hydrolase from Loligo vulgaris Lam. Purification and characterization

1984

D'Aniello, A.; Strazullo, L.

J. Biol. Chem.

259

4237-4243

208940

7259189

Purification and properties of asparaginase from Lupinus arboreus and Lupinus angustifolius

1981

Chang, K.S.; Farnden, K.J.F.

Arch. Biochem. Biophys.

208

49-58

209090

10684596

Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu

2000

Ortlund, E.; Lacount, M.W.; Lewinski, K.; Lebioda, L.

Biochemistry

39

1199-1204

209091

10499283

Cloning, sequence analysis, and expression of ansB from Pseudomonas fluorescens, encoding periplasmic glutaminase/asparaginase

1999

Huser, A.; Klöppner, U.; Röhm, K.H.

FEMS Microbiol. Lett.

178

327-335

209092

9020792

Ion binding induces closed conformation in Pseudomonas 7A glutaminase-asparaginase (PGA): Crystal structure of the PGA-SO42-NH4+ complex at 1.7 A resolution

1997

Jakob, C.G.; Lewinski, K.; LaCount, M.W.; Roberts, J.; Lebioda, L.

Biochemistry

36

923-931

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

209098

401650

L-Asparaginases from Citrobacter freundii

1977

Davidson, L.; Burkom, M.; Ahn, S.; Chang, L.C.; Kitto, B.

Biochim. Biophys. Acta

480

282-294

209100

5441

Purification and properties of a highly potent antitumor glutaminase-asparaginase from Pseudomonas 7A

1976

Roberts, J.

J. Biol. Chem.

251

2119-2123

209101

-

Extracellular asparaginase-glutaminase of Tilachlidium humicola

1973

Imada, A.; Igarski, S.

J. Takeda Res. Lab.

32

140-151

209103

5017769

Isolation, crystallization, and properties of Achromobacteraceae glutaminase-asparaginase with antitumor activity

1972

Roberts, J.; Holcenberg, J.S.; Dolowy, W.C.

J. Biol. Chem.

247

84-90

286694

4616960

Studies on the regulatory functions of malic enzymes: III. Regulatory effects of L-aspartate, Coenzyme A, and divalent metal ions on NAD-linked malic enzyme from Escherichia coli

1974

Yamaguchi, M.; Tokushige, M.; Takeo, K.; Katsuki, H.

J. Biochem.

76

1259-1268

391705

12021281

Engineering the substrate specificity of D-amino-acid oxidase

2002

Sacchi, S.; Lorenzi, S.; Molla, G.; Pilone, M.S.; Rossetti, C.; Pollegioni, L.

J. Biol. Chem.

277

27510-27516

391706

12209855

Cellular and subcellular distribution of D-aspartate oxidase in human and rat brain

2002

Zaar, K.; Kost, H.P.; Schad, A.; Volkl, A.; Baumgart, E.; Fahimi, H.D.

J. Comp. Neurol.

450

272-282

391707

10209293

Purification of beef kidney D-aspartate oxidase overexpressed in Escherichia coli and characterization of its redox potentials and oxidative activity towards agonists and antagonists of excitatory amino acid receptors

1999

Negri, A.; Tedeschi, G.; Ceciliani, F.; Ronchi, S.

Biochim. Biophys. Acta

1431

212-222

391708

10665376

D-Aspartate oxidase is present in ovaries, eggs and embryos but not in testis of Xenopus laevis

1999

Tedeschi, G.; Negri, A.; Bernardini, G.; Oungre, E.; Ceciliani, F.; Ronchi, S.

Comp. Biochem. Physiol. B

124

489-494

391709

9820813

C-terminal tripeptide Ser-Asn-Leu (SNL) of human D-aspartate oxidase is a functional peroxisome-targeting signal

1998

Amery, L.; Brees, C.; Baes, M.; Setoyama, C.; Miura, R.; Mannaerts, G.P.; Van Veldhoven, P.P.

Biochem. J.

