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Ligand 3-hydroxyanthranilic acid

Basic Ligand Information

Molecular Structure

Related pathways

Pathway Source

Pathways

BRENDA

tryptophan metabolism

KEGG

Aminobenzoate degradation, Biosynthesis of cofactors, Microbial metabolism in diverse environments, Tryptophan metabolism

MetaCyc

2-nitrobenzoate degradation I, anthranilate degradation IV (aerobic), diazepinomicin biosynthesis, L-tryptophan degradation to 2-amino-3-carboxymuconate semialdehyde, L-tryptophan degradation XI (mammalian, via kynurenine), L-tryptophan degradation XII (Geobacillus) more

Show all BRENDA pathways known for 3-hydroxyanthranilic acid

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (18 results)

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Show Natural Substrate (18 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.4

3-hydroxyanthranilic acid + O2 = 2-amino-3-oxo-3H-phenoxazine-1,9-dicarboxylic acid + H2O

713565

-

1.10.3.5

2 3-hydroxyanthranilic acid + 2 O2 = 2-amino-2H-phenoxazin-3-one-1,9-dicarboxylic acid + 2 H2O2

389976

-

1.10.3.5

3-hydroxyanthranilic acid + O2 = 2-amino-2H-isophenoxazine-3-one-1,9-dicarboxylic acid + H2O2

389977

-

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

1YFY, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

4HSL, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

6CD3, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

6D62, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

6VI6, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

6VI7, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

6VI8, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439366, 439370, 439367, 649382, 658927, 677020, 723950, 741516, 743276, 765043

1YFY, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439366, 439370, 439367, 649382, 658927, 677020, 723950, 741516, 743276, 765043

4HSL, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439366, 439370, 439367, 649382, 658927, 677020, 723950, 741516, 743276, 765043

6CD3, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439366, 439370, 439367, 649382, 658927, 677020, 723950, 741516, 743276, 765043

6D62, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439366, 439370, 439367, 649382, 658927, 677020, 723950, 741516, 743276, 765043

6VI6, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439366, 439370, 439367, 649382, 658927, 677020, 723950, 741516, 743276, 765043

6VI7, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439366, 439370, 439367, 649382, 658927, 677020, 723950, 741516, 743276, 765043

6VI8, 3D-view

1.10.3.5

2 entries

1.13.11.6

14 entries

2.1.1.97

S-adenosyl-L-methionine + 3-hydroxyanthranilate = S-adenosyl-L-homocysteine + 3-hydroxy-4-methylanthranilate

485687, 485686

-

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.7.1.3

3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + L-Ala

289268, 289278, 34546, 289260, 289277, 289287, 289261, 289284, 289258, 289259, 289265, 289269, 289264, 289276, 289286, 289288, 289272

-

3.7.1.3

3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + L-alanine

-

-

3.7.1.3

2 entries

Substrate in Enzyme-catalyzed Reactions (48 results)

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Show Substrate (48 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.2

3-hydroxyanthranilic acid + O2 = ?

763198

-

1.10.3.4

3-hydroxyanthranilic acid + O2 = 2-amino-3-oxo-3H-phenoxazine-1,9-dicarboxylic acid + H2O

713565

-

1.10.3.5

2 3-hydroxyanthranilic acid + 2 O2 = 2-amino-2H-phenoxazin-3-one-1,9-dicarboxylic acid + 2 H2O2

389978, 389977, 389980, 389981, 389976, 389979

-

1.10.3.5

3-hydroxyanthranilic acid + O2 = 2-amino-2H-isophenoxazine-3-one-1,9-dicarboxylic acid + H2O2

389977

-

1.10.3.5

2 entries

1.11.1.16

3-hydroxyanthranilic acid + H2O2 = ? + H2O

394603

-

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

1YFY, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

4HSL, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

6CD3, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

6D62, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

6VI6, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

6VI7, 3D-view

1.13.11.6

2-amino-3-hydroxybenzoic acid + O2 = 2,3-pyridinedicarboxylic acid + H2O

696784

6VI8, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439368, 439373, 439364, 439365, 439369, 439376, 439379, 439367, 439371, 439374, 439375, 439366, 439372, 439370, 649382, 658927, 677020, 675782, 672036, 672037, 723950, 741516, 743276, 765043, 765681

