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  • In Vivo Product
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• • k_cat Value (Turnover Number)
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Ligand 4-methylcatechol

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 4-methylcatechol

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (10 results)

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Show Natural Substrate (10 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.1

4-methylcatechol + O2 = 4-methyl-1,2-benzoquinone + H2O

673779

-

1.10.3.1

2 4-methylcatechol + O2 = 2 4-methyl-1,2-benzoquinone + 2 H2O

744954, 713387, 744955

-

1.13.11.1

4-methylcatechol + O2 = (2Z,4Z)-3-methylhexa-2,4-dienedioate

680483

1dmh, 3D-view

1.13.11.1

4-methylcatechol + O2 = (2Z,4Z)-3-methylhexa-2,4-dienedioate

680483

3hjs, 3D-view

1.13.11.1

4-methylcatechol + O2 = 3-methyl-cis,cis-hexadienedioate

680483

1dmh, 3D-view

1.13.11.1

4-methylcatechol + O2 = 3-methyl-cis,cis-hexadienedioate

680483

3hjs, 3D-view

1.13.11.1

4-methylcatechol + O2 = 3-methylhexa-2,4-dienedioate

648899

1dmh, 3D-view

1.13.11.1

4-methylcatechol + O2 = 3-methylhexa-2,4-dienedioate

648899

3hjs, 3D-view

1.14.18.1

4-methylcatechol + O2 = ?

745136

-

1.14.18.1

2 4-methylcatechol + O2 = 2 4-methyl-1,2-benzoquinone + 2 H2O

746341, 746276, 745557

-

1.10.3.1

2 entries

1.13.11.1

6 entries

1.14.18.1

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (5 results)

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Show Natural Product (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.1

4-methylsalicylate + NADH + 2 H+ + O2 = 4-methylcatechol + NAD+ + H2O + CO2

-

-

1.14.13.1

5-methylsalicylate + NADH + 2 H+ + O2 = 5-methylcatechol + NAD+ + H2O + CO2

-

-

1.14.13.1

2 entries

1.14.14.20

4-methylphenol + FADH2 + O2 = 4-methylcatechol + FAD + H2O

-

-

1.3.1.67

cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + NAD+ = 4-methylcatechol + NADH + H+ + CO2

288487

-

1.3.1.67

cis-p-toluate diol + NAD+ = 4-methylcatechol + NADH + H+ + CO2

288487

-

1.3.1.67

2 entries

Substrate in Enzyme-catalyzed Reactions (61 results)

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Show Substrate (61 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.1

4-methylcatechol + O2 = 4-methyl-1,2-benzoquinone

686666, 440436, 440434

-

1.10.3.1

4-methylcatechol + O2 = 4-methyl-o-benzoquinone

440427, 658788, 440426

-

1.10.3.1

4-methylcatechol + O2 = 4-methyl-1,2-benzoquinone + H2O

674108, 674089, 674142, 675458, 674092, 658787, 675167, 674090, 676649, 658960, 671593, 676381, 675101, 673779, 713239, 712219

-

1.10.3.1

4-methylcatechol + O2 = ?

658950, 699242, 727645, 701760, 706120

-

1.10.3.1

2 4-methylcatechol + O2 = 2 4-methyl-1,2-benzoquinone + 2 H2O

744954, 713387, 744955, 726187

-

1.10.3.1

2 4-methylcatechol + O2 = 2 4-methyl-1,2-benzoquinone

744661

-

1.10.3.2

4-methylcatechol + O2 = 6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O

396398, 396358, 396394, 396380, 396352, 396357, 396369

-

1.10.3.2

4-methylcatechol + O2 = ? + H2O

655627, 655362

-

1.10.3.2

4-methylcatechol + O2 = ?

742691

-

1.10.3.2

4-methyl catechol + O2 = ?

697664, 671391

-

1.10.3.2

4-methylbenzene-1,2-diol + O2 = ?

724662

-

1.10.3.1

6 entries

1.10.3.2

5 entries

1.11.1.14

4-methylcatechol + H2O2 = ?

702714

-

1.11.1.7

4-methylcatechol + H2O2 = ?

695687

-

1.13.11.1

4-methylcatechol + O2 = (2Z,4Z)-3-methylhexa-2,4-dienedioate

394982, 394980, 395005, 394988, 394995, 394996, 395004, 394983, 395006, 394993, 395002, 394989, 394991, 395001, 395008, 395003, 395009, 680483, 394990, 394998, 394987

1dmh, 3D-view

1.13.11.1

4-methylcatechol + O2 = (2Z,4Z)-3-methylhexa-2,4-dienedioate

394982, 394980, 395005, 394988, 394995, 394996, 395004, 394983, 395006, 394993, 395002, 394989, 394991, 395001, 395008, 395003, 395009, 680483, 394990, 394998, 394987

3hjs, 3D-view

1.13.11.1

4-methylpyrocatechol + O2 = 2,4,5-trimethyl-cis-cis-muconate

395007

1dmh, 3D-view

1.13.11.1

4-methylpyrocatechol + O2 = 2,4,5-trimethyl-cis-cis-muconate

395007

3hjs, 3D-view

1.13.11.1

4-methylcatechol + O2 = 3-methyl-cis,cis-muconate

658329, 671650, 659017, 659536, 676763, 675335

1dmh, 3D-view

1.13.11.1

4-methylcatechol + O2 = 3-methyl-cis,cis-muconate

658329, 671650, 659017, 659536, 676763, 675335

3hjs, 3D-view

1.13.11.1

4-methylcatechol + O2 = ?

