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Ligand anthranilic acid

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

tryptophan metabolism

KEGG

Aminobenzoate degradation, Benzoic acid family, Biosynthesis of alkaloids derived from shikimate pathway, Biosynthesis of amino acids, Biosynthesis of phenylpropanoids, Biosynthesis of plant hormones, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of various alkaloids, Biosynthesis of various antibiotics, Biosynthesis of various other secondary metabolites, Biosynthesis of various plant secondary metabolites, Degradation of aromatic compounds, Dioxin degradation, Microbial metabolism in diverse environments, Phenazine biosynthesis, Phenylalanine, tyrosine and tryptophan biosynthesis, Tryptophan metabolism more

MetaCyc

2-heptyl-3-hydroxy-4(1H)-quinolone biosynthesis, 2-nitrobenzoate degradation II, 4-hydroxy-2(1H)-quinolone biosynthesis, 5-N-acetylardeemin biosynthesis, acetylaszonalenin biosynthesis, acridone alkaloid biosynthesis, anthranilate degradation I (aerobic), anthranilate degradation II (aerobic), anthranilate degradation III (anaerobic), anthranilate degradation IV (aerobic), antimycin biosynthesis, asperlicin E biosynthesis, aurachin A, B, C and D biosynthesis, aurachin RE biosynthesis, benzoylanthranilate biosynthesis, carbazole degradation, des-methyl avenacin A-1 biosynthesis, fumiquinazoline D biosynthesis, indole degradation to anthranil and anthranilate, indole-3-acetate degradation II, L-tryptophan biosynthesis, L-tryptophan degradation I (via anthranilate), L-tryptophan degradation XI (mammalian, via kynurenine), N-methylanthraniloyl-beta-D-glucopyranose biosynthesis, quinolinone B biosynthesis, viridicatin biosynthesis more

Show all BRENDA pathways known for anthranilic acid

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (20 results)

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Show Natural Substrate (20 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.12.1

anthranilate + NADPH + H+ + O2 = catechol + CO2 + NADP+ + NH3

743231

-

1.14.12.1

anthranilic acid + alanine + O2 = catechol + CO2 + NH3 + ?

659034

-

1.14.12.1

anthranilic acid + NAD(P)H + O2 + H2O = catechol + CO2 + NAD(P)+ + NH3

439106, 439107, 396140, 439112, 439108, 439110, 439109, 659053, 657969, 659034

-

1.14.12.1

3 entries

1.14.13.35

anthranilate + NADPH + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3

4583, 4575

-

1.7.1.17

anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD+ = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH + 2 H+

765875

-

2.1.1.111

S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + N-methylanthranilate

485120, 485122, 689543, 485121

-

2.1.1.274

S-adenosyl-L-methionine + anthranilate = ?

726129

-

2.1.1.277

S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + O-methyl anthranilate

723460, 758244

-

2.3.1.118

acetyl-CoA + o-aminobenzoic acid = CoA + N-acetyl-o-aminobenzoic acid

486161

-

2.3.1.144

benzoyl-CoA + anthranilate = CoA + N-benzoylanthranilate

485081

-

2.3.1.144

coumaroyl-CoA + anthranilate = CoA + N-(4-hydroxycinnamoyl)-anthranilate

718662

-

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

760106, 759160, 680670, 735669, 759106, 759199, 638665, 638670, 638671, 638675, 638663, 638667, 638674, 638666, 638664, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 651722, 660181, 680467, 693629, 724752

1zyk, 3D-view

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

760106, 759160, 680670, 735669, 759106, 759199, 638665, 638670, 638671, 638675, 638663, 638667, 638674, 638666, 638664, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 651722, 660181, 680467, 693629, 724752

2gvq, 3D-view

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

760106, 759160, 680670, 735669, 759106, 759199, 638665, 638670, 638671, 638675, 638663, 638667, 638674, 638666, 638664, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 651722, 660181, 680467, 693629, 724752

4owv, 3D-view

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

760106, 759160, 680670, 735669, 759106, 759199, 638665, 638670, 638671, 638675, 638663, 638667, 638674, 638666, 638664, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 651722, 660181, 680467, 693629, 724752

4x5d, 3D-view

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

760106, 759160, 680670, 735669, 759106, 759199, 638665, 638670, 638671, 638675, 638663, 638667, 638674, 638666, 638664, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 651722, 660181, 680467, 693629, 724752

4x5e, 3D-view

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

760106, 759160, 680670, 735669, 759106, 759199, 638665, 638670, 638671, 638675, 638663, 638667, 638674, 638666, 638664, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 651722, 660181, 680467, 693629, 724752

4yi7, 3D-view

6.2.1.32

ATP + anthranilate + CoA = AMP + diphosphate + anthraniloyl-CoA

744708

-

6.2.1.32

ATP + anthranilate + CoA = AMP + diphosphate + anthranilyl-CoA

438854, 438855, 713, 438858, 692840

-

2.3.1.144

2 entries

2.4.2.18

6 entries

6.2.1.32

2 entries

6.3.2.40

2 ATP + S-adenosyl-L-methionine + anthranilate + L-phenylalanine = cyclopeptine + 2 AMP + 2 diphosphate + S-adenosyl-L-homocysteine

765012, 765546

-

In Vivo Product in Enzyme-catalyzed Reactions (16 results)

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Show Natural Product (16 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.23

2,3-dihydroxyindole + O2 = anthranilate + CO2

439539

-

1.7.1.17

2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH + 2 H+ = anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD+

0

-

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

1zyk, 3D-view

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

2gvq, 3D-view

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

4owv, 3D-view

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

4x5d, 3D-view

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

4x5e, 3D-view

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

4yi7, 3D-view

2.4.2.18

6 entries

3.1.2.23

2-aminobenzoyl-CoA + H2O = 2-aminobenzoate + CoA

0

-

3.5.1.9

N-formylanthranilic acid + H2O = formate + anthranilic acid

209260, 209250, 209262, 209259, 209261, 209249, 209258, 209248

-

3.5.5.1

2-aminobenzonitrile + 2 H2O = 2-aminobenzoic acid + NH3

0

-

3.7.1.3

L-kynurenine + H2O = anthranilate + L-alanine

289268, 289278, 0, 34546, 289260, 289277, 289280, 289281, 289282, 289287, 289261, 289267, 289284, 289258, 289259, 289265, 289269, 289264, 289266, 289276, 289279, 289283, 289285, 289286, 289288, 289263, 289273, 289272

-

4.1.3.27

chorismate + ammonia = anthranilate + pyruvate + H2O

0

-

4.1.3.27

chorismate + L-Gln = anthranilate + pyruvate + L-glutamate

0

-

4.1.3.27

chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate

0

-

4.1.3.27

chorismate + NH4+ = anthranilate + pyruvate + H2O

0

-

4.1.3.27

4 entries

Substrate in Enzyme-catalyzed Reactions (66 results)

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Show Substrate (66 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.12.1

anthranilate + NADPH + H+ + O2 = catechol + CO2 + NADP+ + NH3

743231

-

1.14.12.1

anthranilic acid + alanine + O2 = ?

659034

-

1.14.12.1

anthranilic acid + alanine + O2 = catechol + CO2 + NH3 + ?

