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  • In Vivo Product
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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

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

744954, 713387, 744955

-

1.10.3.1

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

673779

-

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

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

746341, 746276, 745557

-

1.14.18.1

4-methylcatechol + O2 = ?

745136

-

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 (62 results)

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Show Substrate (62 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.1

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

744661

-

1.10.3.1

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

744954, 713387, 744955, 726187

-

1.10.3.1

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

440436, 686666, 440434

-

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 = 4-methyl-o-benzoquinone

440427, 658788, 440426

-

1.10.3.1

4-methylcatechol + O2 = ?

658950, 699242, 727645, 701760, 706120

-

1.10.3.2

4-methyl catechol + O2 = ?

697664, 671391

-

1.10.3.2

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

724662

-

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 = ?

742691

-

1.10.3.2

4-methylcatechol + O2 = ? + H2O

655627, 655362

-

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-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-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 = 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

1.13.11.1

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 = ?

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-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

1.13.11.2

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

439561, 439584, 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

439561, 439584, 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-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-4-methylmuconate semialdehyde

657781, 659889, 659881, 659414

3hpy, 3D-view

1.13.11.2

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

657781, 659889, 659881, 659414

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

1.13.11.2

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

1.13.11.1

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

-

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

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

746341, 744824, 746276, 745557

-

1.14.18.1

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

659827

-

1.14.18.1

4-methyl-catechol + O2 = ?

698436

-

1.14.18.1

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

700667

-

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-methylcatechol + O2 = 4-cresol + H2O

636399

-

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 = 4-methyl-o-benzoquinone + H2O

636360, 636339, 636340, 636355, 636357, 636381, 636338, 636348, 636347, 636352, 636368, 636350, 636342, 636351, 636439, 636345, 636393, 636346, 636336, 636382, 636349, 636337, 636341, 636353, 636358, 636359, 636380, 636450, 636343, 636354, 636356, 636403, 636442

-

1.14.18.1

4-methylcatechol + O2 = ?

745136, 745746, 728714

-

1.14.18.1

9 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 (37 results)

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Show Product (37 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.2.6

4-cresol + H2O2 = 4-methylcatechol + H2O

-

-

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

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

-

-

1.14.13.1

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

-

-

1.14.13.1

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

-

-

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

-

-

1.14.13.236

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 + H+ + O2 = 4-methyl-catechol + NADP+ + H2O + nitrite

-

-

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

-

-

1.14.13.7

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

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

-

-

1.14.13.7

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

-

-

1.14.13.7

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

-

-

1.14.13.7

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

-

-

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

-

-

1.14.12.12

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 + AH2 = 4-methylcatechol + H2O + A

-

-

1.14.18.1

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

-

-

1.14.18.1

p-cresol + O2 = 4-methylpyrocatechol + H2O

636352, 636393, 636359,

-

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

-

439593

3hpy, 3D-view

1.13.11.2

-

439593

5znh, 3D-view

1.13.11.2

suicide inhibition

439588

3hpy, 3D-view

1.13.11.2

suicide inhibition

439588

5znh, 3D-view

1.13.11.3

-

439501

-

1.13.11.3

0.006 mM, 59% inhibition

439500

-

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

-

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

-

636351, 636352

-

1.14.18.1

substrate inhibition

636342

-

1.14.18.1

2 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (38 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (38 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

1.13.11.1

1dmh, 3D-view

1.13.11.1

3hjs, 3D-view

1.13.11.1

1dmh, 3D-view

1.13.11.1

3hjs, 3D-view

1.13.11.1

1dmh, 3D-view

1.13.11.1

3hjs, 3D-view

1.13.11.1

1dmh, 3D-view

1.13.11.1

3hjs, 3D-view

1.13.11.1

1dmh, 3D-view

1.13.11.1

3hjs, 3D-view

1.13.11.1

1dmh, 3D-view

1.13.11.1

3hjs, 3D-view

1.13.11.1

1dmh, 3D-view

1.13.11.1

3hjs, 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

1.13.11.2

3hpy, 3D-view

1.13.11.2

5znh, 3D-view

1.13.11.2

3hpy, 3D-view

1.13.11.2

5znh, 3D-view

1.13.11.2

3hpy, 3D-view

1.13.11.2

5znh, 3D-view

1.13.11.2

3hpy, 3D-view

1.13.11.2

5znh, 3D-view

1.13.11.2

3hpy, 3D-view

1.13.11.2

5znh, 3D-view

1.13.11.2

3hpy, 3D-view

1.13.11.2

5znh, 3D-view

1.13.11.2

3hpy, 3D-view

1.13.11.2

5znh, 3D-view

1.13.11.2

3hpy, 3D-view

1.13.11.2

5znh, 3D-view

1.13.11.1

18 entries

1.13.11.2

18 entries

2.4.2.21

1l4g, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (36 results)