743243, 697533, 697245, 697316, 743749

1dmh, 3D-view

1.13.11.1

4-methylcatechol + O2 = ?

743243, 697533, 697245, 697316, 743749

3hjs, 3D-view

1.13.11.1

4-methylcatechol + O2 = 4-methyl-cis,cis-muconate

712893, 711314, 723960

1dmh, 3D-view

1.13.11.1

4-methylcatechol + O2 = 4-methyl-cis,cis-muconate

712893, 711314, 723960

3hjs, 3D-view

1.13.11.1

4-methylcatechol + O2 = 3-methyl-cis,cis-hexadienedioate

680483

1dmh, 3D-view

1.13.11.1

4-methylcatechol + O2 = 3-methyl-cis,cis-hexadienedioate

680483

3hjs, 3D-view

1.13.11.1

4-methylcatechol + O2 = 3-methylhexa-2,4-dienedioate

648899

1dmh, 3D-view

1.13.11.1

4-methylcatechol + O2 = 3-methylhexa-2,4-dienedioate

648899

3hjs, 3D-view

1.13.11.2

4-methylcatechol + O2 = 2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate

680435, 677966

3hpy, 3D-view

1.13.11.2

4-methylcatechol + O2 = 2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate

680435, 677966

5znh, 3D-view

1.13.11.2

4-methylcatechol + O2 = 2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate

439584, 439561, 439588, 439568, 439577, 439581, 439360, 439566, 439576, 439589, 439578, 741500, 439571, 439591, 743104, 743838, 743800

3hpy, 3D-view

1.13.11.2

4-methylcatechol + O2 = 2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate

439584, 439561, 439588, 439568, 439577, 439581, 439360, 439566, 439576, 439589, 439578, 741500, 439571, 439591, 743104, 743838, 743800

5znh, 3D-view

1.13.11.2

4-methylcatechol + O2 = 2-hydroxy-4-methylmuconate semialdehyde

659889, 657781, 659881, 659414

3hpy, 3D-view

1.13.11.2

4-methylcatechol + O2 = 2-hydroxy-4-methylmuconate semialdehyde

659889, 657781, 659881, 659414

5znh, 3D-view

1.13.11.2

4-methylcatechol + O2 = ?

724201, 723819, 726474, 685660, 677966, 687854

3hpy, 3D-view

1.13.11.2

4-methylcatechol + O2 = ?

724201, 723819, 726474, 685660, 677966, 687854

5znh, 3D-view

1.13.11.2

4-methylcatechol + O2 = 2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate + H+

390225

3hpy, 3D-view

1.13.11.2

4-methylcatechol + O2 = 2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate + H+

390225

5znh, 3D-view

1.13.11.1

14 entries

1.13.11.2

10 entries

1.13.11.25

4-methylcatechol = ?

439527

-

1.13.11.3

4-methylcatechol + O2 = 3-methyl-cis,cis-muconate

439502, 439505

-

1.13.11.3

4-methylcatechol + O2 = ?

725655

-

1.13.11.3

2 entries

1.13.11.36

4-methylpyrocatechol + O2 = 2-hydroxy-3-methylmuconic acid semialdehyde

439432

-

1.13.11.39

4-methylcatechol + O2 = 2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate

439410, 439412, 439404, 439409, 439414, 674226, 439416, 703749, 742574, 439407

-

1.13.11.39

4-methylcatechol + O2 = ?

725631, 659021, 659212, 685422, 724567

-

1.13.11.39

2 entries

1.13.11.56

4-methylcatechol + O2 = ?

698539, 698537

2ehz, 3D-view

1.14.13.166

4-methylcatechol + NADH + H+ + O2 = ? + NAD+ + H2O

719711

-

1.14.17.B1

4-methylcatechol + ascorbate + O2 = 4-methyl-o-benzoquinone + dehydroascorbate + H2O

636344

-

1.14.18.1

4-methylcatechol + O2 = 4-methyl-o-benzoquinone + H2O

636360, 636339, 636340, 636355, 636357, 636381, 636338, 636348, 636347, 636352, 636368, 636350, 636439, 636342, 636351, 636345, 636393, 636346, 636382, 636336, 636349, 636337, 636341, 636353, 636358, 636359, 636380, 636343, 636354, 636356, 636403, 636442

-

1.14.18.1

4-methyl catechol + O2 = 4-methyl-o-benzoquinone + H2O

659827

-

1.14.18.1

4-methylcatechol + O2 = 4-methyl-1,2-benzoquinone + H2O

713387, 699242, 711787, 712053, 713302, 712619

-

1.14.18.1

4-methylcatechol + O2 = ?

