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  • In Vivo Product
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Ligand 3,4-Dihydroxyphenylacetate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

4-hydroxyphenylacetate degradation

KEGG

Alcoholism, Amphetamine addiction, Cocaine addiction, Degradation of aromatic compounds, Dopaminergic synapse, Microbial metabolism in diverse environments, Tyrosine metabolism more

MetaCyc

4-hydroxyphenylacetate degradation, aromatic biogenic amine degradation (bacteria), dopamine degradation

Show all BRENDA pathways known for 3,4-Dihydroxyphenylacetate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (19 results)

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Show Natural Substrate (19 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.15

3,4 dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

713419

1f1v, 3D-view

1.13.11.15

3,4 dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

713419

1q0c, 3D-view

1.13.11.15

3,4 dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

713419

4ghd, 3D-view

1.13.11.15

3,4 dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

713419

4ghg, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-5carboymethylmuconate semialdehyde

743618

1f1v, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-5carboymethylmuconate semialdehyde

743618

1q0c, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-5carboymethylmuconate semialdehyde

743618

4ghd, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-5carboymethylmuconate semialdehyde

743618

4ghg, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde

439620, 724298, 724360, 725555, 725557, 726271, 724361, 439615, 347717, 439614, 288303, 438892, 439617, 438890, 288301, 288040, 439619, 439625

1f1v, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde

439620, 724298, 724360, 725555, 725557, 726271, 724361, 439615, 347717, 439614, 288303, 438892, 439617, 438890, 288301, 288040, 439619, 439625

1q0c, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde

439620, 724298, 724360, 725555, 725557, 726271, 724361, 439615, 347717, 439614, 288303, 438892, 439617, 438890, 288301, 288040, 439619, 439625

4ghd, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde

439620, 724298, 724360, 725555, 725557, 726271, 724361, 439615, 347717, 439614, 288303, 438892, 439617, 438890, 288301, 288040, 439619, 439625

4ghg, 3D-view

1.13.11.15

12 entries

1.14.13.63

3,4-dihydroxyphenylacetate + NAD(P)H + O2 = 2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O

673422

-

2.1.1.6

homoprotocatechuic acid + S-adenosyl-L-methionine = ?

441526

-

2.8.2.1

3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.14

3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.15

3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.3

3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.4

3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?

702138

-

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

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Show Natural Product (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.9

4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O

-

-

1.14.14.9

4-hydroxyphenylacetate + FMNH + O2 = 3,4-dihydroxyphenylacetate + FMN + H2O

-

-

1.14.14.9

4-hydroxyphenylacetate + FMNH2 + O2 = 3,4-dihydroxyphenylacetate + FMN + H2O

-

-

1.14.14.9

4-hydroxyphenylacetate + NAD(P)H + H+ + O2 = 3,4-dihydroxyphenylacetate + NAD(P)+ + H2O

-

-

1.14.14.9

4-hydroxyphenylacetate + NADH + H+ + O2 = 3,4-dihydroxyphenylacetate + NAD+ + H2O

-

-

1.14.14.9

4-hydroxyphenylacetate + NADH + O2 = 3,4-dihydroxyphenylacetate + NAD+ + H2O

438900, 438897, 438899, 438890, , 438895, 438898, 438893, 288301, 288303, 438892, 438887, 288040, 438894

-

1.14.14.9

4-hydroxyphenylacetate + NADPH + H+ + O2 = 3,4-dihydroxyphenylacetate + NADP+ + H2O

-

-

1.14.14.9

7 entries

1.2.1.3

3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O = 3,4-dihydroxyphenylacetic acid + NADH + H+

-

-

3.1.2.B5

3,4-dihydroxyphenylacetyl-CoA + H2O = 3,4-dihydroxyphenylacetate + CoA

-

-

Substrate in Enzyme-catalyzed Reactions (56 results)

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Show Substrate (56 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.1

3,4-dihydroxyphenyl acetic acid + O2 = ?

675458

-

1.10.3.1

3,4-dihydroxyphenylacetic acid + O2 = (3,4-dioxocyclohexa-1,5-dien-1-yl)acetic acid + H2O

687246, 712219, 686666

-

1.10.3.1

3,4-dihydroxyphenylacetic acid + O2 = ?