1YFY, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439368, 439373, 439364, 439365, 439369, 439376, 439379, 439367, 439371, 439374, 439375, 439366, 439372, 439370, 649382, 658927, 677020, 675782, 672036, 672037, 723950, 741516, 743276, 765043, 765681

4HSL, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439368, 439373, 439364, 439365, 439369, 439376, 439379, 439367, 439371, 439374, 439375, 439366, 439372, 439370, 649382, 658927, 677020, 675782, 672036, 672037, 723950, 741516, 743276, 765043, 765681

6CD3, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439368, 439373, 439364, 439365, 439369, 439376, 439379, 439367, 439371, 439374, 439375, 439366, 439372, 439370, 649382, 658927, 677020, 675782, 672036, 672037, 723950, 741516, 743276, 765043, 765681

6D62, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439368, 439373, 439364, 439365, 439369, 439376, 439379, 439367, 439371, 439374, 439375, 439366, 439372, 439370, 649382, 658927, 677020, 675782, 672036, 672037, 723950, 741516, 743276, 765043, 765681

6VI6, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439368, 439373, 439364, 439365, 439369, 439376, 439379, 439367, 439371, 439374, 439375, 439366, 439372, 439370, 649382, 658927, 677020, 675782, 672036, 672037, 723950, 741516, 743276, 765043, 765681

6VI7, 3D-view

1.13.11.6

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde

439377, 439368, 439373, 439364, 439365, 439369, 439376, 439379, 439367, 439371, 439374, 439375, 439366, 439372, 439370, 649382, 658927, 677020, 675782, 672036, 672037, 723950, 741516, 743276, 765043, 765681

6VI8, 3D-view

1.13.11.6

14 entries

1.14.13.2

3-hydroxyanthranilate + NADPH + O2 = ? + NADP+ + H2O

684919

-

1.14.13.23

3-hydroxyanthranilate + NADPH + O2 = ?

438963

-

1.14.13.35

3-hydroxyanthranilate + NADPH + O2 = ?

438866, 438875

-

1.14.18.1

3-hydroxyanthranilic acid + O2 = cinnabarinic acid + H2O

636435

-

2.1.1.97

S-adenosyl-L-methionine + 3-hydroxyanthranilate = S-adenosyl-L-homocysteine + 3-hydroxy-4-methylanthranilate

485687, 485686

-

2.1.1.97

S-adenosyl-L-methionine + 3-hydroxyanthranilic acid = S-adenosyl-L-homocysteine + 4-methyl-3-hydroxyanthranilic acid

485687, 485686

-

2.3.1.133

4-coumaroyl-CoA + 3-hydroxyanthranilate = CoA + 3-(4-coumaroyl)oxyanthranilate

720787, 736977

-

2.3.1.133

caffeoyl-CoA + 3-hydroxyanthranilate = CoA + 3-caffeoyloxyanthranilate

720787

-

2.3.1.133

cinnamoyl-CoA + 3-hydroxyanthranilate = CoA + 3-cinnamoyloxyanthranilate

720787

-

2.3.1.133

feruloyl-CoA + 3-hydroxyanthranilate = CoA + 3-feruloyloxyanthranilate

720787

-

2.3.1.133

sinapoyl-CoA + 3-hydroxyanthranilate = CoA + 3-sinapoyloxyanthranilate

720787

-

2.3.1.144

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

718662

-

2.3.1.144

2,5-dimethoxycinnamoyl-CoA + 3-hydroxyanthranilate = CoA + N-(2,5-dimethoxycinnamoyl)-3-hydroxyanthranilate

718662

-

2.3.1.144

2-coumaroyl-CoA + 3-hydroxyanthranilate = CoA + N-(2-coumaroyl)-3-hydroxyanthranilate

718662

-

2.3.1.144

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

718662

-

2.3.1.144

3,4-dimethoxycinnamoyl-CoA + 3-hydroxyanthranilate = CoA + N-(3,4-dimethoxycinnamoyl)-3-hydroxyanthranilate