745136, 745746, 728714

-

1.14.18.1

4-methylcatechol + 1/2 O2 = 4-methyl-1,2-benzoquinone + H2O

685018, 686841, 687240, 684232, 687231, 686844, 686484, 686847, 685753, 686845

-

1.14.18.1

4-methyl-catechol + O2 = ?

698436

-

1.14.18.1

4-methylbenzene-1,2-diol + O2 = ?

700667

-

1.14.18.1

2 4-methylcatechol + O2 = 2 4-methyl-1,2-benzoquinone + 2 H2O

746341, 744824, 746276, 745557

-

1.14.18.1

8 entries

1.16.3.1

4-methylcatechol + Fe2+ + O2 = ?

438006

-

1.17.9.1

4-methylcatechol + acceptor + H2O = 3,4-dihydroxybenzaldehyde + reduced acceptor

437874, 288313

-

1.5.99.12

N6-(DELTA2-isopentenyl)adenine + 4-methylcatechol + H2O = adenine + 3-methylbut-2-enal + reduced 4-methylcatechol

656984

-

1.5.99.12

N6-(DELTA2-isopentenyl)adenosine + 4-methylcatechol + H2O = adenosine + 3-methylbut-2-enal + reduced 4-methylcatechol

656984

-

1.5.99.12

2 entries

2.1.1.6

S-adenosyl-L-methionine + 4-methylcatechol = S-adenosyl-L-homocysteine + ?

658517

-

2.1.1.68

S-adenosyl-L-methionine + homocatechol = S-adenosyl-L-homocysteine + 2-methoxy-4-methylphenol

485543

-

2.8.2.1

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

645671

-

Product in Enzyme-catalyzed Reactions (36 results)

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Show Product (36 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.12.12

m-cresol + NADH + O2 = methylhydroquinone + 3-methylcatechol + 4-methylcatechol + NAD+

-

-

1.14.12.12

p-cresol + NADH + O2 = 4-methylcatechol + NAD+

-

-

1.14.12.23

2-nitrotoluene + NADH + O2 = 4-methylcatechol + nitrite + NAD+

-

-

1.14.12.23

3-nitrotoluene + NADH + O2 = 3-methylcatechol + 4-methylcatechol + nitrite + NAD+

-

-

1.14.12.23

3-nitrotoluene + NADH + O2 = 4-methylcatechol + nitrite + NAD+

-

-

1.14.12.23

4-nitrotoluene + NADH + O2 = 4-methylcatechol + nitrite + NAD+

-

-

1.14.12.24

3-nitrotoluene + NADH + O2 = 4-methylcatechol + nitrite + NAD+

-

-

1.14.12.24

4-nitrotoluene + NADH + O2 = 4-methylcatechol + nitrite + NAD+

-

-

1.14.13.1

5-methylsalicylate + NADH + O2 = 1,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O

-

-

1.14.13.1

4-methylsalicylate + NADH + O2 = 1,2-dihydroxy-4-methylbenzene + CO2 + NAD+ + H2O

-

-

1.14.13.1

4-methylsalicylate + NADH + 2 H+ + O2 = 4-methylcatechol + NAD+ + H2O + CO2

-

-

1.14.13.1

5-methylsalicylate + NADH + 2 H+ + O2 = 4-methylcatechol + NAD+ + H2O + CO2

-

-

1.14.13.1

5-methylsalicylate + NADH + 2 H+ + O2 = 5-methylcatechol + NAD+ + H2O + CO2

-

-

1.14.13.1

4-methylsalicylate + NADH + H+ + O2 = 4-methylbenzene-1,2-diol + NAD+ + H2O + CO2

-

-

1.14.13.236

m-cresol + NADH + H+ + O2 = 4-methylcatechol + NAD+ + H2O

-

-

1.14.13.236

p-cresol + NADH + H+ + O2 = 4-methylcatechol + NAD+ + H2O

-

-

1.14.13.31

4-methyl-2-nitrophenol + NADPH + O2 = 4-methylcatechol + NADP+ + H2O

-

-

1.14.13.31

5-methyl-2-nitrophenol + NADPH + O2 = 5-methylcatechol + NADP+ + H2O

-

-

1.14.13.31

4-methyl-2-nitrophenol + NADPH + H+ + O2 = 4-methyl-catechol + NADP+ + H2O + nitrite