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Show Turnover Number (36 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

-

-

676763

1.13.11.1

5.6

-

25°C

671650

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

685422

1.13.11.39

1

-

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

10 entries

1.14.18.1

4 entries

K_M Value (111 results)

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Show KM Value (111 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 enzyme L69A, 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

0.013

-

-

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

711314

1.13.11.1

0.053

-

wild-type enzyme

697316

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

-

-

636351

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

-

in ternary solution composed of hexane-isopropanol-water

636342

1.14.18.1

4

5

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

636358

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

35 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)

top print hide

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 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

Kim, S.J.; Shin, H.J.; Park, Y.C.; Kim, Y.; Min, K.H.; Kim, Y.C.

J. Biochem. Mol. Biol.

32

399-404

439432

19349

Catechol 2,3-dioxygenase from pyrazon-degrading bacteria

1977

Muller, R.; Haug, S.; Eberspächer, J.; Lingens, F.

Hoppe-Seyler's Z. Physiol. Chem.

358

797-805

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

439502

-

Protocatechuate 3,4-dioxygenase from Nocardia erythropolis

1984

Kurane, R.; Ara, K.; Nakamura, I.; Suzuki, T.; Fukuoka, S.

Agric. Biol. Chem.

48

2105-2111

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

439527

5506273

3,4-Dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase from Nocardia restrictus. I. Isolation of the enzyme and study of its physical and chemical properties

1970

Tai, H.H.; Sih, C.J.

J. Biol. Chem.

245

5062-5071

439561

2262792

Construction of hybrid xylE genes between the two duplicate homologous genes from TOL plasmid pWW53: comparison of the kinetic properties of the gene products

1990

Williams, P.A.; Assinder, S.J.; Shaw, L.E.

J. Gen. Microbiol.

136

1583-1589

439566

7259155

Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol

1981

Klecka, G.M.; Gibson, D.T.

Appl. Environ. Microbiol.

41

1159-1165

439568

2126328

Catechol 2,3-dioxygenases from Pseudomonas aeruginosa 2x

1990

Kataeva, I.A.; Golovleva, L.A.

Methods Enzymol.

188

115-121

439571

7096306

Immobilization of metapyrocatechase and its properties in comparison with the soluble enzyme

1982

Iwaki, M.; Nozaki, M.

J. Biochem.

91

1549-1553

439576

7928969

Substrate specificity of catechol 2,3-dioxygenase encoded by TOL plasmid pWW0 of Pseudomonas putida and its relationship to cell growth

1994

Cerdan, P.; Wasserfallen, A.; Rekik, M.; Timmis, K.N.; Harayama, S.

J. Bacteriol.

176

6074-6081

439577

-

Characteristics of catechol 2,3-dioxygenase produced by 4-chlorobenzoate-degrading Pseudomonas sp. S-47

1997

Kim, K.P.; Seo, D.I.; Min, K.H.; Ka, J.O.; Park, Y.K.; Kim, C.K.

J. Microbiol.

35

295-299

439578

9588193

Structure of catechol 2,3-dioxygenase gene from Alcaligenes eutrophus 335

1998

Kang, B.S.; Ha, J.Y.; Lim, J.C.; Lee, J.; Kim, C.K.; Min, K.R.; Kim, Y.

Biochem. Biophys. Res. Commun.

245

791-796

439581

9614705

Purification, characterization, and gene analysis of catechol 2,3-dioxygenase from the aniline-assimilating bacterium Pseudomonas species AW-2

1998

Murakami, S.; Nakanishi, Y.; Kodama, N.; Takenaka, S.; Shinke, R.; Aoki, K.

Biosci. Biotechnol. Biochem.

62

747-752

439584

10484174

Catechol 2,3-dioxygenase from the thermophilic, phenol-degrading Bacillus thermoleovorans strain A2 has unexpected low thermal stability

1999

Milo, R.E.; Duffner, F.M.; Muller, R.