718662

-

2.3.1.144

3-coumaroyl-CoA + 3-hydroxyanthranilate = CoA + N-(3-coumaroyl)-3-hydroxyanthranilate

718662

-

2.3.1.144

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

718662

-

2.3.1.144

4-coumaroyl-CoA + 3-hydroxyanthranilate = CoA + N-(4-coumaroyl)-3-hydroxyanthranilate

718662

-

2.3.1.144

benzoyl-CoA + 3-hydroxyanthranilate = CoA + N-benzoyl-3-hydroxyanthranilate

485081

-

2.3.1.144

caffeoyl-CoA + 3-hydroxyanthranilate = CoA + N-caffeoyl-3-hydroxyanthranilate

718662

-

2.3.1.144

cinnamoyl-CoA + 3-hydroxyanthranilate = CoA + N-cinnamoyl-3-hydroxyanthranilate

718662

-

2.3.1.144

feruloyl-CoA + 3-hydroxyanthranilate = CoA + N-feruloyl-3-hydroxyanthranilate

718662

-

2.3.1.144

sinapoyl-CoA + 3-hydroxyanthranilate = CoA + N-sinapoyl-3-hydroxyanthranilate

718662

-

2.1.1.97

2 entries

2.3.1.133

5 entries

2.3.1.144

13 entries

2.3.1.99

caffeoyl-CoA + 3-hydroxyanthranilate = CoA + 5-O-caffeoyl-3-hydroxyanthranilate

779058

-

2.4.2.18

3-hydroxyanthranilate + 5-phospho-alpha-D-ribose 1-diphosphate = ?

778045

-

2.7.7.97

ATP + 3-hydroxy-anthranilate = diphosphate + 3-hydroxy-anthranilyl-adenylate

740648

-

2.7.7.97

ATP + 3-hydroxyanthranilate = ?

740654

-

2.7.7.97

ATP + 3-hydroxyanthranilic acid = ?

740587

-

2.7.7.97

3 entries

Product in Enzyme-catalyzed Reactions (5 results)

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Show Product (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.8

anthranilate + FADH2 + O2 = 3-hydroxyanthranilate + FAD

-

-

1.14.14.8

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

-

-

3.7.1.3

3-hydroxy-DL-kynurenine + H2O = 3-hydroxyanthranilate + DL-alanine

-

-

3.7.1.3

3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + L-Ala

289268, 289278, 34546, 289260, 289277, 289287, 289261, 289284, 289258, 289259, 289265, 289269, 289264, 289276, 289286, 289288, 289272

-

3.7.1.3

3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + L-alanine

289268, 289278, 34546, 289260, 289277, 289287, 289261, 289284, 289258, 289259, 289265, 289269, 289264, 289276, 289286, 289288, 289272, -

-

1.14.14.8

2 entries

3.7.1.3

3 entries

Activator in Enzyme-catalyzed Reactions (3 results)

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Show Activating Compound (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.35

induces

438876

-

1.14.18.1

higher than 0.005 mM, 600% activation of N-acetyl-tyrosine hydroxylation, activation of 4-tert-butylphenol oxidation, shortens lag time of the enzyme

636435

-

1.4.3.5

145% increase in pyridoxine 5-phosphate oxidase activity, 28% increase in pyridoxamine 5-phosphate oxidase activity

391873

-

Inhibitor in Enzyme-catalyzed Reactions (11 results)

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Show Inhibitors (11 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

1.13.11.52

-

395454

-

1.13.11.74

20% inhibition at 0.05 mM

722493

-

1.14.13.35

-

438877

-

1.2.1.3

46% inhibition at 0.002 mM

692623

-

2.3.1.133

0.8 mM, about 45% inhibition

736977

-

2.4.2.18

competitive

638669

-

2.7.1.35

IC50: 0.12 mM

641412

-

3.7.1.3

0.001 mM in 0.06 mM Tris-HCl buffer

289267

-

4.1.1.46

-

4574, 4578

-

3D Structure of Enzyme-Ligand-Complex (PDB) (35 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (35 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.13.11.6