-

-

1.14.13.7

4-chlorophenol + NADH + H+ + O2 = 1,2-dihydroxy-4-methylbenzene + NAD+ + H2O

-

-

1.14.13.7

4-methylphenol + NADH + H+ + O2 = 1,2-dihydroxy-4-methylbenzene + NAD+ + H2O

-

-

1.14.13.7

m-cresol + NADH + H+ + O2 = 4-methylcatechol + NAD+ + H2O

-

-

1.14.13.7

p-cresol + NADH + H+ + O2 = 4-methylcatechol + NAD+ + H2O

-

-

1.14.13.7

p-cresol + NADPH + O2 = 4-methylcatechol + NADP+ + H2O

-

-

1.14.13.7

2 2-cresol + NADPH + O2 = 3-methylcatechol + 4-methylcatechol + NADP+ + H2O

-

-

1.14.13.7

3-cresol + NADPH + O2 = 3-methylcatechol + 4-methylcatechol + NADP+ + H2O

-

-

1.14.13.7

4-cresol + NADPH + O2 = 4-methylcatechol + NADP+ + H2O

-

-

1.14.13.7

m-cresol + NADPH + H+ + O2 = 3-methylcatechol + 4-methylcatechol + NADP+

-

-

1.14.13.7

4-cresol + NADPH + H+ + O2 = 4-methylcatechol + NADP+ + H2O

-

-

1.14.12.12

2 entries

1.14.12.23

4 entries

1.14.12.24

2 entries

1.14.13.1

6 entries

1.14.13.236

2 entries

1.14.13.31

3 entries

1.14.13.7

10 entries

1.14.14.20

4-methylphenol + FADH2 + O2 = 4-methylcatechol + FAD + H2O

-

-

1.14.18.1

p-cresol + O2 = 4-methylpyrocatechol + H2O

636352, 636393, 636359

-

1.14.18.1

p-cresol + O2 + AH2 = 4-methylcatechol + H2O + A

-

-

1.14.18.1

p-cresol + O2 + AH2 = 4-methylpyrocatechol + H2O + A

-

-

1.3.1.67

cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + NAD+ = 4-methylcatechol + NADH + H+ + CO2

288487

-

1.3.1.67

cis-p-toluate diol + NAD+ = 4-methylcatechol + NADH + H+ + CO2

288487

-

1.14.18.1

3 entries

1.3.1.67

2 entries

4.1.1.83

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

-

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.18.1

effect of a range of diphenol treatments on the activation of latent red clover PPO tested. 23.0% activation

687251

-

Inhibitor in Enzyme-catalyzed Reactions (18 results)

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Show Inhibitors (18 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.1

field bean PPO obeys Michaelis-Menten kinetics and exhibits the phenomenon of inhibition by excess substrate for catechol, 4-methylcatechol and 4-tert-butylcatechol

686666

-

1.13.11.1

-

394983, 394987

1dmh, 3D-view

1.13.11.1

-

394983, 394987

3hjs, 3D-view

1.13.11.1

2 entries

1.13.11.15

-

439614

-

1.13.11.2

suicide inhibition

439588

3hpy, 3D-view

1.13.11.2

suicide inhibition

439588

5znh, 3D-view

1.13.11.2

-

439593

3hpy, 3D-view

1.13.11.2

-

439593

5znh, 3D-view

1.13.11.3

0.006 mM, 59% inhibition

439500

-

1.13.11.3

-

439501

-

1.13.11.2

4 entries

1.13.11.3

2 entries

1.13.11.39

-

439411

-

1.13.11.56

0.0005 mM, 36% inhibition, competitive inhibitor

698537

2ehz, 3D-view

1.13.11.74

complete inhibition at 0.05 mM

722493

-

1.13.11.74

uncompetitive inhibition

722603

-

1.13.11.74

2 entries

1.14.11.29

-

725647

-

1.14.11.30

-

725647

-

1.14.18.1

substrate inhibition

636342

-

1.14.18.1

-

636351, 636352

-

1.14.18.1

2 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (7 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (7 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.11.1.15

4k7n, 3D-view

1.13.11.1

1dmh, 3D-view

1.13.11.1

3hjs, 3D-view

1.13.11.2

3hpy, 3D-view

1.13.11.2

5znh, 3D-view

1.13.11.1

2 entries

1.13.11.2

2 entries

1.13.11.56

2ehz, 3D-view

2.4.2.21

1l4g, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (35 results)

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Show Turnover Number (35 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.10.3.1