686666

-

1.10.3.1

3 entries

1.10.3.2

3,4-dihydroxyphenylacetate + O2 = ? + H2O

687338

-

1.11.1.7

3,4-dihydroxyphenylacetic acid + H2O2 = ? + H2O

687246

-

1.11.2.2

3,4-dihydroxyphenylacetic acid + H2O2 = ? + H2O

659636

-

1.13.11.15

3,4 dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

713419

1f1v, 3D-view

1.13.11.15

3,4 dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

713419

1q0c, 3D-view

1.13.11.15

3,4 dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

713419

4ghd, 3D-view

1.13.11.15

3,4 dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

713419

4ghg, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

699014

1f1v, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

699014

1q0c, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

699014

4ghd, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde

699014

4ghg, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-5carboymethylmuconate semialdehyde

743618

1f1v, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-5carboymethylmuconate semialdehyde

743618

1q0c, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-5carboymethylmuconate semialdehyde

743618

4ghd, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-5carboymethylmuconate semialdehyde

743618

4ghg, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethyl-cis,cis-muconate semialdehyde

654735, 655783

1f1v, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethyl-cis,cis-muconate semialdehyde

654735, 655783

1q0c, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethyl-cis,cis-muconate semialdehyde

654735, 655783

4ghd, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethyl-cis,cis-muconate semialdehyde

654735, 655783

4ghg, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde

439607, 439614, 288301, 390253, 439603, 439618, 439617, 347717, 439620, 288303, 396333, 438886, 438892, 439569, 439621, 439622, 439615, 439616, 439619, 439626, 439624, 674920, 288040, 438890, 439623, 439625, 724298, 724360, 725555, 725557, 439605, 726271, 724361, 672032

1f1v, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde

439607, 439614, 288301, 390253, 439603, 439618, 439617, 347717, 439620, 288303, 396333, 438886, 438892, 439569, 439621, 439622, 439615, 439616, 439619, 439626, 439624, 674920, 288040, 438890, 439623, 439625, 724298, 724360, 725555, 725557, 439605, 726271, 724361, 672032

1q0c, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde

439607, 439614, 288301, 390253, 439603, 439618, 439617, 347717, 439620, 288303, 396333, 438886, 438892, 439569, 439621, 439622, 439615, 439616, 439619, 439626, 439624, 674920, 288040, 438890, 439623, 439625, 724298, 724360, 725555, 725557, 439605, 726271, 724361, 672032

4ghd, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde

439607, 439614, 288301, 390253, 439603, 439618, 439617, 347717, 439620, 288303, 396333, 438886, 438892, 439569, 439621, 439622, 439615, 439616, 439619, 439626, 439624, 674920, 288040, 438890, 439623, 439625, 724298, 724360, 725555, 725557, 439605, 726271, 724361, 672032

4ghg, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboymethylmuconate semialdehyde

743618

1f1v, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboymethylmuconate semialdehyde

743618

1q0c, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboymethylmuconate semialdehyde

743618

4ghd, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboymethylmuconate semialdehyde

743618

4ghg, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = ?

700982

1f1v, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = ?

700982

1q0c, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = ?

700982

4ghd, 3D-view

1.13.11.15

3,4-dihydroxyphenylacetate + O2 = ?

700982

4ghg, 3D-view

1.13.11.3

3,4-dihydroxyphenylacetate + O2 = ?

439505, 439513

3mfl, 3D-view

1.13.11.3

3,4-dihydroxyphenylacetate + O2 = ?

439505, 439513

3pcn, 3D-view

1.13.11.15

28 entries

1.13.11.3

2 entries

1.13.11.50

3,4-dihydroxyphenylacetate + O2 = ?

696107

-

1.14.13.63

3,4-dihydroxyphenylacetate + NAD(P)H + O2 + H+ = 2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O

7425

-

1.14.13.63

3,4-dihydroxyphenylacetate + NAD(P)H + O2 = 2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O

673422

-

1.14.13.63

3,4-Dihydroxyphenylacetate + NADH + O2 = 2,4,5-Trihydroxyphenylacetate + NAD+

7425

-

1.14.14.9

3,4-dihydroxyphenylacetate + ? = ?

438898, 438894

-

1.14.14.9

3,4-dihydroxyphenylacetate + FAD + H2O = 4-hydroxyphenylacetate + FADH2 + O2

438895

-

1.14.18.1

3,4-dihydroxyphenylacetic acid + 1/2 O2 = (3,4-dioxocyclohexa-1,5-dien-1-yl)acetic acid + H2O

685018

-

1.14.18.1

3,4-dihydroxyphenylacetic acid + O2 = ?

674092, 745746, 659827

-

2.1.1.6

S-adenosyl-L-methionine + (3,4-dihydroxyphenyl)acetic acid = S-adenosyl-L-homocysteine + (4-hydroxy-3-methoxyphenyl)acetic acid + (3-hydroxy-4-methoxyphenyl)acetic acid

755786

-

2.1.1.6

3,4-dihydroxyphenylacetic acid + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + ?

441507, 441513, 441518

-

2.1.1.6

S-adenosyl-L-methionine + 3,4-dihydroxyphenylacetic acid = S-adenosyl-L-homocysteine + ?