336

367-371

391710

-

D-Aspartate oxidase and free acidic D-amino acids in fish tissues

1998

Kera, Y.; Hasegawa, S.; Watanabe, T.; Segawa, H.; Yamada, R.H.

Comp. Biochem. Physiol. B

119

95-100

391711

9148742

cDNA cloning and expression of the flavoprotein D-aspartate oxidase from bovine kidney cortex

1997

Simonic, T.; Duga, S.; Negri, A.; Tedeschi, G.; Malcovati, M.; Tenchini, M.L.; Ronchi, S.

Biochem. J.

322

729-735

391712

9163533

Structural and functional characterization of the human brain D-aspartate oxidase

1997

Setoyama, C.; Miura, R.

J. Biochem.

121

798-803

391713

8645733

Purification and properties of D-aspartate oxidase from Cryptococcus humicolus UJ1

1996

Yamada, R.h.; Ujiie, H.; Kera, Y.; Nakase, T.; Kitagawa, K.; Imasaka, T.; Arimoto, K.; Takahashi, M.; Matsumura, Y.

Biochim. Biophys. Acta

1294

153-158

391714

7915543

Properties of the flavoenzyme D-aspartate oxidase from Octopus vulgaris

1994

Tedeschi, G.; Negri, A.; Ceciliani, F.; Ronchi, S.; Vetere, A.; D'Aniello, G.; D'Aniello, A.

Biochim. Biophys. Acta

1207

217-222

391715

-

Isolation, enzyme production and characterization of D-aspartate oxidase from Fusarium sacchari var. elongatum Y-105

1994

Wakayama, M.; Nakashima, S.; Sakai, K.; Moriguchi, M.

J. Ferment. Bioeng.

78

377-379

391716

7903300

Biological role of D-amino acid oxidase and D-aspartate oxidase. Effects of D-amino acids

1993

D'Aniello, A.; D'Onofrio, G.; Pischetola, M.; D'Aniello, G.; Vetere, A.; Petrucelli, L.; Fisher, G.H.

J. Biol. Chem.

268

26941-26949

391717

8103425

Further study on the specificity of D-amino acid oxidase and of D-aspartate oxidase and time course for complete oxidation of D-amino acids

1993

D'Aniello, A.; Vetere, A.; Petrucelli, L.

Comp. Biochem. Physiol. B

105

731-734

391718

1555574

Chemical modification of functional arginyl residues in beef kidney D-aspartate oxidase

1992

Tedeschi, G.; Negri, A.; Ceciliani, F.; Biondi, P.A.; Secchi, C.; Ronchi, S.

Eur. J. Biochem.

205

127-132

391719

-

Structural studies of beef kidney D-aspartate oxidase

1990

Negri, A.; Tedeschi, G.; Ceciliani, F.; Simonic, T.

Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York

-

179-187

391720

-

Modification of substrate specificity of D-aspartate oxidase chemically modified phenylglyoxal

1990

Tedeschi, G.; Negri, A.; Biondi, P.A.; Secchi, C.; Ronchi, S.

Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York

-

189-192

391721

2901415

The kinetic mechanism of beef kidney D-aspartate oxidase

1988

Negri, A.; Massey, V.; Williams, C.H.; Schopfer, L.M.

J. Biol. Chem.

263

13557-13563

391722

3611051

D-Aspartate oxidase from beef kidney. Purification and properties

1987

Negri, A.; Massey, V.; Williams, C.H.

J. Biol. Chem.

262

10026-10034

391723

6151397

Thiazolidine-2-carboxylate derivatives formed from glyoxylate and L-cysteine or L-cysteinylglycine as possible physiological substrates for D-aspartate oxidase

1984

Burns, C.L.; Main, D.E.; Buckthal, D.J.; Hamilton, G.A.

Biochem. Biophys. Res. Commun.

125

1039-1045

391724

7049247

The mammalian enzyme which replaces B protein of E.coli quinolinate synthetase is D-aspartate oxidase

1982

Nasu, S.; Wicks, F.D.; Gholson, R.K.