26.66

-

-

686666

1.10.3.1

841.6

-

-

675458

1.10.3.1

842

-

pH 7.0

674142

1.10.3.1

2340

-

-

675458

1.10.3.1

4 entries

1.10.3.2

93.9

-

pH 3.8, 55°C

671391

1.13.11.1

0.72

-

mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication

711314

1.13.11.1

1.6

-

-

395008

1.13.11.1

2.7

-

pH not specified in the publication, 25°C

680483

1.13.11.1

4

-

-

395002

1.13.11.1

5.45

-

wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication

711314

1.13.11.1

5.51

-

mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication

711314

1.13.11.1

5.6

-

25°C

671650

1.13.11.1

5.6

-

-

676763

1.13.11.1

6.3

-

-

395005

1.13.11.1

7.32

-

in 50 mM Tris/HCl, pH 7.2, 25°C

712893

1.13.11.1

12

-

rate dependent on the nucleophilic reactivity

395004

1.13.11.1

20.7

-

pH not specified in the publication, 25°C

680483

1.13.11.2

0.76

-

pH 7.5, 25°C

726474

1.13.11.2

4.7

-

pH 7.5, 60°C

726474

1.13.11.2

53

-

strain 1YB2, pH 7.5, 25°C

659889

1.13.11.2

64

-

strain 1YdBTEX2, pH 7.5, 25°C

659889

1.13.11.2

930

-

-

439588

1.13.11.39

0.064

-

25°C, pH 7.5

659021

1.13.11.39

0.24

-

25°C, pH 7.5

659021

1.13.11.39

0.36

-

25°C, pH 7.5

659021

1.13.11.39

0.7

-

pH 8.0, 20°C

703749

1.13.11.39

1

-

25°C; 60°C

685422

1.13.11.39

1.19

-

pH 7.5, 30°C

725631

1.13.11.39

2

-

25°C

685422

1.13.11.39

3.25

-

pH 7.5, 30°C

725631

1.13.11.39

43.2

-

pH 7.5, 30°C

725631

1.14.18.1

12

-

recombinant enzyme, pH 7.2, 37°C

745746

1.14.18.1

842

-

-

636439

1.14.18.1

842.1

-

-

685018

1.14.18.1

7220

-

-

636347

1.13.11.1

12 entries

1.13.11.2

5 entries

1.13.11.39

9 entries

1.14.18.1

4 entries

K_M Value (110 results)

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Show KM Value (110 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.10.3.1