658517

-

2.1.1.6

homoprotocatechuic acid + S-adenosyl-L-methionine = ?

441526

-

2.8.2.1

3'-phosphoadenylylsulfate + 3,4-dihydroxyphenylacetate = adenosine 3',5'-bisphosphate + ?

645680

-

2.8.2.1

3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.1

3'-phosphoadenylylsulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?

645654

-

1.14.13.63

3 entries

1.14.14.9

2 entries

1.14.18.1

2 entries

2.1.1.6

4 entries

2.8.2.1

3 entries

2.8.2.14

3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.15

3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.3

3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.4

3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid = adenosine 3',5'-bisphosphate + ?

702138

-

4.1.1.83

(3,4-dihydroxyphenyl)acetate + H+ = 4-methylcatechol + CO2

658599, 678213, 715289

-

Product in Enzyme-catalyzed Reactions (24 results)

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Show Product (24 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.12.9

3-chlorophenylacetate + NADH + O2 + H2O = 3,4-dihydroxyphenylacetate + Cl- + NAD+

-

-

1.14.12.9

4-bromophenylacetate + NADH + O2 + H2O = 3,4-dihydroxyphenylacetate + Br- + NAD+

-

-

1.14.12.9

4-chlorophenylacetate + ferrocytochrome c + H+ + O2 = 3,4-dihydroxyphenylacetate + chloride + ferricytochrome c

-

-

1.14.12.9

4-chlorophenylacetate + NADH + O2 + H2O = 3,4-dihydroxyphenylacetate + Cl- + NAD(P)+

-

-

1.14.12.9

4-chlorophenylacetate + reduced 2,6-dichlorophenolindophenol + O2 = 3,4-dihydroxyphenylacetate + chloride + oxidized 2,6-dichlorophenolindophenol

-

-

1.14.12.9

4-fluorophenylacetate + NADH + O2 + H2O = 3,4-dihydroxyphenylacetate + F- + NAD+

-

-

1.14.12.9

4-hydroxyphenylacetate + NADH + O2 + H2O = 3,4-dihydroxyphenylacetate + OH- + NAD+

-

-

1.14.14.9

4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O

-

-

1.14.14.9

4-hydroxyphenylacetate + FMNH + O2 = 3,4-dihydroxyphenylacetate + FMN + H2O

-

-

1.14.14.9

4-hydroxyphenylacetate + FMNH2 + O2 = 3,4-dihydroxyphenylacetate + FMN + H2O

-

-

1.14.14.9

4-hydroxyphenylacetate + NAD(P)H + H+ + O2 = 3,4-dihydroxyphenylacetate + NAD(P)+ + H2O

-

-

1.14.14.9

4-hydroxyphenylacetate + NAD(P)H + O2 = 3,4-dihydroxyphenylacetate + NAD(P)+ + H2O

288040

-

1.14.14.9

4-hydroxyphenylacetate + NADH + H+ + O2 = 3,4-dihydroxyphenylacetate + NAD+ + H2O

-

-

1.14.14.9

4-hydroxyphenylacetate + NADH + O2 = 3,4-dihydroxyphenylacetate + NAD+ + H2O

438893, 438894, 438899, 438900, , 438886, 438887, 438895, 438897, 438901, 438898, 438890, 438896, 288301, 288303, 438892, 288040

-

1.14.14.9

4-hydroxyphenylacetate + NADPH + H+ + O2 = 3,4-dihydroxyphenylacetate + NADP+ + H2O

-

-

1.14.14.9

4-hydroxyphenylacetic acid + O2 + NADH + H+ = 3,4-dihydroxyphenylacetic acid + H2O + NAD+

-

-

1.2.1.3

3,4-dihydroxyphenyl acetaldehyde + NAD+ + H2O = 3,4-dihydroxyphenylacetate + NADH

-

-

1.2.1.3

3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O = 3,4-dihydroxyphenylacetate + NADH + H+

-

-

1.2.1.3

3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O = 3,4-dihydroxyphenylacetic acid + NADH + H+

-

-

1.14.12.9

7 entries

1.14.14.9

9 entries

1.2.1.3

3 entries

1.2.1.39

3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O = 3,4-dihydroxyphenylacetate + NADH + H+

-

-

1.2.1.5

3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O = 3,4-dihydroxyphenylacetate + NADH + H+

-

-

1.2.1.5

3,4-dihydroxyphenylacetaldehyde + NAD+ = 3,4-dihydroxyphenylacetate + NADH

-

-

1.2.1.5

2 entries

3.1.2.20

3,4-dihydroxyphenylacetyl-CoA + H2O = CoA + 3,4-dihydroxyphenylacetate

-

-

3.1.2.B5

3,4-dihydroxyphenylacetyl-CoA + H2O = 3,4-dihydroxyphenylacetate + CoA

-

-

Inhibitor in Enzyme-catalyzed Reactions (21 results)