Biochim. Biophys. Acta

704

240-252

391725

7285908

Oxidation of meso-diaminosuccinic acid, a possible natural substrate for D-aspartate oxidase

1981

Rinaldi, A.; Pellegrini, M.; Crifo, C.; de Marco, C.

Eur. J. Biochem.

117

635-638

391726

236180

D-Asparatate oxidase in the thyroid gland

1975

Jaroszewicz, L.

Enzyme

20

80-89

391727

6060479

D-aspartate oxidase of kidney

1967

Dixon, M.; Kenworthy, P.

Biochim. Biophys. Acta

146

54-76

391728

-

On the prosthetic group of the D-aspartic oxidase

1950

Still, J.L.; Sperling, E.

J. Biol. Chem.

182

585-589

391754

-

Studies on the metabolism of D-amino acid in microorganisms. Part 4. On the nature of the purified D-glutamic-aspartic oxidase of Aspergillus ustus

1957

Mitzushima, S

J. Gen. Appl. Microbiol.

3

233-239

391755

14481396

Mutants of Neurospora deficient in D-amio-acid oxidase

1962

Onishi, E.; Macleod, H.; Horowitz, N.H.

J. Biol. Chem.

237

138-142

391830

-

Immobilized D-amino acid oxidase. Preparation, some enzymatic properties, and potential uses

1974

Tosa, T.; Sano, R.; Chibata, I.

Agric. Biol. Chem.

38

1529-1534

394966

11823469

Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase

2002

Satomura, T.; Kawakami, R.; Sakuraba, H.; Ohshima, T.

J. Biol. Chem.

277

12861-12867

395286

4387700

Purification and properties of D-glutamate oxidase from Candida boidinii 2201

1998

Fukunaga, S.; Yno, S.; Takahashi, M.; Taguchi, S.; Kera, Y.; Odani, S.; Yamada, R.H.

J. Ferment. Bioeng.

85

579-583

395287

-

D-Glutamtoxydase aus der Antennendruse des Flusskrebses Orconectes limosus: Reinigung und Charakterisierung

1968

Urich, K.

Z. Naturforsch. B

23

1508-1511

395288

13583997

Purification and properties of D-glutamic acid oxidase from Octopus vulgaris Lam.

1958

Rocca, E.; Ghiretti, F.

Arch. Biochem. Biophys.

77

336-349

485858

99635

Aspartate carbamyltransferase (Streptococcus faecalis)

1978

Chang, T.Y.; Prescott, L.M.; Jones, M.E.

Methods Enzymol.

51

41-50

636736

4953710

D-Alanine-D-glutamate transaminase. I. Purification and characterization

1965

Martinez-Carrion, M.; Jenkins, W.T.

J. Biol. Chem.

240

3538-3546

636737

5835935

D-Alanine-D-glutamate transaminase. II. Inhibitors and the mechanism of transamination of D-amino acids

1965

Martinez-Carrion, M.; Jenkins, W.T.

J. Biol. Chem.

240

3547-3552

636738

4710577

Occurrence of D-amino acid aminotransferase in pea seedlings

1973

Ogawa, T.; Fukuda, M.

Biochem. Biophys. Res. Commun.

52

998-1002

636742

1158891

D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties

1975

Yonaha, K.; Misono, H.; Yamamoto, T.; Soda, K.

J. Biol. Chem.

250

6983-6989

639962

14189882

Pyridoxamine-oxaloacetic transaminase of rat kidney

1964

Wu, H.L.C.; Mason, M.

J. Biol. Chem.

239

1492-1497

640098

4396841

Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase

1971

Miller, J.E.; Litwack, G.

J. Biol. Chem.

246

3234-3240

640195

3228235

Novel D-amino acid transaminase

1988

Aretz, W.; Sauber, K.

Ann. N. Y. Acad. Sci.

542

366-370

649148

11679741

Crystallization and preliminary X-ray analysis of aspartate racemase from Pyrococcus horikoshii OT3

2001

Liu, L.; Iwata, K.; Kawarabayasi, Y.; Kikuchi, H.; Kita, A.; Yohda, M.; Miki, K.