0.12

-

pH 7.0

674142

1.10.3.1

1.2

-

pH 7.0, 25°C

674090

1.10.3.1

1.25

-

pH 3.5, 25°C

675101

1.10.3.1

1.809

-

-

699242

1.10.3.1

1.9

-

-

675458

1.10.3.1

2.36

-

-

675458

1.10.3.1

2.77

-

pH 6.0, 25°C

674089

1.10.3.1

3.44

-

-

706120

1.10.3.1

3.88

-

pH 5.0, 20°C

744955

1.10.3.1

4

-

-

440434

1.10.3.1

4.5

-

-

686666

1.10.3.1

5.2

-

-

686666

1.10.3.1

6.58

-

pH 6.0, 25°C, leaf enzyme

673779

1.10.3.1

6.78

-

pH 6.0, 25°C, stem enzyme

673779

1.10.3.1

8

-

pH 6.0, 30°C

744661

1.10.3.1

8.3

-

pH 6.5, 25°C

676649

1.10.3.1

9.86

-

-

706120

1.10.3.1

10

-

pH 7.0, 50°C

713387

1.10.3.1

11.6

-

-

658960

1.10.3.2

0.175

-

-

396394

1.10.3.2

1

-

-

396380

1.10.3.2

1.56

-

isoenzyme lac90

396398

1.10.3.2

4.5

-

-

396358

1.13.11.1

0.0012

-

-

395005

1.13.11.1

0.0017

-

pH not specified in the publication, 25°C

680483

1.13.11.1

0.00284

-

mutant L69G/A72G

697316

1.13.11.1

0.0035

-

at pH 7.2 and 45°C

743243

1.13.11.1

0.004

-

in 50 mM Tris/HCl, pH 7.2, 25°C

712893

1.13.11.1

0.0068

-

-

394987

1.13.11.1

0.0099

-

pH not specified in the publication, 25°C

680483

1.13.11.1

0.01

-

mutant A72G

697316

1.13.11.1

0.01

-

mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication

711314

1.13.11.1

0.0128

-

mutant L69A

697316

1.13.11.1

0.0128

-

mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication

711314

1.13.11.1

0.013

-

-

676763

1.13.11.1

0.014

-

-

395008

1.13.11.1

0.018

-

-

395002

1.13.11.1

0.0215

-

25°C

671650

1.13.11.1

0.053

-

wild-type enzyme

697316

1.13.11.1

0.053

-

wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication

711314

1.13.11.1

0.09

-

-

395004

1.13.11.1

0.0936

-

mutant A72D

697316

1.13.11.1

0.213

-

mutant A72S

697316

1.13.11.1

0.4

-

-

697245

1.13.11.1

0.435

-

mutant A72N

697316

1.13.11.2

0.00129

-

-

439589

1.13.11.2

0.0017

-

-

439588

1.13.11.2

0.0019

-

strain 1YB2, pH 7.5, 25°C

659889

1.13.11.2

0.0025

-

pH 8.0, 35°C, immobilized enzyme

724201

1.13.11.2

0.003

-

pH 7.5, 25°C

726474

1.13.11.2

0.0052

-

strain 1YdBTEX2, pH 7.5, 25°C

659889

1.13.11.2

0.006

-

-

439588

1.13.11.2

0.008

-

metapyrocatechase 2

439568

1.13.11.2

0.0084

-

25°C, pH 7.2

687854

1.13.11.2

0.0109

-

-

439581

1.13.11.2

0.012

-

pH 7.5, 60°C

726474

1.13.11.2

0.02

-

metapyrocatechase 1

439568

1.13.11.2

0.0425

-

pH 8.0, 35°C, free enzyme

724201

1.13.11.2

0.05

-

-

439360

1.13.11.2

1.1

-

-

439566

1.10.3.1

19 entries

1.10.3.2

4 entries

1.13.11.1

22 entries

1.13.11.2

15 entries

1.13.11.3

0.014

-

pH 7.5, 38°C

725655

1.13.11.36

0.16

-

-

439432

1.13.11.39

0.0273

-

pH 7.5, 30°C

725631

1.13.11.39

0.11

-

60°C, pH 7.5

659212

1.13.11.39

0.2824

-

pH 7.5, 30°C

725631

1.13.11.39

0.3597

-

pH 8.0, 20°C

703749

1.13.11.39

0.3605

-

pH 7.5, 30°C

725631

1.13.11.39

2.8

-

25°C, pH 7.5

659021

1.13.11.39

5.6

-

25°C

685422

1.13.11.39

7.6

-

60°C

685422

1.13.11.39

11

-

25°C

685422

1.13.11.39

61

-

25°C, pH 7.5

659021

1.13.11.39

93

-

25°C, pH 7.5

659021

1.14.18.1

0.1

-

-

685018

1.14.18.1

0.15

-

pH 6.5, 28°C

745557

1.14.18.1

0.17

-

; in H2O

636351

1.14.18.1

0.2

-

in MOPS buffer, pH 7.0

636342

1.14.18.1

0.2

-

measured in bis(2-ethylhexyl)sodium sulfosuccinate-isooctane reverse micelles

636351

1.14.18.1

0.3

-

in aqueous solution

685753

1.14.18.1

0.5

-

in CHCl3

685753

1.14.18.1

0.9

-

-

636393

1.14.18.1

1

-

-

686845

1.14.18.1

1.15

-

-

636450

1.14.18.1

2.36

-

-

636439

1.14.18.1

2.5

-

-

636399

1.14.18.1

2.5

-

recombinant enzyme, pH 7.2, 37°C

745746

1.14.18.1

2.62

-

apparent value

700667

1.14.18.1

2.7

-

-

636442

1.14.18.1

2.8

-

pH 8.0, 20°C

712053

1.14.18.1

3.14

-

pH 7.0, 25°C

745136

1.14.18.1

3.2

-

-

636382

1.14.18.1

3.3

-

-

636403

1.14.18.1

4

5

in poly-(10)-oxyethylene oleyl ether-cyclohexane reverse micelles

636358

1.14.18.1

4

-

in ternary solution composed of hexane-isopropanol-water

636342

1.14.18.1

4.2

-

-

636352

1.14.18.1

4.75

-

-

636347

1.14.18.1

5

-

-

636380

1.14.18.1

5.13

-

-

636381

1.14.18.1

5.2

-

at pH 3.5-5.0, strong increase in Km above pH 5.0

636336

1.14.18.1

6.9

-

-

686847

1.14.18.1

9

-

-

636358

1.14.18.1

10

-

pH 7.0, 50°C

713387

1.14.18.1

15

-

in ternary solution composed of toluene-isopropanol-water

636342

1.14.18.1

20.5

-

at pH 6.3, strong increase in Km above pH 5.0

636336

1.14.18.1

21

-

polyphenol oxidase shows the best activity toward catechol and 4-methyl catechol

686841

1.14.18.1

33

-

in 1-butyl-3-methylimidazolium hexafluorophosphate, much higher than those obtained in CHCl3 and aqueous solution

685753

1.14.18.1

2000

-

-

686484

1.13.11.39

11 entries

1.14.18.1

34 entries

1.16.3.1

0.0603

-

-

438006

1.17.9.1

0.26

-

-

288313

2.1.1.68

0.04

-

isozyme I

485543

K_i Value (6 results)

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Show KI Value (6 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.15

1.5

-

-

439614

1.13.11.3

0.44

-

-

439500

1.13.11.74

0.0095

-

pH and temperature not specified in the publication

722603

1.14.18.1

0.23

-

in bis(2-ethylhexyl)sodium sulfosuccinate-isooctane reverse micelles

636351

1.14.18.1

3.6

-

in H2O, substrate inhibition

636351

1.14.18.1

104

-

weak substrate inhibition

636352

1.14.18.1

3 entries

IC₅₀ Value (2 results)

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Show IC50 Value (2 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.14.11.29

0.004

-

pH 7.0, 37°C

725647

1.14.11.30

0.05

-

pH 7.0, 37°C

725647

References & Links

Literature References (212)

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Show Reference (212 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

288313

2722739

Anaerobic oxidation of p-cresol mediated by a partially purified methylhydroxylase from a denitrifying bacterium

1989

Bossert, I.D.; Whited, G.; Gibson, D.T.; Young, L.Y.

J. Bacteriol.

171

2956-2962

288487

3711022

Identification of cis-diols as intermediates in the oxidation of aromatic acids by a strain of Pseudomonas putida that contains a TOL plasmid

1986

Whited, M.G.; McCombie, W.R.