Extremophiles

3

185-190

439588

7744021

Substrate specificity differences between two catechol 2,3-dioxygenases encoded by the TOL and NAH plasmids from Pseudomonas putida

1995

Cerdan, P.; Rekik, M.; Harayama, S.

Eur. J. Biochem.

229

113-118

439589

7629031

Overexpression of Pseudomonas putida catechol 2,3-dioxygenase with high specific activity by genetically engineered Escherichia coli

1995

Kobayashi, T.; Ishida, T.; Horiike, K.; Takahara, Y.; Numao, N.; Nakazawa, A.; Nakazawa, T.; Nozaki, M.

J. Biochem.

117

614-622

439591

8633871

Catechol 2,3-dioxygenases functional in oxygen-limited (hypoxic) environments

1996

Kukor, J.J.; Olsen, R.H.

Appl. Environ. Microbiol.

62

1728-1740

439593

11889489

Ferredoxin-mediated reactivation of the chlorocatechol 2,3-dioxygenase from Pseudomonas putida GJ31

2002

Tropel, D.; Meyer, C.; Armengaud, J.; Jouanneau, Y.

Arch. Microbiol.

177

345-351

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

440426

16657726

Isolation and characterization of polyphenol oxidase isozymes of clingstone peach

1971

Wong, T.C.; Luh, B.S.; Whitaker, J.R.

Plant Physiol.

48

19-23

440427

-

Properties of polyphenol oxidase from Alternaria tenuis

1979

Motoda, S.

J. Ferment. Technol.

57

79-85

440434

10995279

Purification and characterization of a polyphenol oxidase from the seeds of field bean (Dolichos lablab)

2000

Paul, B.; Gowda, L.R.

J. Agric. Food Chem.

48

3839-3846

440436

11117875

Characterization of polyphenol oxidase in coffee

2000

Mazzafera, P.; Robinson, S.P.

Phytochemistry

55

285-296

485543

-

Purification and properties of the three o-diphenol-O-methyltransferases of tobacco leaves

1981

Collendavelloo, J.; Legrand, M.; Geoffroy, P.; Barthelemy, J.; Fritig, B.

Phytochemistry

20

611-616

636336

-

Polyphenoloxidase from apple, partial purification and some properties

1989

Janovitz-Klapp, A.; Richard, F.; Nicholas, J.

Phytochemistry

28

2903-2907

636337

-

Identification of a tyrosinase from periphytic marine bacterium

1990

Kelley, S.K.; Coyne, V.E.; Sledjeski, D.D.; Fuqua, W.C.; Weiner, R.M.

FEMS Microbiol. Lett.

67

275-280

636338

2126551

N-acetyl-6-hydroxytryptophan oxidase, a developmentally controlled phenol oxidase from Aspergillus nidulans

1990

Birse, C.E.; Clutterbuck, A.J.

J. Gen. Microbiol.

136

1725-1730

636339

2494997

Isolation and characterization of variant cDNAs encoding mouse tyrosinase

1989

Terao, M.; Tabe, L.; Garattini, E.; Sartori, D.; Studer, M.; Mintz, B.

Biochem. Biophys. Res. Commun.

159

848-853

636340

2510599

Purification of tyrosinase to homogeneity based on its resistance to sodium dodecyl sulfate-proteinase K digestion

1989

Yurkow, E.J.; Laskin, J.D.

Arch. Biochem. Biophys.

275

122-129

636341

-

Properties of cuticular phenoloxidase from pupae of the housefly, Musca domestica L.

1991

Hara, T.; Tsukamoto, T.; Watanabe, K.; Yamasaki, N.; Funatsu, M.

Agric. Biol. Chem.

55

13-17

636342

-

Alterations to the catalytic properties of polyphenoloxidase in detergentless microemulsions and ternary water-organic solvent mixtures

1991

Vulfson, E.N.; Ahmed, G.; Gill, I.; Kozlov, I.A.; Goodenough, P.W.; Law, B.A.

Biotechnol. Lett.

13

91-96

636343

-

Isolation and characterization of an environmental acid-fast organism producing diphenoloxidase activity in vivo

1990

Harris, E.B.; Sanchez, R.M.; Job, C.K.; Prabhakaran, K.; Hastings, R.C.

FEMS Microbiol. Lett.

70

95-100

636344

-

The hydroxylation step in the biosynthetic pathway leading from norcolaurine to reticuline

1990

Loeffler, S.; Zenk, M.H.