659034

-

1.14.12.1

anthranilic acid + NAD(P)H + O2 + H2O = catechol + CO2 + NAD(P)+ + NH3

439106, 439107, 396140, 439112, 439108, 439110, 439109, 659034, 659053, 657969

-

1.14.12.1

anthranilic acid + NADH + O2 + H2O = catechol + CO2 + NAD+ + NH3

657969

-

1.14.12.13

2-aminobenzoate + NADH + O2 = ? + NAD+ + CO2

439074

-

1.14.12.13

anthranilate + NADH + O2 = catechol + ? + NAD+ + CO2

439074

-

1.14.12.1

5 entries

1.14.12.13

2 entries

1.14.13.1

anthranilate + NADH + 2 H+ + O2 = 2-aminophenol + NAD+ + H2O + CO2

684569

-

1.14.13.172

anthranilate + NADH + H+ + O2 = 5-hydroxyanthranilate + NAD+ + H2O

743932

-

1.14.13.27

anthranilate + NAD(P)H + O2 = 2-hydroxyaniline + NAD(P)+ + H2O2 + CO2

438911, 438909

-

1.14.13.35

anthranilate + NADPH + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3

4583, 438867, 438873, 438874, 438875, 438876, 438877, 4575, 396426, 438868, 438866

-

1.14.14.8

anthranilate + FADH2 + O2 = 3-hydroxyanthranilate + FAD

709852

-

1.14.14.8

anthranilate + FADH2 + O2 = 3-hydroxyanthranilate + FAD + H2O

709852

-

1.14.14.8

2 entries

1.14.19.58

anthranilate + FADH2 + chloride + O2 + H+ = 5-chloro-anthranilate + FAD + 2 H2O

744705

-

1.14.19.59

anthranilate + FADH2 + chloride + O2 + H+ = 5-chloro-anthranilate + FAD + 2 H2O

744705

-

1.7.1.17

anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD+ = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH + 2 H+

765875

-

2.1.1.111

S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + N-methylanthranilate

485120, 485121, 485122, 757422, 689543

-

2.1.1.273

S-adenosyl-L-methionine + anthranilate = methyl anthranilate + S-adenosyl-L-homocysteine

757953

-

2.1.1.273

S-adenosyl-L-methionine + anthranilic acid = S-adenosyl-L-homocysteine + methyl anthranilate

723416

-

2.1.1.274

S-adenosyl-L-methionine + anthranilate = ?

726129

-

2.1.1.274

S-adenosyl-L-methionine + anthranilate = methyl anthranilate + S-adenosyl-L-homocysteine

757953

-

2.1.1.274

S-adenosyl-L-methionine + anthranilic acid = S-adenosyl-L-homocysteine + methyl anthranilate

723416

-

2.1.1.273

2 entries

2.1.1.274

3 entries

2.1.1.277

S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + O-methyl anthranilate

723460, 758244

-

2.1.1.B126

S-adenosyl-L-methionine + anthranilate = methyl anthranilate + S-adenosyl-L-homocysteine

758090

-

2.3.1.113

malonyl-CoA + anthranilate = CoA + N-malonylanthranilate

486140

-

2.3.1.118

acetyl-CoA + o-aminobenzoic acid = CoA + N-acetyl-o-aminobenzoic acid

486161

-

2.3.1.144

2,3-dimethoxycinnamoyl-CoA + anthranilate = CoA + N-(2,3-dimethoxycinnamoyl)-anthranilate

718662

-

2.3.1.144

2,4-dimethoxycinnamoyl-CoA + anthranilate = CoA + N-(2,4-dimethoxycinnamoyl)-anthranilate

718662

-

2.3.1.144

2,5-dimethoxycinnamoyl-CoA + anthranilate = CoA + N-(2,5-dimethoxycinnamoyl)-anthranilate

718662

-

2.3.1.144

2-coumaroyl-CoA + anthranilate = CoA + N-(2-coumaroyl)anthranilate

718662

-

2.3.1.144

3,4,5-trimethoxycinnamoyl-CoA + anthranilate = CoA + N-(3,4,5-trimethoxycinnamoyl)-anthranilate

718662

-

2.3.1.144

3-coumaroyl-CoA + anthranilate = CoA + N-(3-hydroxycinnamoyl)-anthranilate

718662

-

2.3.1.144

3-hydroxy-4-methoxycinnamoyl-CoA + anthranilate = CoA + N-(3-hydroxy-4-methoxycinnamoyl)-anthranilate

718662

-

2.3.1.144

3-methoxycinnamoyl-CoA + anthranilate = CoA + N-(3-methoxycinnamoyl)-anthranilate

718662

-

2.3.1.144

4-coumaroyl-CoA + anthranilate = CoA + N-(4-coumaroyl)-anthranilate

718662

-

2.3.1.144

4-coumaroyl-CoA + anthranilate = CoA + N-4-(coumaroyl)anthranilate

736747, 486330

-

2.3.1.144

4-methoxycinnamoyl-CoA + anthranilate = CoA + N-(4-methoxycinnamoyl)-anthranilate

718662

-

2.3.1.144

benzoyl-CoA + anthranilate = CoA + N-benzoylanthranilate

736747, 485081, 486330

-

2.3.1.144

caffeoyl-CoA + anthranilate = CoA + N-(3,4-dihydroxycinnamoyl)-anthranilate

718662

-

2.3.1.144

cinnamoyl-CoA + anthranilate = CoA + N-cinnamoylanthranilate

718662, 486330

-

2.3.1.144

coumaroyl-CoA + anthranilate = CoA + N-(4-hydroxycinnamoyl)-anthranilate

718662

-

2.3.1.144

feruloyl-CoA + anthranilate = CoA + N-feruloylanthranilate

718662

-

2.3.1.144

salicyl-CoA + anthranilate = CoA + N-salicylanthranilate

486330

-

2.3.1.144

sinapoyl-CoA + anthranilate = CoA + N-sinapoylanthranilate

718662

-

2.3.1.144

18 entries

2.3.1.302

p-coumaroyl-CoA + anthranilate = avenanthramide D + CoA

762520, 761938

-

2.3.1.5

acetyl-CoA + 2-aminobenzoic acid = CoA + N-acetyl-2-aminobenzoic acid

686079, 687848

-

2.3.1.5

acetyl-CoA + 2-aminobenzoic acid = CoA + N-acetylanthranilate

487115

-

2.3.1.5

2 entries

2.4.1.120

UDP-alpha-D-glucose + anthranilic acid = UDP + 1-O-anthraniloyl-beta-D-glucose

488516

-

2.4.1.17

2-aminobenzoate + UDPglucuronate = UDP + ?

488748

-

2.4.1.177

anthranilic acid + UDP-glucose = ?