1YFY, 3D-view

1.13.11.6

4HSL, 3D-view

1.13.11.6

6CD3, 3D-view

1.13.11.6

6D62, 3D-view

1.13.11.6

6VI6, 3D-view

1.13.11.6

6VI7, 3D-view

1.13.11.6

6VI8, 3D-view

1.13.11.6

1YFY, 3D-view

1.13.11.6

4HSL, 3D-view

1.13.11.6

6CD3, 3D-view

1.13.11.6

6D62, 3D-view

1.13.11.6

6VI6, 3D-view

1.13.11.6

6VI7, 3D-view

1.13.11.6

6VI8, 3D-view

1.13.11.6

1YFY, 3D-view

1.13.11.6

4HSL, 3D-view

1.13.11.6

6CD3, 3D-view

1.13.11.6

6D62, 3D-view

1.13.11.6

6VI6, 3D-view

1.13.11.6

6VI7, 3D-view

1.13.11.6

6VI8, 3D-view

1.13.11.6

1YFY, 3D-view

1.13.11.6

4HSL, 3D-view

1.13.11.6

6CD3, 3D-view

1.13.11.6

6D62, 3D-view

1.13.11.6

6VI6, 3D-view

1.13.11.6

6VI7, 3D-view

1.13.11.6

6VI8, 3D-view

1.13.11.6

1YFY, 3D-view

1.13.11.6

4HSL, 3D-view

1.13.11.6

6CD3, 3D-view

1.13.11.6

6D62, 3D-view

1.13.11.6

6VI6, 3D-view

1.13.11.6

6VI7, 3D-view

1.13.11.6

6VI8, 3D-view

1.13.11.6

35 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (12 results)

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Show Turnover Number (12 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.13.11.6

0.0046

-

pH 7.2, mutant enzyme R99A

672037

1.13.11.6

0.012

-

pH 7.2, mutant enzyme E110A

672037

1.13.11.6

0.022

-

pH 7.2, mutant enzyme R47A

672037

1.13.11.6

25

-

pH 7.2, wild-type enzyme

672037

2.4.2.18

0.035

-

wild type enzyme, at pH 7.4 and 30°C

778045

2.4.2.18

0.038

-

wild type enzyme, at pH 7.4 and 30°C

778045

2.4.2.18

0.04

-

mutant enzyme N215S, at pH 7.4 and 30°C

778045

2.4.2.18

0.048

-

mutant enzyme P257T, at pH 7.4 and 30°C

778045

2.4.2.18

0.048

-

wild type enzyme, at pH 7.4 and 30°C

778045

2.4.2.18

0.052

-

mutant enzyme N215S/P257T, at pH 7.4 and 30°C

778045

2.4.2.18

0.053

-

wild type enzyme, at pH 7.4 and 30°C

778045

1.13.11.6

4 entries

2.4.2.18

7 entries

2.7.7.97

0.005

-

at pH 8.0 and 28°C

740648

K_M Value (33 results)

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Show KM Value (33 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.10.3.2