Phytochemistry

29

3499-3503

636345

-

Comparison of phenoloxidase activities during the cultivation of several basidomycetes

1989

Tanabe, N.; Sagawa, I.; Ohtsubo, K.i.; Iijima, Y.; Yanagi, S.O.

Agric. Biol. Chem.

53

3061-3063

636346

-

Substrate specificity, de novo synthesis and partial purification of polyphenol oxidase derived from the wood-decay fungus, Coriolus versicolor

1989

Moore, N.L.; Mariam, D.H.; Williams, A.L.; Dashek, W.V.

J. Ind. Microbiol.

4

349-364

636347

-

Purification and properties of phenoloxidase from spinach leaves

1989

Oda, Y.; Kato, H.; Isoda, Y.; Takahashi, N.; Yamamoto, T.; Takada, Y.; Kudo, S.

Agric. Biol. Chem.

53

2053-2061

636348

2529259

Isolation and characterization of the tyrosinase gene from Neurospora crassa

1989

Kupper, U.; Niedermann, D.M.; Travaglini, G.; Lerch, K.

J. Biol. Chem.

264

17250-17258

636349

2753165

Characterization of a new enzyme system that desaturates the side chain of N-acetyldopamine

1989

Saul, S.J.; Sugumaran, M.

FEBS Lett.

251

69-73

636350

-

Purification of prophenol oxidase from Daucus carota cell cultures

1989

S¸derh§ll, I.; S¸derh§ll, K.

Phytochemistry

28

1805-1808

636351

18588108

Characteristics of tyrosinase in AOT-isooctane reverse micelles

1989

Bru, R.; Sanchez-Ferrer, A.; Garcia-Carmona, F.

Biotechnol. Bioeng.

34

304-308

636352

-

Triton X-114 as a tool for purifying spinach polyphenol oxidase

1989

Sanchez-Ferrer, A.; Villalba, J.; Garcia-Carmona, F.

Phytochemistry

28

1321-1325

636353

-

Purification and kinetic properties of phenoloxidase from pupae of the housefly

1989

Hara, T.; Tsukamoto, T.; Maruta, K.; Funatsu, M.

Agric. Biol. Chem.

53

1387-1393

636354

2504146

Purification of a unique glycoprotein that enhances phenol oxidase activity in scorpion (Heterometrus bengalensis) haemolymph

1989

Datta, T.K.; Basu, P.S.; Datta, P.K.; Banerjee, A.

Biochem. J.

260

525-529

636355

2492536

Specific identification of an authentic clone for mammalian tyrosinase

1989

Jimenez, M.; Maloy, W.L.; Hearing, V.J.

J. Biol. Chem.

264

3397-3403

636356

-

Partial purification and some properties of polyphenoloxidases from sago palm

1988

Okamoto, A.; Imagawa, H.; Arai, Y.; Ozawa, T.

Agric. Biol. Chem.

52

2215-2222

636357

3137937

Expression of tyrosinase gene in amelanotic mutant mice

1988

Takeuchi, S.; Yamamoto, H.; Takeuchi, T.

Biochem. Biophys. Res. Commun.

155

470-475

636358

-

Kinetic properties of polyphenoloxidase in organic solvents. A study in Brij 96-cyclohexane reverse micelles

1988

Sanchez-Ferrer, A.; Bru, R.; Garcia-Carmona, F.

FEBS Lett.

233

363-366

636359

-

Characterization of catecholase and cresolase activities of monastrell grape polyphenol oxidase

1988

Sanchez-Ferrer, A.; Bru, R.; Cabanes, J.; Garcia-Carmona, F.

Phytochemistry

27

319-321

636360

3110555

Mammalian monophenol monooxygenase (tyrosinase): purification, properties, and reactions catalyzed

1987

Hearing, V.J.

Methods Enzymol.

142

154-165

636368

16664316

Isolation and partial purification of prophenoloxidase from Daucus carota L. cell cultures

1985

S¸derh§ll, K.; Carlberg, I.; Eriksson, T.

Plant Physiol.

78

730-733

636380

-

Isolation and characterization of the polyphenoloxidase from senescent leaves of black poplar

1984

Tremolieres, M.; Bieth, J.G.

Phytochemistry

23

501-505

636381

-

Characterization of wheat o-diphenolase isoenzyme

1983

Interesse, F.S.; Ruggiero, P.; D'Avella, G.; Lamparelli, F.