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Show Inhibitors (21 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.27

0.75 mM, 50% inhibition, noncompetitive

395375

-

1.13.11.3

-

439486

3mfl, 3D-view

1.13.11.3

-

439486

3pcn, 3D-view

1.13.11.3

-

439483, 439501

3mfl, 3D-view

1.13.11.3

-

439483, 439501

3pcn, 3D-view

1.13.11.3

0.006 mM, 92% inhibition

439500

3mfl, 3D-view

1.13.11.3

0.006 mM, 92% inhibition

439500

3pcn, 3D-view

1.13.11.3

6 entries

1.13.11.5

1 mM, 48% inhibition, substrate analogue

439389

-

1.14.11.11

-

439275

-

1.14.11.2

IC50: 0.3 mM

674423

-

1.14.11.2

-

439186, 439221

-

1.14.11.2

competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+

439194

-

1.14.11.2

3 entries

1.14.13.18

-

347714

-

1.14.13.5

66% inhibition at 4.5 mM

390101

-

2.6.1.5

88% inhibition with tyrosine at 3 mM and dihydroxyphenylacetic acid at 3 mM

640109

-

2.8.2.1

-

645650

-

3.5.1.98

90% residual activity at 0.5 mM

711439

-

3.5.4.1

-

718465

-

3.5.4.B9

-

718465

-

4.1.1.15

-

3980

-

4.1.1.83

-

658599

-

3D Structure of Enzyme-Ligand-Complex (PDB) (67 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (67 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.13.11.15

1f1v, 3D-view

1.13.11.15

1q0c, 3D-view

1.13.11.15

4ghd, 3D-view

1.13.11.15

4ghg, 3D-view

1.13.11.15

1f1v, 3D-view

1.13.11.15

1q0c, 3D-view

1.13.11.15

4ghd, 3D-view

1.13.11.15

4ghg, 3D-view

1.13.11.15

1f1v, 3D-view

1.13.11.15

1q0c, 3D-view

1.13.11.15

4ghd, 3D-view

1.13.11.15

4ghg, 3D-view

1.13.11.15

1f1v, 3D-view

1.13.11.15

1q0c, 3D-view

1.13.11.15

4ghd, 3D-view

1.13.11.15

4ghg, 3D-view

1.13.11.15

1f1v, 3D-view

1.13.11.15

1q0c, 3D-view

1.13.11.15

4ghd, 3D-view

1.13.11.15

4ghg, 3D-view

1.13.11.15

1f1v, 3D-view

1.13.11.15

1q0c, 3D-view

1.13.11.15

4ghd, 3D-view

1.13.11.15

4ghg, 3D-view

1.13.11.15

1f1v, 3D-view

1.13.11.15

1q0c, 3D-view

1.13.11.15

4ghd, 3D-view

1.13.11.15

4ghg, 3D-view

1.13.11.15

1f1v, 3D-view

1.13.11.15

1q0c, 3D-view

1.13.11.15

4ghd, 3D-view

1.13.11.15

4ghg, 3D-view

1.13.11.15

1f1v, 3D-view

1.13.11.15

1q0c, 3D-view

1.13.11.15

4ghd, 3D-view

1.13.11.15

4ghg, 3D-view

1.13.11.15

1f1v, 3D-view

1.13.11.15

1q0c, 3D-view

1.13.11.15

4ghd, 3D-view

1.13.11.15

4ghg, 3D-view

1.13.11.15

1f1v, 3D-view

1.13.11.15

1q0c, 3D-view

1.13.11.15

4ghd, 3D-view

1.13.11.15

4ghg, 3D-view

1.13.11.3

3mfl, 3D-view

1.13.11.3

3pcn, 3D-view

1.13.11.3

3mfl, 3D-view

1.13.11.3

3pcn, 3D-view

1.13.11.3

3mfl, 3D-view

1.13.11.3

3pcn, 3D-view

1.13.11.3

3mfl, 3D-view

1.13.11.3

3pcn, 3D-view

1.13.11.3

3mfl, 3D-view

1.13.11.3

3pcn, 3D-view

1.13.11.3

3mfl, 3D-view

1.13.11.3

3pcn, 3D-view

1.13.11.3

3mfl, 3D-view

1.13.11.3

3pcn, 3D-view

1.13.11.3

3mfl, 3D-view

1.13.11.3

3pcn, 3D-view

1.13.11.3

3mfl, 3D-view

1.13.11.3

3pcn, 3D-view

1.13.11.3

3mfl, 3D-view

1.13.11.3

3pcn, 3D-view

1.13.11.3

3mfl, 3D-view

1.13.11.3

3pcn, 3D-view

1.13.11.15

44 entries

1.13.11.3

22 entries

3.5.1.11

1ai4, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (27 results)