J. Bacteriol.

166

1028-1039

390225

7868591

Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida

1995

Inoue, J.; Shaw, J.P.; Rekik, M.; Harayama, S.

J. Bacteriol.

177

1196-1201

394980

-

Direct oxygenation by O2. Oxygenases

1963

Hayaishi, O.

The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbäck, K. , eds. )

8

353-371

394982

-

Catechol 1,2-dioxygenase from Aspergillus niger

1981

Ninnekar, H.Z.; Vaidyanathan, C.S.

J. Indian Inst. Sci.

63C

131-136

394983

58860

Catechol 1,2-dioxygenase from Acinetobacter calcoaceticus: purification and properties

1976

Patel, R.N.; Hou, C.T.; Felix, A.; Lillard, M.O.

J. Bacteriol.

127

536-544

394987

-

Characteristics of a new catechol 1,2-oxygenase from Trichosporon cutaneum WY 2-2

1981

Itoh, M.

Agric. Biol. Chem.

45

2787-2796

394988

6643492

Rapid reaction studies on the oxygenation reactions of catechol dioxygenase

1983

Walsh, T.A.; Ballou, D.P.; Mayer, R.; Que, L.

J. Biol. Chem.

258

14422-14427

394989

-

Purification and characterization of catechol 1,2-dioxygenase from aniline-assimilating Rhodococcus erythropolis AN-13

1984

Aoki, K.; Konohana, T.; Shinke, R.; Nishira, H.

Agric. Biol. Chem.

48

2087-2095

394990

-

Two catechol 1,2-dioxygenases from an aniline-assimilating bacterium, Frateuria species ANA-18.

1984

Aoki, K.; Konohana, T.; Shinke, R.; Nishira, H.

Agric. Biol. Chem.

48

2097-2104

394991

-

Aromatic metabolism in Rhizobium trifolii: catechol 1,2-dioxygenase

1985

Chen, Y.P.; Glenn, A.R.; Dilworth, M.J.

Arch. Microbiol.

141

225-228

394993

3783431

Degradation of phenolic compounds by the yeast Candida tropicalis HP 15. II. Some properties of the first two enzymes of the degradation pathway

1986

Krug, M.; Straube, G.

J. Basic Microbiol.

26

271-281

394995

3214177

Purification and properties of catechol 1,2-dioxygenase (pyrocatechase) from Pseudomonas putida mt-2 in comparison with that from Pseudomonas arvilla C-1

1988

Nakai, C.; Nakazawa, T.; Nozaki, M.

Arch. Biochem. Biophys.

267

701-713

394996

2295613

Three isoenzymes of catechol 1,2-dioxygenase (pyrocatechase) alphaalpha, alphabeta, and betabeta from Pseudomonas arvilla C-1

1980

Nakai, C.; Horiike, K.; Kuramitsu, S.; Kagamiyama, H.; Nozaki, M.

J. Biol. Chem.

265

660-665

394998

-

Properties of cyanogen bromide-activated, agarose-immobilized catechol 1,2-dioxygenase from freeze-dried extracts of Nocardia sp. NCIB 10503

1990

Smith, M.R.; Ratledge, C.; Crook, S.

Enzyme Microb. Technol.

12

945-949

395001

14056355

Characteristics of catechol oxygenase from Brevibacterium fuscum

1963

Nakagawa, H.; Inoue, H.; Takeda, Y.

J. Biochem.

54

65-74

395002

8661943

Characterization of a chromosomally encoded catechol 1,2-dioxygenase (E.C. 1.13.11.1) from Alcaligenes eutrophus CH34

1996

Sauret-Ignazi, G.; Gagnon, J.; Beguin, C.; Barrelle, M.; Markowicz, J.; Pelmont, J.; Toussaint, A.

Arch. Microbiol.

166

42-50

395003

9369233

Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens

1997

Briganti, F.; Pessione, E.; Giunta, C.; Scozzafava, A.

FEBS Lett.

416

61-64

395004

9799107

Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1

1998

Ridder, L.; Briganti, F.; Boersma, M.G.; Boeren, S.; Vis, E.H.; Scozzafava, A.; Veeger, C.; Rietjens, I.M.C.M.

Eur. J. Biochem.

257

92-100

395005

-

Purification and characterization of catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259 and cloning and sequencing of its catA gene

1998

Strachan, P.D.; Freer, A.A.; Fewson, C.A.

Biochem. J.

333

741-747

395006

9760749

Purification and characterization of four catechol 1,2-dioxygenase isoenzymes from the benzamide-assimilating bacterium Arthrobacter species BA-5-17

1998

Murakami, S.; Wang, C.L.; Naito, A.; Shinke, R.; Aoki, K.

Microbiol. Res.

153

163-171

395007

10424908

Isolation and characterization of catechol 1,2-dioxygenases from Rhodococcus rhodnii strain 135 and Rhodococcus rhodochrous strain 89: comparison with analogous enzymes of the ordinary and modified ortho-cleavage pathways

1999

Solyanikova, I.P.; Golovlev, E.L.; Lisnyak, O.V.; Golovleva, L.A.