Phytochemistry

22

1885-1889

636382

-

Mono- and diphenolase activity from fruit of Malus pumila

1983

Goodenough, P.W.; Kessell, S.; Lea, A.G.H.; Loeffler, T.

Phytochemistry

22

359-363

636393

-

Monophenolase activity of avocado polyphenol oxidase

1980

Kahn, V.; Pomerantz, S.H.

Phytochemistry

19

379-385

636399

-

Preparation and properties of an o-diphenol:O2 oxidoreductase from cocoa husk

1978

Chaplin, M.F.

Phytochemistry

17

1897-1899

636403

-

Catechol oxidase from green olives: properties and partial purification

1977

Ben-Shalom, N.; Kahn, V.; Harel, E.; Mayer, A.M.

Phytochemistry

16

1153-1158

636439

10691963

Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase

2000

Espin, J.C.; Varon, R.; Fenoll, L.G.; Gilabert, M.A.; Garcia-Ruiz, P.A.; Tudela, J.; Garcia-Canovas, F.

Eur. J. Biochem.

267

1270-1279

636442

10725136

Characterization of catecholase and cresolase activities of eggplant polyphenol oxidase

2000

Perez-Gilabert, M.; Garcia Carmona, F.

J. Agric. Food Chem.

48

695-700

636450

11453787

Properties of diphenolase from Vanilla planifolia (Andr.) shoot primordia cultured in vitro

2001

Debowska, R.; Podstolski, A.

J. Agric. Food Chem.

49

3432-3437

645671

10608851

X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity

1999

Dajani, R.; Cleasby, A.; Neu, M.; Wonacott, A.J.; Jhoti, H.; Hood, A.M.; Modi, S.; Hersey, A.; Taskinen, J.; Cooke, R.M.; Manchee, G.R.; Coughtrie, M.W.

J. Biol. Chem.

274

37862-37868

648899

8215795

Metabolism of 2-chloro-4-methylphenoxyacetate by Alcaligenes eutrophus JMP 134

1993

Pieper, D.H.; Stadler-Fritzsche, K.; Engesser, K.H.; Knackmuss, H.J.

Arch. Microbiol.

160

169-178

655362

-

Purification and characterization of laccase from wood-degrading fungus Trichophyton rubrum LKY-7

2002

Jung, H.; Xu, F.; Li, K.

Enzyme Microb. Technol.

30

161-168

655627

14568157

Purification and characterization of laccase from the rice blast fungus, Magnaporthe grisea

2003

Iyer, G.; Chattoo, B.B.

FEMS Microbiol. Lett.

227

121-126

656984

15746157

Tissue localization of cytokinin dehydrogenase in maize: possible involvement of quinone species generated from plant phenolics by other enzymatic systems in the catalytic reaction

2005

Galuszka, P.; Frebortova, J.; Luhova, L.; Bilyeu, K.D.; English, J.T.; Frebort, I.

Plant Cell Physiol.

46

716-728

657781

15607751

Functional characterization and molecular modeling of methylcatechol 2,3-dioxygenase from o-xylene-degrading Rhodococcus sp. strain DK17

2005

Kim, D.; Chae, J.C.; Jang, J.Y.; Zylstra, G.J.; Kim, Y.M.; Kang, B.S.; Kim, E.

Biochem. Biophys. Res. Commun.

326

880-886

658329

15168857

Functional identification of the gene locus (ncg1231) and characterization of catechol 1,2-dioxygenase in Corynebacterium glutamicum

2004

Shen, X.H.; Liu, Z.P.; Liu, S.J.

Biotechnol. Lett.

26

575-580

658517

12920175

Conjugation of catechols by recombinant human sulfotransferases, UDP-glucuronosyltransferases, and soluble catechol O-methyltransferase: structure-conjugation relationships and predictive models

2003

Taskinen, J.; Ethell, B.T.; Pihlavisto, P.; Hood, A.M.; Burchell, B.; Coughtrie, M.W.H.

Drug Metab. Dispos.

31

1187-1197

658787

-

Effect of glutathione and Maillard reaction products prepared from glucose or fructose with glutathione on polyphenoloxidase from apple-I: Enzymatic browning and enzyme activity inhibition

2003

Billaud, C.; Brun-Merimee, S.; Louarme, L.; Nicolas, J.

Food Chem.

84

223-233

658788

100478607

Purification of mulberry (Morus alba L.) polyphenol oxidase by affinity chromatography and investigation of its kinetic and electrophoretic properties

2004

Arslan, O.; Erzengin, M.; Sinan, S.; Ozensoy, O.