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Show Turnover Number (27 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.10.3.1

11.48

-

-

686666

1.10.3.1

142

-

-

675458

1.10.3.1

533

-

-

675458

1.10.3.1

631.6

-

-

675458

1.10.3.1

850

-

-

675458

1.13.11.15

0.067

-

23°C, pH 7.5, mutant enzyme H200A

674920

1.13.11.15

0.12

-

mutant H200F

655783

1.13.11.15

0.21

-

24°C, pH 7.5, mutant enzyme H200F

672032

1.13.11.15

0.3

-

24°C, pH 7.5, mutant enzyme H200A

672032

1.13.11.15

0.9

-

24°C, pH 7.5, mutant enzyme H200E

672032

1.13.11.15

2.67

-

23°C, pH 7.5, mutant enzyme H200N

674920

1.13.11.15

3

-

24°C, pH 7.5, mutant enzyme H20N

672032

1.13.11.15

3.2

-

pH 7.5, 4°C

654735

1.13.11.15

3.6

-

23°C, pH 7.5, mutant enzyme H200Q

674920

1.13.11.15

4

-

24°C, pH 7.5, mutant enzyme H200Q

672032

1.13.11.15

4.6

-

23°C, pH 7.5, wild-type enzyme

674920

1.13.11.15

10

-

24°C, pH 7.5, wild-type enzyme

672032

1.13.11.15

10

-

pH 7.5, 22°C

654735

1.13.11.15

10

-

wild-type

655783

1.13.11.15

62.4

-

pH 7.5, 25°C

743618

1.13.11.15

63.5

-

pH 7.5, 25°C, in presence of ascorbate

743618

1.10.3.1

5 entries

1.13.11.15

16 entries

1.14.13.63

15.6

-

-

7425

1.14.18.1

5.9

-

recombinant enzyme, pH 7.2, 37°C

745746

1.14.18.1

113

-

recombinant enzyme, pH 7.2, 37°C

745746

1.14.18.1

433.1

-

-

685018

4.1.1.83

65

-

in 100 mM Tris-HCl, pH 7.5, 40 mM NaCl, 5 mM MgCl2, 5 mM (NH4)2SO4, 5 mM cysteine, 25 mM substrate, and 5 mM dithiothreitol, at 30°C

678213

4.1.1.83

67

-

in 100 mM Tris-HCl, pH 7.5, 40 mM NaCl, 5 mM MgCl2, 5 mM (NH4)2SO4, 5 mM cysteine, 25 mM substrate, and 5 mM dithiothreitol, at 30°C

678213

1.14.18.1

3 entries

4.1.1.83

2 entries

K_M Value (48 results)

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Show KM Value (48 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.10.3.1