694768

-

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

638665, 638670, 638671, 638675, 760106, 759160, 638663, 638667, 638674, 638666, 638664, 660181, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 680670, 702308, 724752, 735669, 759106, 759199, 651722, 680467, 693629, 721132

1zyk, 3D-view

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

638665, 638670, 638671, 638675, 760106, 759160, 638663, 638667, 638674, 638666, 638664, 660181, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 680670, 702308, 724752, 735669, 759106, 759199, 651722, 680467, 693629, 721132

2gvq, 3D-view

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

638665, 638670, 638671, 638675, 760106, 759160, 638663, 638667, 638674, 638666, 638664, 660181, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 680670, 702308, 724752, 735669, 759106, 759199, 651722, 680467, 693629, 721132

4owv, 3D-view

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

638665, 638670, 638671, 638675, 760106, 759160, 638663, 638667, 638674, 638666, 638664, 660181, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 680670, 702308, 724752, 735669, 759106, 759199, 651722, 680467, 693629, 721132

4x5d, 3D-view

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

638665, 638670, 638671, 638675, 760106, 759160, 638663, 638667, 638674, 638666, 638664, 660181, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 680670, 702308, 724752, 735669, 759106, 759199, 651722, 680467, 693629, 721132

4x5e, 3D-view

2.4.2.18

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

638665, 638670, 638671, 638675, 760106, 759160, 638663, 638667, 638674, 638666, 638664, 660181, 4599, 638672, 638680, 638677, 638679, 638678, 638676, 638668, 638669, 680670, 702308, 724752, 735669, 759106, 759199, 651722, 680467, 693629, 721132

4yi7, 3D-view

2.4.2.18

6 entries

2.5.1.2

thiamine + o-aminobenzoic acid = 4-methyl-5-(2-hydroxyethyl)-thiazole + 2-[[(4-amino-2-methylpyrimidin-5-yl)methyl]amino]benzoic acid

636851

-

2.7.7.97

ATP + anthranilate = ?

740654

-

4.1.1.24

2-Aminobenzoate = Aniline + CO2

4191

-

6.2.1.2

ATP + 2-aminobenzoate + CoA = AMP + diphosphate + 2-aminobenzoyl-CoA

650334

-

6.2.1.25

ATP + 2-aminobenzoate + CoA = AMP + diphosphate + 2-aminobenzoyl-CoA

710, 709, 715, 744341, 651721, 713, 649526, 662906, 662016, 675454, 673729

-

6.2.1.32

ATP + anthranilate + CoA = AMP + diphosphate + anthraniloyl-CoA

744708

-

6.2.1.32

ATP + anthranilate + CoA = AMP + diphosphate + anthranilyl-CoA

692840, 438854, 438855, 713, 438858

-

6.2.1.32

ATP + CoA + anthranilate = AMP + diphosphate + anthranilyl-CoA

713, 438854, 438858, 438855

-

6.2.1.32

3 entries

6.2.1.71

ATP + anthranilate = diphosphate + anthranylyl-adenylate

760609

-

6.3.2.40

2 ATP + S-adenosyl-L-methionine + anthranilate + L-phenylalanine = cyclopeptine + 2 AMP + 2 diphosphate + S-adenosyl-L-homocysteine

765012, 765546

-

Product in Enzyme-catalyzed Reactions (49 results)

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Show Product (49 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.17

indole + O2 = anthranilic acid

395577, 395575, 395576, 395579, 395578

-

1.13.11.17

o-aminobenzaldehyde + O2 = anthranilic acid

395579

-

1.13.11.17

2 entries

1.13.11.23

2,3-dihydroxyindole + O2 = anthranilate + CO2

439539

-

1.2.7.5

2-aminobenzaldehyde + H2O + 2 oxidized benzyl viologen = 2-aminobenzoate + 2 H+ + 2 reduced benzyl viologen

0

-

1.7.1.17

2-(4-dimethylaminophenylazo) benzoic acid + NADH + H+ = N,N'-dimethyl-p-phenylenediamine + 2-aminobenzoic acid + NAD+

0

-

1.7.1.17

4'-(diethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+ = 2-aminobenzoic acid + N,N-diethyl-p-phenylenediamine + 2 NAD+

0

-

1.7.1.17

4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+ = 2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NAD+

0

-

1.7.1.17

4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADPH + 2 H+ = 2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NADP+

0

-

1.7.1.17

Methyl Red + NADH + H+ = 2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NAD+

0

-

1.7.1.17

2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH + 2 H+ = anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD+

0

-

1.7.1.17

ethyl red + 2 NADH + 2 H+ = anthranilate + N,N-diethyl-1,4-phenylenediamine + 2 NAD+

0

-

1.7.1.6

2-[4-(dimethylamino)phenylazo]benzoic acid + NADH = 2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NAD+

0

-

1.7.1.6

2-[4-(dimethylamino)phenylazo]benzoic acid + NADPH = N,N-dimethyl-p-phenylenediamine + 2-aminobenzoic acid + NADP+

0

-

1.7.1.6

4'-dimethylaminoazobenzene-2-carboxylic acid + NADH + H+ = 2-aminobenzoic acid + N,N'-dimethyl-p-phenylenediamine + NAD+

0

-

1.7.1.6

methyl red + 2 NADH + 2 H+ = 2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + 2 NAD+

0

-

1.7.1.6

methyl red + 2 NADH + 2 H+ = N,N-dimethyl-p-phenylenediamine + 2-aminobenzoic acid + 2 NAD+

0

-

1.7.1.6

methyl red + NADH = 2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NAD+

0

-

1.7.1.6

Methyl Red + NADPH + H+ = 2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NADP+

0

-

1.7.1.6

2'-carboxy-4-N,N-dimethylazobenzene + NAD(P)H = 2-carboxy-1-phenylamine + N,N-dimethyl-1,4-phenylenediamine + NADP+

394296

-

1.7.1.6

4-dimethylaminoazobenzene-2'-carboxylic acid + 2 NADH + 2 H+ = anthranilate + N,N'-dimethylaminoaniline + 2 NAD+

0

-

1.7.1.6

4-dimethylaminoazobenzene-2'-carboxylic acid + 2 NADPH + 2 H+ = anthranilate + N,N'-dimethylamino-aniline + 2 NADP+

0

-

1.7.1.6

methyl red + 2 NADH + 2 H+ = anthranilate + 4-amino-N,N-dimethylaniline + 2 NAD+

0

-

1.7.1.6

methyl red + 2 NADH + 2 H+ = anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD+

0

-

1.7.1.6

methyl red + 2 NADH + 2 H+ = o-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NAD+

0

-

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

1zyk, 3D-view

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

2gvq, 3D-view

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

4owv, 3D-view

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

4x5d, 3D-view

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

4x5e, 3D-view

2.4.2.18

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate

0

4yi7, 3D-view

1.7.1.17

7 entries

1.7.1.6

13 entries

2.4.2.18

6 entries

3.1.1.1

methyl 2-aminobenzoate + H2O = methanol + 2-aminobenzoate

652371

-

3.1.2.23

2-aminobenzoyl-CoA + H2O = 2-aminobenzoate + CoA

0

-

3.5.1.11

2-nitro-5-phenylacetamidobenzoic acid + H2O = phenylacetate + 2-aminobenzoic acid

0

-

3.5.1.11

2-phenylacetamidobenzoic acid + H2O = phenylacetate + 2-aminobenzoic acid

0

-

3.5.1.11

phenylacetylanthranilic acid + H2O = phenylacetate + 2-aminobenzoic acid

171890

-

3.5.1.4

2-aminobenzamide + H2O = 2-aminobenzoic acid + NH3

0

-

3.5.1.4

anthranilamide + H2O = anthranilate + NH3

0

-

3.5.1.9

N-acetylanthranilic acid + H2O = acetate + anthranilic acid

209259

-

3.5.1.9

N-formylanthranilic acid + H2O = formate + anthranilic acid

209260, 209250, 209262, 209259, 209261, 209249, 209258, 209248

-

3.5.5.1

2-amino-benzonitrile + H2O = 2-aminobenzoic acid + NH3

0

-

3.5.5.1

2-aminobenzonitrile + 2 H2O = 2-aminobenzoic acid + NH3

0

-

3.5.1.11

3 entries

3.5.1.4

2 entries

3.5.1.9

2 entries

3.5.5.1

2 entries

3.7.1.13

2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate + H2O = anthranilate + 2-hydroxypenta-2,4-dienoate