Food Chem.

88

479-484

658950

12670183

Consistency of polyphenol oxidase (PPO) thermostability in ripening apricots (Prunus armeniaca L.): evidence for the presence of thermostable PPO forming and destabilizing mechanisms in apricots

2003

Yemenicioglu, A.; Cemeroglu, B.

J. Agric. Food Chem.

51

2371-2379

658960

15686433

Characterization and purification of polyphenol oxidase from artichoke (Cynara scolymus L.)

2005

Dogan, S.; Turan, Y.; Erturk, H.; Arslan, O.

J. Agric. Food Chem.

53

776-785

659017

12270830

Differential expression of two catechol 1,2-dioxygenases in Burkholderia sp. strain TH2

2002

Suzuki, K.; Ichimura, A.; Ogawa, N.; Hasebe, A.; Miyashita, K.

J. Bacteriol.

184

5714-5722

659021

12700274

Substrate specificity and expression of three 2,3-dihydroxybiphenyl 1,2-dioxygenases from Rhodococcus globerulus strain P6

2003

McKay, D.B.; Prucha, M.; Reineke, W.; Timmis, K.N.; Pieper, D.H.

J. Bacteriol.

185

2944-2951

659212

12672826

Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8

2003

Hatta, T.; Mukerjee-Dhar, G.; Damborsky, J.; Kiyohara, H.; Kimbara, K.

J. Biol. Chem.

278

21483-21492

659414

15347689

The role of the conserved residues His-246, His-199, and Tyr-255 in the catalysis of catechol 2,3-dioxygenase from Pseudomonas stutzeri OX1

2004

Viggiani, A.; Siani, L.; Notomista, E.; Birolo, L.; Pucci, P.; Di Donato, A.

J. Biol. Chem.

279

48630-48639

659536

16233669

Constitutive synthesis, purification, and characterization of catechol 1,2-dioxygenase from the aniline-assimilating bacterium Rhodococcus sp. AN-22

2004

Matsumura, E.; Ooi, S.; Murakami, S.; Takenaka, S.; Aoki, K.

J. Biosci. Bioeng.

98

71-76

659827

15482430

A heat inducible tyrosinase with distinct properties from Bacillus thuringiensis

2004

Liu, N.; Zhang, T.; Wang, Y.J.; Huang, Y.P.; Ou, J.H.; Shen, P.

Lett. Appl. Microbiol.

39

407-412

659881

14600239

3- and 4-alkylphenol degradation pathway in Pseudomonas sp. strain KL28: genetic organization of the lap gene cluster and substrate specificities of phenol hydroxylase and catechol 2,3-dioxygenase

2003

Jeong, J.J.; Kim, J.H.; Kim, C.K.; Hwang, I.; Lee, K.

Microbiology

149

3265-3277

659889

15583170

Difference in kinetic behaviour of catechol 2,3-dioxygenase variants from a polluted environment

2004

Junca, H.; Plumeier, I.; Hecht, H.J.; Pieper, D.H.

Microbiology

150

4181-4187

671391

17013550

Production, purification and partial characterisation of a novel laccase from the white-rot fungus Panus tigrinus CBS 577.79

2007

Quaratino, D.; Federici, F.; Petruccioli, M.; Fenice, M.; D'Annibale, A.

Antonie van Leeuwenhoek

91

57-69

671593

16406214

Isolation of a latent polyphenol oxidase from loquat fruit (Eriobotrya japonica Lindl.): kinetic characterization and comparison with the active form

2006

Selles-Marchart, S.; Casado-Vela, J.; Bru-Martinez, R.

Arch. Biochem. Biophys.

446

175-185

671650

17089147

Purification and characterization of a catechol 1,2-dioxygenase from a phenol degrading Candida albicans TL3

2007

Tsai, S.C.; Li, Y.K.

Arch. Microbiol.

187

199-206

673779

100487971

Purification and characterization of polyphenol oxidase from Ferula sp.

2006

Erat, M.; Sakiroglu, H.; Kufrevioglu, O.I.

Food Chem.

95

503-508

674089

16366719

Purification and characterization of Ocimum basilicum L. polyphenol oxidase

2005

Dog An, S.; Turan, P.; Dog An, M.; Arslan, O.; Alkan, M.