Biochemistry (Moscow)

64

824-831

395008

11676005

Production of catechol from benzoate by the wild strain Ralstonia species Ba-0323 and characterization of its catechol 1,2-dioxygenase

2001

Wang, C.L.; Takenaka, S.; Murakami, S.; Aoki, K.

Biosci. Biotechnol. Biochem.

65

1957-1964

395009

11307956

Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens

2000

Briganti, F.; Pessione, E.; Giunta, C.; Mazzoli, R.; Scozzafava, A.

J. Protein Chem.

19

709-716

396352

-

Purification and properties of two laccase isoenzymes produced by Botrytis cinerea

1987

Zouari, N.; Romette, J.L.; Thomas, D.

Appl. Biochem. Biotechnol.

15

213-225

396357

-

Molecular properties of extracellular Botrytis cinerea laccase

1984

Marbach, I.; Harel, E.; Mayer, A.M.

Phytochemistry

23

2713-2717

396358

6847630

Excretion of laccase by sycamore (Acer pseudoplatanus L.) cells. Purification and properties of the enzyme

1983

Bligny, R.; Douce, R.

Biochem. J.

209

489-496

396369

-

Laccase in Anacardiaceae

1978

Joel, D.M.; Marbach, I.; Mayer, A.M.

Phytochemistry

17

796-797

396380

-

A laccase-like enzyme in peaches

1968

Mayer, A.M.; Harel, E.

Phytochemistry

7

1253-1256

396394

-

Substrate specificity of laccase from Lentinus edodes

1996

D'Annibale, A.; Celletti, D.; Felici, M.; Di Mattia, E.; Giovannozzi-Sermanni, G.

Acta Biotechnol.

16

257-270

396398

9914531

Biochemical characterization, molecular cloning and expression of laccases - a divergent gene family - in poplar

1999

Ranocha, P.; McDougall, G.; Hawkins, S.; Sterjiades, R.; Borderies, G.; Stewart, D.; Cabanes-MacHeteau, M.; Boudet, A.M.; Goffner, D.

Eur. J. Biochem.

259

485-495

437874

2990444

p-Cresol methylhydroxylase. assay and general properties

1985

McIntire, W.; Hopper, D.J.; Singer, T.P.

Biochem. J.

228

325-335

438006

775938

Ceruloplasmin: the copper transport protein with essential oxidase activity

1976

Frieden, E.; Hsieh, H.S.

Adv. Enzymol. Relat. Areas Mol. Biol.

44

187-236

439360

2997190

Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases

1985

Arciero, D.M.; Orville, A.M.; Lipscomb, J.D.

J. Biol. Chem.

260

14035-14044

439404

3063207

Molecular cloning of 3-phenylcatechol dioxygenase involved in the catabolic pathway of chlorinated biphenyl from Pseudomonas putida and its expression in Escherichia coli

1988

Khan, A.; Tewari, R.; Walia, S.

Appl. Environ. Microbiol.

54

2664-2671

439407

8428946

Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase

1993

Eltis, L.D.; Hofmann, B.; Hecht, H.J.; Luensdorf, H.; Timmis, K.N.

J. Biol. Chem.

268

2727-2732

439409

-

Comparison of enzymic and immunochemical properties of 2,3-dihydroxybiphenyl-1,2-dioxygenases from four Pseudomonas strains

1994

Lee, J.; Sung, T.K.; Moon, J.; Min, K.R.; Kim, C.K.; Kim, Y.

FEMS Microbiol. Lett.

120

355-362

439410

7768806

Molecular and biochemical characterization of two meta-cleavage dioxygenases involved in biphenyl and m-xylene degradation by Beijerinckia sp. strain B1

1995

Kim, E.; Zylstra, G.J.

J. Bacteriol.

177

3095-3103

439411

-

Inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase from Pseudomonas sp. strain CB406 by 3,4-dihydroxybiphenyl (4-phenylcatechol)

1995

Lloyd-Jones, G.; Ogden, R.C.; Williams, P.A.

Biodegradation

6

11-17

439412

8702287

Identification of an alternative 2,3-dihydroxybiphenyl 1,2-dioxygenase in Rhodococcus sp. strain RHA1 and cloning of the gene

1996

Hauschild, J.E.; Masai, E.; Sugiyama, K.; Hatta, T.; Kimbara, K.; Fukuda, M.; Yano, K.

Appl. Environ. Microbiol.

62

2940-2946

439414

9228766

Rapid purification of an active recombinant His-tagged 2,3-dihydroxybiphenyl 1,2-dioxygenase from Pseudomonas putida OU83

1997

Khan, A.A.; Nawaz, M.S.; Cerniglia, C.E.

FEMS Microbiol. Lett.

152

23-29

439416

-

The 2,3-dihydroxybiphenyl 1,2-dioxygenase gene (phnQ) of Pseudomonas sp. DJ77: nucleotide sequence, enzyme assay, and comparison with isofunctional dioxygenases

1999

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