0

-

3.7.1.3

L-kynurenine + H2O = anthranilate + L-alanine

289268, 289278, 0, 34546, 289260, 289277, 289280, 289281, 289282, 289287, 289261, 289267, 289284, 289258, 289259, 289265, 289269, 289264, 289266, 289276, 289279, 289283, 289285, 289286, 289288, 289263, 289273, 289272

-

3.7.1.8

2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid + H2O = 2-aminobenzoic acid + 2-hydroxypenta-2,4-dienoic acid

0

-

4.1.3.27

chorismate + ammonia = anthranilate + pyruvate + H2O

0

-

4.1.3.27

chorismate + L-Gln = anthranilate + pyruvate + L-glutamate

33279, 33283, 33284, 33301, 33303, 33304, 33308, 33311, 33276, 33306, 33310, 33289, 4604, 33296, 33297, 33299, 0, 33302, 33312, 33281, 33286, 33294, 33300, 33282, 33278, 33295, 33298, 33309, 33280, 33287, 33293, 33288, 33290, 33307, 33313, 33291, 33292, 33305, 33277

-

4.1.3.27

chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate

650576, 0, 649565

-

4.1.3.27

chorismate + NH3 = anthranilate + pyruvate + H2O

0

-

4.1.3.27

chorismate + NH4+ = anthranilate + pyruvate + H2O

0

-

4.1.3.27

5 entries

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.35

induces, the enzyme activity increases with an increase in the concentration of anthranilate in the growth medium, optimal amounts of the enzyme are synthesized when the concentration of anthranilate is 1 mg/ml, further increase in the concentration results in a considerable decrease in the growth of the organism as well in the enzyme activity

438876

-

Inhibitor in Enzyme-catalyzed Reactions (59 results)

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Show Inhibitors (59 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.4

-

713565

-

1.10.3.4

competitive

396432

-

1.10.3.4

2 entries

1.13.11.6

competitive inhibition

658927

-

1.13.12.9

-

698757

2yr6, 3D-view

1.14.13.9

22% inhibition at 2 mM and 11% inhibition at 0.2 mM

348521

-

1.2.1.30

competitive inhibitor with benzoic acid as a substrate

288184

-

1.4.3.2

three and two binding sites in isoforms L1 and L2, respectively

692288

1f8s, 3D-view

1.4.3.2

three and two binding sites in isoforms L1 and L2, respectively

692288

2jb3, 3D-view

1.4.3.2

-

669894

1f8s, 3D-view

1.4.3.2

-

669894

2jb3, 3D-view

1.4.3.2

competitive

391815

1f8s, 3D-view

1.4.3.2

competitive

391815

2jb3, 3D-view

1.4.3.2

-

391799

1f8s, 3D-view

1.4.3.2

-

391799

2jb3, 3D-view

1.4.3.2

LAO inhibitor, slightly inhibiting the degradation of fibrinogen

698669

1f8s, 3D-view

1.4.3.2

LAO inhibitor, slightly inhibiting the degradation of fibrinogen

698669

2jb3, 3D-view

1.4.3.3

about 35% inhibition at 0.2 mM

743863

1an9, 3D-view

1.4.3.3

about 35% inhibition at 0.2 mM

743863

1c0i, 3D-view

1.4.3.3

about 35% inhibition at 0.2 mM

743863

2e4a, 3D-view

1.4.3.3

-

391866, 723920, 724965

1an9, 3D-view

1.4.3.3

-

391866, 723920, 724965

1c0i, 3D-view

1.4.3.3

-

391866, 723920, 724965

2e4a, 3D-view

1.4.3.3

83.3% residual activity at 10 mM

741688

1an9, 3D-view

1.4.3.3

83.3% residual activity at 10 mM

741688

1c0i, 3D-view

1.4.3.3

83.3% residual activity at 10 mM

741688

2e4a, 3D-view

1.4.3.2

10 entries

1.4.3.3

9 entries

2.1.1.139

75% activity left at 1.1 mM

288658

-

2.4.2.10

weak

489718

-

2.4.2.18

substrate inhibition

735636, 735688

1zyk, 3D-view

2.4.2.18

substrate inhibition

735636, 735688

2gvq, 3D-view

2.4.2.18

substrate inhibition

735636, 735688

4owv, 3D-view

2.4.2.18

substrate inhibition

735636, 735688

4x5d, 3D-view

2.4.2.18

substrate inhibition

735636, 735688

4x5e, 3D-view

2.4.2.18

substrate inhibition

735636, 735688

4yi7, 3D-view

2.4.2.18

substrate inhibition above 0.008 mM

638669

1zyk, 3D-view

2.4.2.18

substrate inhibition above 0.008 mM

638669

2gvq, 3D-view

2.4.2.18

substrate inhibition above 0.008 mM

638669

4owv, 3D-view

2.4.2.18

substrate inhibition above 0.008 mM

638669

4x5d, 3D-view

2.4.2.18

substrate inhibition above 0.008 mM

638669

4x5e, 3D-view

2.4.2.18

substrate inhibition above 0.008 mM

638669

4yi7, 3D-view

2.4.2.18

substrate inhibition. Concentrations above 0.004 mM result in reduced enzymatic activity

759199

1zyk, 3D-view

2.4.2.18

substrate inhibition. Concentrations above 0.004 mM result in reduced enzymatic activity

759199

2gvq, 3D-view

2.4.2.18

substrate inhibition. Concentrations above 0.004 mM result in reduced enzymatic activity

759199

4owv, 3D-view

2.4.2.18

substrate inhibition. Concentrations above 0.004 mM result in reduced enzymatic activity

759199

4x5d, 3D-view

2.4.2.18

substrate inhibition. Concentrations above 0.004 mM result in reduced enzymatic activity

759199

4x5e, 3D-view

2.4.2.18

substrate inhibition. Concentrations above 0.004 mM result in reduced enzymatic activity

759199

4yi7, 3D-view

2.4.2.18

18 entries

2.6.1.7

weak inhibition

636623

-

2.7.7.48

-

759516

-

3.5.1.9

-

743358

-

3.5.1.9

29% inhibition at 1-2 mM

209242

-

3.5.1.9

45% inhibition at 0.5 mM

209258

-

3.5.1.9

9% inhibition at 0.5-1 mM

209242

-

3.5.1.9

Ki: 1.6 mM

209250

-

3.7.1.3

-

289267, 289286

-

3.7.1.3

1 mM

289266

-

3.5.1.9

5 entries

3.7.1.3

2 entries

4.1.1.46

-

4574

-

4.1.1.55

competitive

4714

-

4.1.3.27

-

33293

-

4.1.3.27

i.e. ortho-aminobenzoate

747843

-

4.1.3.27

2 entries

4.1.99.1

competitive

37354

-

3D Structure of Enzyme-Ligand-Complex (PDB) (94 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (94 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.13.12.9