Acta Crystallogr. Sect. D

57

1674-1676

649266

10800598

L-aspartase: new tricks from an old enzyme

2000

Viola, R.E.

Adv. Enzymol. Relat. Areas Mol. Biol.

74

295-341

649759

12713441

The mcyF gene of the microcystin biosynthetic gene cluster from Microcystis aeruginosa encodes an aspartate racemase

2003

Sielaff, H.; Dittmann, E.; Tandeau De Marsac, N.; Bouchier, C.; Von Dohren, H.; Borner, T.; Schwecke, T.

Biochem. J.

373

909-916

650892

12568809

Purification and characterization of aspartate racemase from the bivalve mollusk Scapharca broughtonii

2003

Shibata, K.; Watanabe, T.; Yoshikawa, H.; Abe, K.; Takahashi, S.; Kera, Y.; Yamada, R.H.

Comp. Biochem. Physiol. B

134

307-314

650894

12670796

Nucleotides modulate the activity of aspartate racemase of Scapharca broughtonii

2003

Shibata, K.; Watanabe, T.; Yoshikawa, H.; Abe, K.; Takahashi, S.; Kera, Y.; Yamada, R.H.

Comp. Biochem. Physiol. B

134

713-719

651785

11432787

A novel alpha-amino-acid esterase from Bacillus mycoides capable of forming peptides of DD- and DL-configurations

2001

Sugihara, A.; Shimada, Y.; Sugihara, S.; Nagao, T.; Watanabe, Y.; Tominaga, Y.

J. Biochem.

130

119-126

652886

12051922

Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization

2002

Liu, L.; Iwata, K.; Kita, A.; Kawarabayasi, Y.; Yohda, M.; Miki, K.

J. Mol. Biol.

319

479-489

654786

15701048

D-Amino acid oxidase: structure, catalytic mechanism, and practical application

2005

Tishkov, V.I.; Khoronenkova, S.V.

Biochemistry

70

40-54

654898

15450847

On the mechanism of Rhodotorula gracilis D-amino acid oxidase: role of the active site serine 335

2004

Boselli, A.; Piubelli, L.; Molla, G.; Sacchi, S.; Pilone, M.S.; Ghisla, S.; Pollegioni, L.

Biochim. Biophys. Acta

1702

19-32

655928

15115779

Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme

2004

Takahashi, S.; Takahashi, T.; Kera, Y.; Matsunaga, R.; Shibuya, H.; Yamada, R.H.

J. Biochem.

135

533-540

656415

12541299

Distribution and characteristics of D-amino acid and D-aspartate oxidases in fish tissues

2003

Sarower, M.G.; Matsui, T.; Abe, H.

J. Exp. Zool. A

295

151-159

657350

-

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Changes in D-aspartic acid and D-glutamic acid levels in the tissues and physiological fluids of mice with various D-aspartate oxidase activities

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Diversity of D-amino acid utilizing bacteria from Kongsfjorden, Arctic, and the metabolic pathways for seven D-amino acids

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AtDAT1 is a key enzyme of D-amino acid stimulated ethylene production in Arabidopsis thaliana

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Characterization and improvement of substrate-binding affinity of D-aspartate oxidase of the thermophilic fungus Thermomyces dupontii

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Appl. Microbiol. Biotechnol.

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Rat D-aspartate oxidase is more similar to the human enzyme than the mouse enzyme

2018

Katane, M.; Kuwabara, H.; Nakayama, K.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Homma, H.

Biochim. Biophys. Acta

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Biochemical characterization of d-aspartate oxidase from Caenorhabditis elegans its potential use in the determination of free D-glutamate in biological samples

2020

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Biochemical characterization of mouse D-aspartate oxidase

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Structure and kinetic properties of human D-aspartate oxidase, the enzyme-controlling D-aspartate levels in brain

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Biochemical characterization of D-aspartate oxidase from Caenorhabditis elegans its potential use in the determination of free D-glutamate in biological samples

2020

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Biochim. Biophys. Acta Proteins Proteom.

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