1.16

-

-

675458

1.10.3.1

2.9

-

-

686666

1.10.3.1

4.4

-

-

675458

1.10.3.1

5.1

-

-

675458

1.10.3.1

6

-

-

686666

1.10.3.1

6.66

-

for Cucumis melo L. inodorus cv. Amarillo

687246

1.10.3.1

7.18

-

for Cucumis melo L. cantalupensis cv. Charentais

687246

1.11.1.7

5.05

-

for Cucumis melo L. inodorus cv. Amarillo

687246

1.11.1.7

24

-

for Cucumis melo L. cantalupensis cv. Charentais

687246

1.11.2.2

0.52

-

25°C, pH 5.5

659636

1.11.2.2

21.9

-

25°C, pH 5.5

659636

1.13.11.15

0.0004

-

24°C, pH 7.5, mutant enzyme H200E

672032

1.13.11.15

0.0034

-

32°C

439618

1.13.11.15

0.004

-

28°C

439618

1.13.11.15

0.0047

-

21°C

439618

1.13.11.15

0.005

-

24°C, pH 7.5, mutant enzyme H200A

672032

1.13.11.15

0.0058

-

38°C

439618

1.13.11.15

0.0074

-

47°C

439618

1.13.11.15

0.01

-

24°C, pH 7.5, mutant enzyme H20N

672032

1.13.11.15

0.011

-

recombinant enzyme

439625

1.13.11.15

0.012

-

23°C, pH 7.5, mutant enzyme H200A

674920

1.13.11.15

0.014

-

Mn-MndD

700982

1.13.11.15

0.015

-

-

439623

1.13.11.15

0.015

-

Fe-MndD

700982

1.13.11.15

0.016

-

-

439603

1.13.11.15

0.017

-

23°C, pH 7.5, mutant enzyme H200E

674920

1.13.11.15

0.018

-

23°C, pH 7.5, mutant enzyme H200Q

674920

1.13.11.15

0.021

-

23°C, pH 7.5, mutant enzyme H200N

674920

1.13.11.15

0.021

-

23°C, pH 7.5, wild-type enzyme

674920

1.13.11.15

0.025

-

-

439569, 439605

1.13.11.15

0.025

-

pH 7.5, 22°C

654735

1.13.11.15

0.028

-

24°C, pH 7.5, mutant enzyme H200Q

672032

1.13.11.15

0.03

-

24°C, pH 7.5, wild-type enzyme

672032

1.13.11.15

0.031

-

24°C, pH 7.5, mutant enzyme H200F

672032

1.13.11.15

0.031

-

Fe-HPCD

700982

1.13.11.15

0.035

-

Mn-HPCD

700982

1.13.11.15

0.058

-

pH 7.5, 25°C, in presence of ascorbate

743618

1.13.11.15

0.067

-

pH 7.5, 25°C

743618

1.10.3.1

7 entries

1.11.1.7

2 entries

1.11.2.2

2 entries

1.13.11.15

27 entries

1.14.13.63

0.09

-

-

7425

1.14.18.1

1.3

-

-

685018

1.14.18.1

11

-

recombinant enzyme, pH 7.2, 37°C

745746

1.14.18.1

19

-

recombinant enzyme, pH 7.2, 37°C

745746

1.14.18.1

3 entries

2.1.1.6

0.64

-

-

441513

2.8.2.1

0.01

-

pH 5.8, 37°C

645654

2.8.2.15

0.0209

-

isoform Sult1d1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C

702138

4.1.1.83

0.388

-

in 100 mM Tris-HCl, pH 7.5, 40 mM NaCl, 5 mM MgCl2, 5 mM (NH4)2SO4, 5 mM cysteine, 25 mM substrate, and 5 mM dithiothreitol, at 30°C

678213

4.1.1.83

0.41

-

in 100 mM Tris-HCl, pH 7.5, 40 mM NaCl, 5 mM MgCl2, 5 mM (NH4)2SO4, 5 mM cysteine, 25 mM substrate, and 5 mM dithiothreitol, at 30°C

678213

4.1.1.83

0.5

-

-

658599

4.1.1.83

3 entries

K_i Value (5 results)

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Show KI Value (5 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.3

0.013

-

-

439486

1.13.11.3

0.041

-

-

439500

1.14.11.2

0.009

-

-

439194

1.14.11.2

0.04

-

-

439221

1.13.11.3

2 entries

1.14.11.2

2 entries

4.1.1.83

0.4

-

-

658599

IC₅₀ Value (3 results)

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Show IC50 Value (3 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.14.11.2

0.3

-

IC50: 0.3 mM

674423

3.5.4.1

0.019

-

pH 7.4, 37°C

718465

3.5.4.B9

0.019

-

at pH 7.8 and 37°C

718465

References & Links

Literature References (95)

top print hide

Show Reference (95 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

3980

658037

Purification and some properties of L-glutamate decarboxylase from human brain

1978

Blindermann, J.M.; Maitre, M.; Ossola, L.; Mandel, P.

Eur. J. Biochem.

86

143-152

7425

1935954

Purification and characterisation of 3-hydroxyphenylacetate 6-hydroxylase: a novel FAD-dependent monooxygenase from a Flavobacterium species

1991

van Berkel, W.J.H.; van den Tweel, W.J.J.

Eur. J. Biochem.

201

585-591

288040

20216

The catabolism of L-tyrosine by an Arthrobacter sp.

1977

Blakley, E.R.

Can. J. Microbiol.

23

1128-1139

288301

6995433

Catabolism of 3- and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coli

1980

Cooper, R.A.; Skinner, M.A.

J. Bacteriol.

143

302-306

288303

6895079

Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida

1981

Barbour, M.G.; Bayly, R.C.

J. Bacteriol.

147

844-850

347714

234937

Metabolic function and properties of 4-hydroxyphenylacetic acid 1-hydroxylase from Pseudomonas acidovorans

1975

Hareland, W.A.; Crawford, R.L.; Chapman, P.J.; Dagley, S.

J. Bacteriol.

121

272-285

347717

7217006

Degradation of 4-chlorophenylacetic acid by a Pseudomonas species

1981

Klages, U.; Markus, A.; Lingens, F.

J. Bacteriol.

146

64-68

390101

6869819

Method for enzymatic determination of imidazole acetic acid

1983

Watanabe, T.; Kambe, H.; Imamura, I.; Taguchi, Y.; Tamura, T.; Wada, H.