2yr6, 3D-view

1.4.3.2

1f8s, 3D-view

1.4.3.2

2jb3, 3D-view

1.4.3.2

1f8s, 3D-view

1.4.3.2

2jb3, 3D-view

1.4.3.2

1f8s, 3D-view

1.4.3.2

2jb3, 3D-view

1.4.3.2

1f8s, 3D-view

1.4.3.2

2jb3, 3D-view

1.4.3.2

1f8s, 3D-view

1.4.3.2

2jb3, 3D-view

1.4.3.2

1f8s, 3D-view

1.4.3.2

2jb3, 3D-view

1.4.3.2

1f8s, 3D-view

1.4.3.2

2jb3, 3D-view

1.4.3.2

1f8s, 3D-view

1.4.3.2

2jb3, 3D-view

1.4.3.3

1an9, 3D-view

1.4.3.3

1c0i, 3D-view

1.4.3.3

2e4a, 3D-view

1.4.3.3

1an9, 3D-view

1.4.3.3

1c0i, 3D-view

1.4.3.3

2e4a, 3D-view

1.4.3.3

1an9, 3D-view

1.4.3.3

1c0i, 3D-view

1.4.3.3

2e4a, 3D-view

1.4.3.3

1an9, 3D-view

1.4.3.3

1c0i, 3D-view

1.4.3.3

2e4a, 3D-view

1.4.3.3

1an9, 3D-view

1.4.3.3

1c0i, 3D-view

1.4.3.3

2e4a, 3D-view

1.4.3.3

1an9, 3D-view

1.4.3.3

1c0i, 3D-view

1.4.3.3

2e4a, 3D-view

1.4.3.3

1an9, 3D-view

1.4.3.3

1c0i, 3D-view

1.4.3.3

2e4a, 3D-view

1.4.3.3

1an9, 3D-view

1.4.3.3

1c0i, 3D-view

1.4.3.3

2e4a, 3D-view

1.4.3.2

16 entries

1.4.3.3

24 entries

1.8.3.7

6s07, 3D-view

2.3.1.180

3h78, 3D-view

2.4.2.18

1zyk, 3D-view

2.4.2.18

2gvq, 3D-view

2.4.2.18

4owv, 3D-view

2.4.2.18

4x5d, 3D-view

2.4.2.18

4x5e, 3D-view

2.4.2.18

4yi7, 3D-view

2.4.2.18

1zyk, 3D-view

2.4.2.18

2gvq, 3D-view

2.4.2.18

4owv, 3D-view

2.4.2.18

4x5d, 3D-view

2.4.2.18

4x5e, 3D-view

2.4.2.18

4yi7, 3D-view

2.4.2.18

1zyk, 3D-view

2.4.2.18

2gvq, 3D-view

2.4.2.18

4owv, 3D-view

2.4.2.18

4x5d, 3D-view

2.4.2.18

4x5e, 3D-view

2.4.2.18

4yi7, 3D-view

2.4.2.18

1zyk, 3D-view

2.4.2.18

2gvq, 3D-view

2.4.2.18

4owv, 3D-view

2.4.2.18

4x5d, 3D-view

2.4.2.18

4x5e, 3D-view

2.4.2.18

4yi7, 3D-view

2.4.2.18

1zyk, 3D-view

2.4.2.18

2gvq, 3D-view

2.4.2.18

4owv, 3D-view

2.4.2.18

4x5d, 3D-view

2.4.2.18

4x5e, 3D-view

2.4.2.18

4yi7, 3D-view

2.4.2.18

1zyk, 3D-view

2.4.2.18

2gvq, 3D-view

2.4.2.18

4owv, 3D-view

2.4.2.18

4x5d, 3D-view

2.4.2.18

4x5e, 3D-view

2.4.2.18

4yi7, 3D-view

2.4.2.18

1zyk, 3D-view

2.4.2.18

2gvq, 3D-view

2.4.2.18

4owv, 3D-view

2.4.2.18

4x5d, 3D-view

2.4.2.18

4x5e, 3D-view

2.4.2.18

4yi7, 3D-view

2.4.2.18

1zyk, 3D-view

2.4.2.18

2gvq, 3D-view

2.4.2.18

4owv, 3D-view

2.4.2.18

4x5d, 3D-view

2.4.2.18

4x5e, 3D-view

2.4.2.18

4yi7, 3D-view

2.4.2.18

48 entries

3.4.19.1

2hu8, 3D-view

3.4.21.26

1e8n, 3D-view

4.1.1.48

3t44, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (46 results)

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Show Turnover Number (46 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.1.1.277

0.37

-

25°C, pH not specified in the publication, isoenzyme AAMT2

723460

2.1.1.277

0.45

-

25°C, pH not specified in the publication, isoenzyme AAMT1

723460

2.4.2.18

-999

-

I36E/M47D double mutant, kcat/KM: 4.8 1/s*microM

693629

2.4.2.18

-999

-

wild-type, kcat/KM: 4.8 1/s*microM

693629

2.4.2.18

0.014

-

25°C

638678

2.4.2.18

0.014

-

at 25°C

638678

2.4.2.18

0.035

-

40°C

638678

2.4.2.18

0.035

-

at 40°C

638678

2.4.2.18

0.046

-

mutant enzyme I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M, pH 7.2, 37°C

724752

2.4.2.18

0.067

-

50°C

638678

2.4.2.18

0.067

-

at 50°C

638678

2.4.2.18

0.105

-

60°C

638678

2.4.2.18

0.105

-

at 60°C

638678

2.4.2.18

0.24

-

wild-type, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.4.2.18

0.28

-

+/-0.06, I36E/M47D double mutant, pH 7.2, 37°C, 0.01 microM subunit concentration

693629

2.4.2.18

0.33

-

wild-type, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.4.2.18

0.34

-

cosubstrate: 5-phospho-alpha-D-ribose 1-diphosphate

638668

2.4.2.18

0.4

-

87°C

638678

2.4.2.18

0.4

-

at 87°C

638678

2.4.2.18

0.41

-

+/-0.04, wild-type, pH 7.2, 37°C, 0.01 microM subunit concentration

693629

2.4.2.18

0.48

-

60°C, pH 7.5, 2 mM Mg2+, mutant enzyme K106Q

680670

2.4.2.18

0.62

-

60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme R164A

680670

2.4.2.18

0.73

-

60°C, pH 7.5, 0.05 mM Mg2+,mutant enzyme R164A/H154A

680670

2.4.2.18

0.78

-

mutant enzyme I36E/M47D/D83G/N109S/F149S, pH 7.2, 37°C

724752

2.4.2.18

1.1

-

60°C, pH 7.5, 2 mM Mg2+, wild-type enzyme

680670

2.4.2.18

1.2

-

mutant enzyme I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M, pH 7.2, 37°C