0.69

-

pH 5, 30°C

763198

1.10.3.5

0.014

-

air used as source of oxygen

389981

1.10.3.5

0.05

-

-

389981

1.13.11.6

0.002

-

-

439375

1.13.11.6

0.003

0.0036

-

439366, 439367

1.13.11.6

0.0102

-

pH 7.2, mutant enzyme E110A

672037

1.13.11.6

0.0159

-

deleted complemented strain

439379

1.13.11.6

0.0192

-

wild-type strain

439379

1.13.11.6

0.021

-

-

439364

1.13.11.6

0.0224

-

pH 7.2, wild-type enzyme

672037

1.13.11.6

0.105

-

-

439370

1.13.11.6

0.147

-

pH 7.2, mutant enzyme R47A

672037

1.13.11.6

0.872

-

pH 7.2, mutant enzyme R99A

672037

1.13.11.6

16

19

-

658927

1.10.3.5

2 entries

1.13.11.6

11 entries

1.14.18.1

0.78

-

-

636435

2.1.1.97

0.64

-

-

485687

2.3.1.133

0.449

-

pH 7.0, 30°C, with caffeoyl-CoA

720787

2.3.1.133

0.473

-

pH 7.0, 30°C, with 4-coumaroyl-CoA

720787

2.3.1.133

0.83

-

pH 7.5, 30°C

736977

2.3.1.99

0.1531

-

cosubstrate 4-coumaroyl-CoA, Michaelis-Menten plot, pH 9.0, 30°C

779058

2.3.1.99

0.2027

-

cosubstrate 4-coumaroyl-CoA, Hanes-Woolf plot, pH 9.0, 30°C

779058

2.3.1.99

0.761

-

cosubstrate caffeoyl-CoA, Michaelis-Menten plot, pH 9.0, 30°C

779058

2.3.1.99

0.7806

-

cosubstrate caffeoyl-CoA, Hanes-Woolf plot, pH 9.0, 30°C

779058

2.4.2.18

0.01963

-

wild type enzyme, at pH 7.4 and 30°C

778045

2.4.2.18

0.02266

-

wild type enzyme, at pH 7.4 and 30°C

778045

2.4.2.18

0.02823

-

wild type enzyme, at pH 7.4 and 30°C

778045

2.4.2.18

0.03595

-

mutant enzyme P257T, at pH 7.4 and 30°C

778045

2.4.2.18

0.05003

-

wild type enzyme, at pH 7.4 and 30°C

778045

2.4.2.18

0.06096

-

mutant enzyme N215S/P257T, at pH 7.4 and 30°C

778045

2.4.2.18

0.06506

-

mutant enzyme N215S, at pH 7.4 and 30°C

778045

2.4.2.18

0.09971

-

wild type enzyme, at pH 7.4 and 30°C

778045

2.4.2.18

1.075

-

wild type enzyme, at pH 7.4 and 30°C

778045

2.3.1.133

3 entries

2.3.1.99

4 entries

2.4.2.18

9 entries

2.7.7.97

0.018

-

at pH 8.0 and 28°C

740648

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.4.2.18

0.012

-

-

638669

IC₅₀ Value (1 result)

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Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

2.7.1.35

0.12

-

IC50: 0.12 mM

641412

References & Links

Literature References (83)

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Show Reference (83 entries)

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PUBMED ID

TITLE

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AUTHORS

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Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7

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658927

12672479

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672037

15909978

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677020

16522801

Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from Saccharomyces cerevisiae: a special subgroup of the type III extradiol dioxygenases

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696784

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Crystal structure of bovine 3-hydroxyanthranilate 3,4-dioxygenase

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Purification and characterization of actinomycin synthetase I, a 4-methyl-3-hydroxyanthranilic acid-AMP ligase from Streptomyces chrysomallus

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Combined purification of actinomycin synthetase I and 3-hydroxyanthranilic acid 4-methyltransferase from Streptomyces antibioticus

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741516

28375145

Crystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase with native and non-native metals bound in the active site

2017

Pidugu, L.S.; Neu, H.; Wong, T.L.; Pozharski, E.; Molloy, J.L.; Michel, S.L.; Toth, E.A.

Acta Crystallogr. Sect. D

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741516

28375145

Crystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase with native and non-native metals bound in the active site

2017

Pidugu, L.S.; Neu, H.; Wong, T.L.; Pozharski, E.; Molloy, J.L.; Michel, S.L.; Toth, E.A.

Acta Crystallogr. Sect. D

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743276

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Human 3-hydroxyanthranilate 3,4-dioxygenase dynamics and reaction, a multilevel computational study

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Human 3-hydroxyanthranilate 3,4-dioxygenase dynamics and reaction, a multilevel computational study

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Mol. Biosyst.

11

898-907

741516

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743276

2 entries

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Adapting to oxygen 3-hydroxyanthrinilate 3,4-dioxygenase employs loop dynamics to accommodate two substrates with disparate polarities

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Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens

2020

Wang, Y.; Liu, K.F.; Yang, Y.; Davis, I.; Liu, A.

Proc. Natl. Acad. Sci. USA

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19720-19730

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Biochemical investigation of the tryptophan biosynthetic enzyme anthranilate phosphoribosyltransferase in plants

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299

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Hydroxycinnamoyltransferase and CYP98 in phenolic metabolism in the rosmarinic acid-producing hornwort Anthoceros agrestis

2022

Ernst, L.; Wohl, J.; Bauerbach, E.; Petersen, M.

Planta

255

75

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