Anal. Biochem.

130

321-327

390253

3053656

Molecular cloning, expression, and analysis of the genes of the homoprotocatechuate catabolic pathway of Escherichia coli C

1988

Jenkins, J.R.; Cooper, R.A.

J. Bacteriol.

170

5317-5324

395375

7118918

Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874

1982

Lindstedt, S.; Rundgren, M.

J. Biol. Chem.

257

11922-11931

396333

-

Nonheme iron dioxygenase

1974

Nozaki, M.

Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York

-

135-165

438886

14263147

Metabolism of p-hydroxyphenylacetic acid in Pseudomonas ovalis

1964

Adachi, K.; Takeda, Y.; Senoh, S.; Kita, H.

Biochim. Biophys. Acta

93

483-493

438887

3401220

Purification and properties of 4-hydroxyphenylacetic acid 3-hydroxylase from Pseudomonas putida

1988

Raju, S.G.; Kamath, A.V.; Vaidyanathan, C.S.

Biochem. Biophys. Res. Commun.

154

537-543

438890

597294

Regulation of the 4-hydroxyphenylacetic acid meta-cleavage pathway in an Acinetobacter sp

1977

Barbour, M.G.; Bayly, R.C.

Biochem. Biophys. Res. Commun.

79

663-670

438892

1027447

Regulation of the meta-cleavage of 4-hydroxyphenylacetic acid by Pseudomonas putida

1977

Barbour, M.G.; Bayly, R.C.

Biochem. Biophys. Res. Commun.

76

565-571

438893

8077235

Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme

1994

Prieto, M.A.; Garcia, J.L.

J. Biol. Chem.

269

22823-22829

438894

8458860

Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range

1993

Prieto, M.A.; Perez-Aranda, A.; Garcia, J.L.

J. Bacteriol.

175

2162-2167

438895

-

Purification and characterization of the 4-hydroxyphenylacetic acid-3-hydroxylase from Pseudomonas putida U

1997

Fernandez-Medarde, A.; Luengo, J.M.

FEMS Microbiol. Lett.

157

47-53

438896

10653707

Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase

2000

Xun, L.; Sandvik, E.R.

Appl. Environ. Microbiol.

66

481-486

438897

8276789

Mechanism of p-hydroxyphenylacetate-3-hydroxylase. A two-protein enzyme

1994

Arunachalam, U.; Massey, V.; Miller, S.M.

J. Biol. Chem.

269

150-155

438898

9042756

Molecular cloning and analysis of the genes encoding the 4-hydroxyphenylacetate hydroxylase from Klebsiella pneumoniae

1997

Gibello, A.; Suarez, M.; Allende, J.L.; Martin, M.

Arch. Microbiol.

167

160-166

438899

10633095

Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new flavin:NAD(P)H reductase subfamily

2000

Galan, B.; Diaz, E.; Prieto, M.A.; Garcia, J.L.

J. Bacteriol.

182

627-636

438900

11683878

A novel two-protein component flavoprotein hydroxylase. p-Hydroxyphenylacetate hydroxylase from Acinetobacter baumannii

2001

Chaiyen, P.; Suadee, C.; Wilairat, P.

Eur. J. Biochem.

268

5550-5561

438901

8163477

Studies on the oxidative half-reaction of p-hydroxyphenylacetate 3-hydroxylase

1994

Arunachalam, U.; Massey, V.

J. Biol. Chem.

269

11795-11801

439186

3041180

Recent developments in posttranslational modification: intracellular processing

1987

Kivirikko, K.I.; Myllylä, R.

Methods Enzymol.

144

96-114

439194

3011801

Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase

1986

Majamaa, K.; Gunzler, V.; Hanauske-Abel, H.M.; Myllylä, R.; Kivirikko, K.I.

J. Biol. Chem.

261

7819-7823

439221

2851981

Prolyl 4-hydroxylase from Volvox carteri. A low-Mr enzyme antigenically related to the alpha subunit of the vertebrate enzyme

1988

Kaska, D.D.; Myllylä, R.; Gunzler, V.; Gibori, A.; Kivirikko, K.I.

Biochem. J.

256

257-263

439275

3569262

Purification and characterization of hyoscyamine 6 beta-hydroxylase from root cultures of Hyoscyamus niger L. Hydroxylase and epoxidase activities in the enzyme preparation

1987

Hashimoto, T.; Yamada, Y.

Eur. J. Biochem.

164

277-285

439389

9056215

Spectrophotometric determination of homogentisate using Aspergillus nidulans homogentisate dioxygenase

1997

Fernandez-Canon, J.M.; Penalva, M.A.

Anal. Biochem.

245

218-221

439483

4967959

Protocatechuate 3,4-dioxygenase. I. Crystallization and characterization

1968

Fujisawa, H.; Hayaishi, O.