724752

2.4.2.18

1.2

-

mutant F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.4.2.18

1.3

-

mutant enzyme I36E/M47D/T77I/D83G/F149S, pH 7.2, 37°C

724752

2.4.2.18

2

-

60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A/P178A

680670

2.4.2.18

2

-

mutant D83G, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.4.2.18

2.7

-

mutant enzyme I36E/M47D/D83G/F149S/F193S, pH 7.2, 37°C

724752

2.4.2.18

2.9

-

cosubstrate: 5-phospho-alpha-D-ribose 1-diphosphate

638666

2.4.2.18

3.4

-

mutant enzyme I36E/M47D/D83G/F149S, pH 7.2, 37°C

724752

2.4.2.18

3.5

-

mutant enzyme I36E/M47D/D83G/F149S/I169T, pH 7.2, 37°C

724752

2.4.2.18

3.9

-

mutant enzyme I36E/M47D/D83G/F149S/L320M, pH 7.2, 37°C

724752

2.4.2.18

4.1

-

cosubstrate: 5-phospho-alpha-D-ribose 1-diphosphate

638670, 638671

2.4.2.18

4.2

-

60°C, pH 7.5, 0.05 mM Mg2+, wild-type enzyme

680670

2.4.2.18

4.4

-

-

638667

2.4.2.18

4.4

-

mutant D83G/F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.4.2.18

5.1

-

60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A

680670

2.4.2.18

5.6

-

60°C, pH 7.5, 2 mM Mg2+,mutant enzyme E224Q

680670

2.4.2.18

6

-

60°C, pH 7.5, 2 mM Mg2+,mutant enzyme D223N

680670

2.4.2.18

13.3

-

mutant D83G/F149S, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.1.1.277

2 entries

2.4.2.18

41 entries

6.2.1.25

3.9

-

pH 8.0, 31°C, recombinant wild-type enzyme

744341

6.2.1.32

21.7

-

28°C, isoenzyme E3

713

6.2.1.32

267

-

28°C, isoenzyme E2

713

6.2.1.32

2 entries

K_M Value (59 results)

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Show KM Value (59 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.12.1

0.12

-

-

439109

1.14.13.1

0.028

-

30°C, pH 7.0

684569

1.14.13.35

0.15

-

-

438875, 438877

2.1.1.111

0.007

-

wild-type

689543

2.1.1.111

0.024

-

N298E mutant

689543

2.1.1.277

0.311

-

25°C, pH not specified in the publication, isoenzyme AAMT2

723460

2.1.1.277

0.641

-

25°C, pH not specified in the publication, isoenzyme AAMT1

723460

2.1.1.111

2 entries

2.1.1.277

2 entries

2.3.1.113

0.012

-

-

486140

2.3.1.118

0.48

-

-

486161

2.3.1.144

0.02

-

-

486330

2.3.1.144

0.033

-

-

485081

2.3.1.144

2 entries

2.3.1.302

3.4

-

pH 7, temperature not specified in the publication

762520

2.3.1.5

13

-

-

487115

2.4.1.177

2.74

-

pH 8.0, 21°C

694768

2.4.2.18

0.000005

-

at 87°C, Km decreases at lower temperatures

638678

2.4.2.18

0.000018

-

wild-type, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.4.2.18

0.00002

-

wild-type, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.4.2.18

0.00004

-

60°C, pH 7.5, 0.05 mM Mg2+, wild-type enzyme

680670

2.4.2.18

0.000058

-

I36E/M47D double mutant, pH 7.2, 37°C, 0.01 microM subunit concentration

693629

2.4.2.18

0.00007

-

60°C, pH 7.5, 2 mM Mg2+, wild-type enzyme

680670

2.4.2.18

0.000085

-

wild-type, pH 7.2, 37°C, 0.01 microM subunit concentration

693629

2.4.2.18

0.00012

-

mutant D83G, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.4.2.18

0.00016

-

60°C, pH 7.5, 2 mM Mg2+,mutant enzyme D223N

680670

2.4.2.18

0.00053

-

60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A

680670

2.4.2.18

0.00075

-

60°C, pH 7.5, 2 mM Mg2+, mutant enzyme K106Q

680670

2.4.2.18

0.00091

-

60°C, pH 7.5, 2 mM Mg2+,mutant enzyme E224Q

680670

2.4.2.18

0.0012

-

mutant F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.4.2.18

0.0016

-

-

638666

2.4.2.18

0.002

-

25°C

638678

2.4.2.18

0.0022

-

at pH 8.5 and 55°C

759199

2.4.2.18

0.0026

-

40°C

638678

2.4.2.18

0.003

-

TAX6trpR782

638665

2.4.2.18

0.0031

-

mutant D83G/F149S, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.4.2.18

0.0032

-

50°C

638678

2.4.2.18

0.0035

-

60°C

638678

2.4.2.18

0.0036

-

mutant D83G/F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C

702308

2.4.2.18

0.004

-

trpAB1653trpR782

638665

2.4.2.18

0.0046

-

-

638669

2.4.2.18

0.005

-

87°C

638678

2.4.2.18

0.007

-

mutant enzyme I36E/M47D/D83G/F149S/I169T, pH 7.2, 37°C

724752

2.4.2.18

0.008

-

mutant enzyme I36E/M47D/D83G/F149S/L320M, pH 7.2, 37°C

724752

2.4.2.18

0.011

-

mutant enzyme I36E/M47D/D83G/F149S, pH 7.2, 37°C

724752

2.4.2.18

0.0125

-

60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A/P178A

680670

2.4.2.18

0.029

-

mutant enzyme I36E/M47D/D83G/F149S/F193S, pH 7.2, 37°C

724752

2.4.2.18

0.037

-

mutant enzyme I36E/M47D/T77I/D83G/F149S, pH 7.2, 37°C

724752

2.4.2.18

0.051

-

mutant enzyme I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M, pH 7.2, 37°C

724752

2.4.2.18

0.06

-

mutant enzyme I36E/M47D/D83G/N109S/F149S, pH 7.2, 37°C

724752

2.4.2.18

0.082

-

mutant enzyme I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M, pH 7.2, 37°C

724752

2.4.2.18

0.149

-

60°C, pH 7.5, 0.05 mM Mg2+,mutant enzyme R164A/H154A

680670

2.4.2.18

0.297

-

60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme R164A

680670

2.4.2.18

36 entries

2.5.1.2

37

-

-

636851

6.2.1.25

0.021

-

pH 8.0, 31°C, recombinant wild-type enzyme

744341

6.2.1.25

0.15

-

37°C

651721

6.2.1.25

0.25

-

-

713

6.2.1.25

0.25

-

in Tris-HCl at pH 8.0

675454

6.2.1.25

0.5

-

-

709

6.2.1.32

0.013

-

isoenzyme E2

713

6.2.1.32

0.015

-

isoenzyme E3

713

6.2.1.32

0.02

-

isoenzyme E2

438858

6.2.1.25

5 entries

6.2.1.32

3 entries

K_i Value (10 results)

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Show KI Value (10 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.6

2

-

for the pI 4.98 enzyme

658927

1.13.11.6

4.9

-

for the pI 4.98 enzyme

658927

1.13.11.6

6.5

-

for the pI 5.6 enzyme

658927

1.13.11.6

3 entries

1.13.12.9

0.87

-

20 mM Tris-HCl, pH 8.0, 25°C

698757

1.2.1.30

0.261

-

-

288184

1.4.3.2

0.01189

-

isoform L2, free enzyme

692288

1.4.3.2

0.02544

-

isoform L2, enzyme-substrate complex

692288

1.4.3.2

0.42

-

-

391799

1.4.3.2

3 entries

1.4.3.3

1.6

-

in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C

724965

2.4.2.18

0.03

-

-

638669

References & Links

Literature References (221)

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Show Reference (221 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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Ziegler, K.; Buder, R.; Winter, J.; Fuchs, G.

Arch. Microbiol.

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Benzoate-CoA ligase from Rhodopseudomonas palustris

1990

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Methods Enzymol.

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Purification and characterization of benzoate-coenzyme A ligase and 2-aminobenzoate-coenzyme A ligase from a denitrifying Pseudomonas sp.

1991

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J. Bacteriol.

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New aerobic benzoate oxidation pathway via benzoyl-coenzyme A and 3-hydroxybenzoyl-coenzyme A in a denitrifying Pseudomonas sp.

1993

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J. Bacteriol.

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Enzymatic decarboxylation of the aminobenzoates

1957

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J. Am. Chem. Soc.

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Enzyme-catalysed non-oxidative decarboxylation of aromatic acids. I. Piurification and spectroscopic properties of 2,3-dihydroxybenzoic acid decarboxylase from Aspergillus niger

1987

Kamath, A.V.; Dasgupta, D.; Vaidyanathan, C.S.

Biochem. Biophys. Res. Commun.

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Catabolism of tryptophan, anthranilate, and 2,3-dihydroxybenzoate in Trichosporon cutaneum

1981

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J. Bacteriol.

146

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4583

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1990

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Appl. Environ. Microbiol.

56

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Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes

1975

Largen, M.; Belser, W.L.

J. Bacteriol.

121

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4604

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Subunit structure of anthranilate synthetase from Neurospora crassa

1975

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J. Biol. Chem.

250

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4714

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Phthalate and 4-hydroxyphthalate metabolism in Pseudomonas testosteroni: purification and properties of 4,5-dihydroxyphthalate decarboxylase

1978

Nakazawa, T.; Hayashi, E.

Appl. Environ. Microbiol.

36

264-269

33276

5333199

Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli

1966

Baker, T.I.; Crawford, I.P.

J. Biol. Chem.

241

5577-5584

33277

4878701

Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium

1968

Zalkin, H.; Kling, D.

Biochemistry

7

3566-3573

33278

5001612

Anthranilate synthetase. Some physical and kinetic properties of the enzyme from Serratia marcescens

1971

Robb, F.; Hutchinson, M.A.; Belser, W.L.

J. Biol. Chem.

246

6908-6912

33279

-

Anthranilate synthetase from Serratia marcescens

1971

Zalkin, H.; Hwang, L.H.

J. Biol. Chem.

246

6899-6907

33280

4652566

Anthranilate synthetase from 5-methyltryptophan-susceptible and -resistant cultured Daucus carota cells

1972

Widholm, J.M.

Biochim. Biophys. Acta

279

48-57

33281

4692828

Anthranilate synthase from Pseudomonas putida. Purification and properties of a two-component enzyme

1973

Queener, S.W.; Queener, S.F.; Meeks, J.R.; Gunsalus, I.C.

J. Biol. Chem.

248

151-161

33282

4349869

Anthranilate synthetase of Acinetobacter calcoaceticus. Separation and partial characterization of subunits

1973

Sawula, R.V.; Crawford, I.P.

J. Biol. Chem.

248

3573-3581

33283

4275326

Anthranilate synthetase

1973

Zalkin, H.

Adv. Enzymol. Relat. Areas Mol. Biol.

38

1-39

33284

4615242

L-Tryptophan-agarose in the purification of an anthranilate synthetase complex

1974

Marcus, S.L.

Methods Enzymol.

34B

389-394

33286

765343

Properties of anthranilate synthetase component II from Pseudomonas putida

1976

Goto, Y.; Zalkin, H.; Keim, P.S.; Heinrikson, R.L.

J. Biol. Chem.

251

941-949

33287

4044

Aromatic amino acid biosynthesis in Alcaligenes eutrophus H 16 III. Properites and regulation of anthranilate synthase

1976

Friedrich, C.G.; Friedrich, B.; Schlegel, H.G.

Arch. Microbiol.

107

125-131

33288

-

Zur Charakterisierung der Anthranilat-Synthetase bei Claviceps

1976

Schmauder, H.P.; Gröger, D.

Biochem. Physiol. Pflanz.

169

471-486

33289

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Anthranilate synthase-amidotransferase (combined). A novel from of antrhanilate synthase from Euglena gracilis

1976

Hankins, C.N.; Mills, S.E.

J. Biol. Chem.

251

7774-7778

33290

875641

Purification and properties of anthranilate synthetase from the ergot fungus, Claviceps spec., strain SD 58

1977

Mann, D.F.; Floss, H.G.

Lloydia

40

136-145

33291

-

Die Enzyme der Biosynthese aromatischer Aminosäuren bei Hansenula henricii: Charakterisierung der Anthranilat-synthase

1978

Bode, R.; Birnbaum, D.

Biochem. Physiol. Pflanz.

172

245-253

33292

-

Die Enzyme der Biosynthese aromatischer Aminosäuren bei Hansenula henricii: Hemmung der Anthranilat-Synthase durch Tryptophan und Tryptophanderivate

1978

Bode, R.; Birnbaum, D.

Biochem. Physiol. Pflanz.

172

255-261

33293

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Characterization and regulation of anthranilate synthetase from a chloramphenicol-producing streptomycete

1978

Francis, M.M.; Vining, L.C.; Westlake, D.W.S.

J. Bacteriol.

134

10-16

33294

659439

Anthranilate synthetase component II from Pseudomonas putida. Covalent structure and identification of the cysteine residue involved in catalysis

1978

Kawamura, M.; Keim, P.S.; Goto, Y.; Zalkin, H.; Heinrikson, R.L.

J. Biol. Chem.

253

4659-4668

33295

6986371

Primary structure of Serratia marcescens anthranilate synthase component II

1980

Tso, J.Y.; Hermodson, M.A.; Zalkin, H.

J. Biol. Chem.

255

1451-1457

33296

6453559

Subunit structure of anthranilate synthase from Neurospora crassa: preparation and characterization of a protease-free form

1981

Keesey, J.; Paukert, J.; Demoss, J.A.

Arch. Biochem. Biophys.

207

103-109

33297

6219992

Purification and characterization of the trifunctional beta-subunit of anthranilate synthase from Neurospora crassa

1983

Walker, M.S.; DeMoss, J.A.

J. Biol. Chem.

258

3571-3575

33298

2935703

Anthranilate synthase

1985

Zalkin, H.

Methods Enzymol.

113

287-292

33299

24232024

Anthranilate synthase forms in plants and cultured cells of Nicotiana tabacum L.

1986

Brotherton, J.E.; Hauptmann, R.M.; Widholm, J.M.

Planta

168

214-221

33300

3600373

Anthranilate synthase from fluorescent Pseudomonads

1987

Crawford, I.P.

Methods Enzymol.

142

300-306

33301

-

Anthranilate synthase from Ailanthus altissima cells suspension cultures

1996

Romero, R.M.; Roberts, M.F.

Phytochemistry

41

395-402

33302

7890741

Immunological characterization and chloroplast localization of the tryptophan biosynthetic enzymes of the flowering plant Arabidopsis thaliana

1995

Zhao, J.; Last, R.L.

J. Biol. Chem.

270

6081-6087

33303

8234345

Characterization of composite aminodeoxyisochorismate synthase and aminodeoxyisochorismate lyase activities of anthranilate synthase

1993

Morollo, A.A.; Bauerle, R.