J. Biol. Chem.

243

2673-2681

439486

199266

Protocatechuate 3,4-dioxygenase. Inhibitor studies and mechanistic implications

1977

Que, L.; Lipscomb, J.D.; Munck, E.; Wood, J.M.

Biochim. Biophys. Acta

485

60-74

439500

1252412

Protocatechuate 3, 4-dioxygenase from Acinetobacter calcoaceticus

1976

Hou, C.T.; Lillard, M.O.; Schwartz, R.D.

Biochemistry

15

582-588

439501

6766312

Intergeneric evolutionary homology revealed by the study of protocatechuate 3,4-dioxygenase from Azotobacter vinelandii

1980

Durham, D.R.; Stirling, L.A.; Ornsten, L.N.; Perry, J.J.

Biochemistry

19

149-155

439505

8772173

Purification and characterization of a novel type of protocatechuate 3,4-dioxygenase with the ability to oxidize 4-sulfocatechol

1996

Hammer, A.; Stolz, A.; Knackmuss, H.J.

Arch. Microbiol.

166

92-100

439513

11454212

Cloning of the genes for a 4-sulphocatechol-oxidizing protocatechuate 3,4-dioxygenase from Hydrogenophaga intermedia S1 and identification of the amino acid residues responsible for the ability to convert 4-sulphocatechol

2001

Contzen, M.; Burger, S.; Stolz, A.

Mol. Microbiol.

41

199-205

439569

19416

Comparison of two dioxygenases from Pseudomonas putida

1977

Lee, Y.L.; Dagley, S.

J. Bacteriol.

131

1016-1017

439603

2261999

Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C

1990

Roper, D.I.; Cooper, R.A.

FEBS Lett.

275

53-57

439605

588248

Degradation of (+/-)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde

1977

Kutty, R.K.; Devi, N.A.; Veeraswamy, M.; Ramesh, S.; Rao, P.V.S.

Biochem. J.

167

163-170

439607

6243936

Involvement of superoxide in the reactions of the catechol dioxygenases

1980

Mayer, R.; Widom, J.; Que, L.

Biochem. Biophys. Res. Commun.

92

285-291

439614

6270137

3,4-Dihydroxyphenylacetate 2,3-dioxygenase. A manganese(II) dioxygenase from Bacillus brevis

1981

Que, L.; Widom, J.; Crawford, R.L.

J. Biol. Chem.

256

10941-10944

439615

-

Phenylalanine and tyrosine catabolism in some cheese coryneform bacteria

1985

Lee, C.W.; Lucas, S.; Desmazeaud, M.J.

FEMS Microbiol. Lett.

26

201-205

439616

3309170

Isolation from urine of two Serratia marcescens strains excreting a diffusible yellow pigment

1987

Trias, J.; Vinas, M.; Guinea, J.; Loren, J.G.

J. Gen. Microbiol.

133

773-777

439617

3121590

Catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO1 via meta cleavage of homoprotocatechuic acid

1988

Cuskey, S.M.; Olsen, R.H.

J. Bacteriol.

170

393-399

439618

838683

Purification and properties of homoprotocatechuate 2,3-dioxygenase from Bacillus stearothermophilus

1977

Jamaluddin, M.P.

J. Bacteriol.

129

690-697

439619

931949

Catabolism of L-tyrosine by the homoprotocatechuate pathway in gram-positive bacteria

1976

Sparnins, V.L.; Chapman, P.J.

J. Bacteriol.

127

362-366

439620

4420192

Bacterial degradation of 4-hydroxyphenylacetic acid and homoprotocatechuic acid

1974

Sparnins, V.L.; Chapman, P.J.; Dagley, S.

J. Bacteriol.

120

159-167

439621

4770367

Studies on 3,4-dihydroxyphenylacetate 2,3-dioxygenase. I. Role of iron, substrate binding, and some other properties

1973

Ono-Kamimoto, M.

J. Biochem.

74

1049-1059

439622

4837446

Studies on 3,4-dihydroxyphenylacetate-2,3-dioxygenase. II. Role of sulfhydryl groups and subunit structure

1974

Ono-Kamimoto, M.; Senoh, S.

J. Biochem.

75

321-331

439623

8621411

Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity

1996

Miller, M.A.; Lipscomb, J.D.

J. Biol. Chem.

271

5524-5535

439624

9047314

Manganese(II) active site mutants of 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Arthrobacter globiformis strain CM-2

1997

Boldt, Y.R.; Whiting, A.K.; Wagner, M.L.; Sadowsky, M.J.; Que, L.Jr.; Wackett, L.P.

Biochemistry

36

2147-2153

439625

9179284

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