Proc. Natl. Acad. Sci. USA

90

9983-9987

33304

10089433

Crystallization and preliminary crystallographic studies of the anthranilate synthase partial complex from Salmonella typhimurium

1999

Tolbert, W.D.; Chatterji, S.; Bauerle, R.; Kretsinger, R.

Acta Crystallogr. Sect. D

55

305-306

33305

8444181

Purification and characterization of anthranilate synthase from Catharanthus roseus

1993

Poulsen, C.; Bongaerts, R.J.M.; Verpoorte, R.

Eur. J. Biochem.

212

431-440

33306

-

Chorismate-utilizing enzymes isochorismate synthase, anthranilate synthase, and p-aminobenzoate synthase: mechanistic insight through inhibitor design

1995

Kozlowski, M.C.; Tom, N.J.; Seto, C.T.; Sefler, A.M.; Bartlett, P.A.

J. Am. Chem. Soc.

117

2128-2140

33307

7757119

Purification and cDNA cloning of anthranilate synthase from Ruta graveolens: modes of expression and properties of native and recombinant enzymes

1995

Bohlmann, J.; DeLuca, V.; Eilert, U.; Martin, W.

Plant J.

7

491-501

33308

2063197

Subunit communication in the anthranilate synthase complex from Salmonella typhimurium

1991

Caligiuri, M.G.; Bauerle, R.

Science

252

1845-1848

33309

1478932

Characterization of Bacillus caldotenax anthranilate synthase I produced in Escherichia coli and identification of its essential arginine residue by site-directed mutagenesis

1992

Shiratsuchi, A.; Sato, S.

J. Biochem.

112

714-718

33310

-

Identification of amino acid residues involved in feedback inhibition of the anthranilate synthase in Escherichia coli

1999

Kwak, J.H.; Hong, K.W.; Lee, S.H.; Hong, J.H.; Lee, S.Y.

J. Biochem. Mol. Biol.

32

20-24

33311

2111807

The Rhizobium meliloti trpE(G) gene is regulated by attenuation, and its product, anthranilate synthase, is regulated by feedback inhibition

1990

Bae, Y.M.; Crawford, I.P.

J. Bacteriol.

172

3318-3327

33312

2153661

Identification and characterization of genes for a second anthranilate synthase in Pseudomonas aeruginosa: interchangeability of the two anthranilate synthases and evolutionary implications

1990

Essar, D.W.; Eberly, L.; Hadero, A.; Crawford, I.P.

J. Bacteriol.

172

884-900

33313

-

Anthranilate synthase from Ruta graveolens: partial purification and properties

1991

Hertel, S.C.; Hieke, M.; Gröger, D.

Biochem. Physiol. Pflanz.

187

121-129

34546

4008484

Isolation and characterization of a rat liver enzyme with both cysteine conjugate beta-lyase and kynureninase activity

1985

Stevens, J.L.

J. Biol. Chem.

260

7945-7950

37354

-

Tryptophanase from Aeromonas liquefaciens. Purification, molecular weight and some chemical, catalytic and immunochemical properties

1973

Cowell, J.L.; Moser, K.; DeMoss, R.D.

Biochim. Biophys. Acta

315

449-463

171890

6990827

Colorimetric assay of penicillin amidase activity using phenylacetyl-aminobenzoic acid as substrate

1980

Szewczuk, A.; Siewinski, M.; Slowinska, R.

Anal. Biochem.

103

166-169

209242

1722445

Inhibition studies on liver arylformamidases of rainbow trout and cattle

1991

Serrano, A.E.; Nagayama, F.

Comp. Biochem. Physiol. B

99

281-285

209248

-

Die Formamidase von Hansenula henricii: Isolierung, Charakterisierung und Regulation multipler Formen

1979

Bode, R.; Birnbaum, D.

Biochem. Physiol. Pflanz.

174

26-38

209249

92861

Vorkommen und Verteilung multipler Formen der Formamidase bei verschiedenen Hefen

1979

Bode, R.; Birnbaum, D.

Z. Allg. Mikrobiol.

19

221-222

209250

84781

Formamidase - Untersuchungen zu Mikroheterogenität, katalytischen Eigenschaften und Inhibitoren

1979

Menge, U.

Hoppe-Seyler's Z. Physiol. Chem.

360

185-196

209258

4190298

The purification and properties of formamidase from rat liver

1970

Shinohara, R.; Ishiguro, I.

Biochim. Biophys. Acta

198

324-331

209259

4187479

Formamidase in guinea pig liver II. Effect of aliphatic alcohols

1969

Santti, R.S.

Hoppe-Seyler's Z. Physiol. Chem.

350

1279-1285

209260

5719175

Kynurenine formamidase and tetrahydrofolic acid

1968

Santti, R.; Soini, J.

Acta Chem. Scand.

22

3321-3323

209261

13163050

Kynurenine fromamidase from Neurospora

1954

Jakoby, W.B.

J. Biol. Chem.

207

657-663

209262

14794728

The conversion of tryptophan to kynurenine in liver. II. The enzymatic hydrolysis of formylkynurenine

1950

Mehler, A.H.; Knox, W.E.

J. Biol. Chem.

187

431-438

288184

9171390

Purification, characterization, and properties of an aryl aldehyde oxidoreductase from Nocardia sp. strain NRRL 5646

1997

Li, T.; Rosazza, J.P.N.

J. Bacteriol.

179

3482-3487

288658

-

3'-Demethoxy-3'hydroxystaurosporine O-methyltransferase from Streptomyces longisporoflavus catalyzing the last step in the biosynthesis of staurosporine

1998

Weidner, S.; Kittelmann, M.; Goeke, K.; Ghisalba, O.; Zähner, H.

J. Antibiot.

51

697-682

289258

13129249

Kynureninase from Neurospora: Interaction of enzyme with substrates, coenzyme, and amines

1953

Jacoby, W.B.; Bonner, D.M.

J. Biol. Chem.

205

709-715

289259

13129248

Kynureninase from Neurospora: Purification and properties

1953

Jacoby, W.B.; Bonner, D.M.

J. Biol. Chem.

205

699-707

289260

13032082

The relation of liver kynureninase to tryptophan metabolism in pyridoxine deficiency

1952

Knox, W.E.

Biochem. J.

53

379-385

289261

-

Die Reindarstellung der Kynureninase

1956

Wiss, O.; Weber, F.

Hoppe-Seyler's Z. Physiol. Chem.

304

232-240

289263

4730493

Properties of crystalline Kynureninase from Pseudomonas marginalis

1973

Moriguchi, M.; Yamamoto, T.; Soda, K.

Biochemistry

12

2969-2974

289264

164432

Kynureninase-type enzymes of Penicillium roqueforti, Aspergillus niger, Rhizopus stolonifer, and Pseudomonas fluorescens: Further evidence for distinct kynureninase and hydroxykynureninase activities

1975

Shetty, A.S.; Gaertner, F.H.

J. Bacteriol.

122

235-244

289265

136367

Crystalline inducible kynureninase of Neurospora crassa

1976

Tanizawa, K.; Yamamoto, T.; Soda, K.

FEBS Lett.

70

235-238

289266

118164

The mechanism of kynurenine hydrolysis catalyzed by kynureninase

1979

Tanizawa, K.; Soda, K.

J. Biochem.

86

1199-1209

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