J. Agric. Food Chem.

53

10224-10230

674090

15713040

A kinetic study of p-cresol oxidation by quince fruit polyphenol oxidase

2005

Orenes-Pinero, E.; Garcia-Carmona, F.; Sanchez-Ferrer, A.

J. Agric. Food Chem.

53

1196-1200

674092

15769132

Characterization of a tomato polyphenol oxidase and its role in browning and lycopene content

2005

Spagna, G.; Barbagallo, R.N.; Chisari, M.; Branca, F.

J. Agric. Food Chem.

53

2032-2038

674108

16104806

Differential activation of a latent polyphenol oxidase mediated by sodium dodecyl sulfate

2005

Gandia-Herrero, F.; Nez-Atieanzar, M.J.; Cabanes, J.; Garcia-Carmona, F.; Escribano, J.

J. Agric. Food Chem.

53

6825-6830

674142

17263494

Kinetic characterization of the oxidation of chlorogenic acid by polyphenol oxidase and peroxidase. Characteristics of the o-quinone

2007

Munoz, J.; Garcia-Molina, F.; Varon, R.; Rodriguez-Lopez, J.N.; Garcia-Ruiz, P.A.; Garcia-Casanovas, F.; Tudela, J.

J. Agric. Food Chem.

55

920-928

674226

15715866

The bphC gene-encoded 2,3-dihydroxybiphenyl-1,2-dioxygenase is involved in complete degradation of dibenzofuran by the biphenyl-degrading bacterium Ralstonia sp. SBUG 290

2005

Wesche, J.; Hammer, E.; Becher, D.; Burchhardt, G.; Schauer, F.

J. Appl. Microbiol.

98

635-645

675101

16119202

Purification and characterization of polyphenol oxidase from nettle (Urtica dioica L.) and inhibitory effects of some chemicals on enzyme activity

2005

Guelcin, I.; Kuefrevioglu, O.I.; Oktay, M.

J. Enzyme Inhib. Med. Chem.

20

297-302

675167

100116480

Polyphenol oxidase from apple (Malus domestica Borkh. cv Bramley’s seedling): purification strategies and characterization

2006

Ni Eidhinn, D.M.; Murphy, E.; O'Beirne, D.

J. Food Sci.

71

C51-C58

675335

-

Catechol 1,2-dioxygenase from Rhodococcus rhodochrous N75 capable of metabolizing alkyl-substituted catechols

2006

Cha, C.

J. Microbiol. Biotechnol.

16

778-785

675458

-

Kinetic study of monophenol and o-diphenol binding to oxytyrosinase

2005

Garcia-Molina, F.; Penalver, M.J.; Fenoll, L.G.; Rodriguez-Lopez, J.N.; Varon, R.; Gracia-Canovas, F.; Tudela, J.

J. Mol. Catal. B

32

185-192

676381

16376392

Polyphenoloxidase activity in coffee leaves and its role in resistance against the coffee leaf miner and coffee leaf rust

2006

Aclecio Melo, G.; Massao Shimizu, M.; Mazzafera, P.

Phytochemistry

67

277-285

676649

16814556

Extraction and partial characterization of polyphenol oxidase from banana (Musa acuminata Grande naine) roots

2006

Wuyts, N.; De Waele, D.; Swennen, R.

Plant Physiol. Biochem.

44

308-314

676763

-

Purification and characterization of a novel catechol 1,2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source

2006

Wang, C.; You, S.; Wang, S.

Proc. Biochem.

41

1594-1601

677966

17451650

Comparative analysis of the catechol 2,3-dioxygenase gene locus in thermoacidophilic archaeon Sulfolobus solfataricus strain 98/2

2007

Chae, J.C.; Kim, E.; Bini, E.; Zylstra, G.J.

Biochem. Biophys. Res. Commun.

357

815-819

680435

9973359

Conversion of 3-chlorocatechol by various catechol 2,3-dioxygenases and sequence analysis of the chlorocatechol dioxygenase region of Pseudomonas putida GJ31

1999

Mars, A.E.; Kingma, J.; Kaschabek, S.R.; Reineke, W.; Janssen, D.B.

J. Bacteriol.

181

1309-1318

680483

17172348

A gene cluster involved in degradation of substituted salicylates via ortho cleavage in Pseudomonas sp. strain MT1 encodes enzymes specifically adapted for transformation of 4-methylcatechol and 3-methylmuconate

2007

Camara, B.; Bielecki, P.; Kaminski, F.; dos Santos, V.M.; Plumeier, I.; Nikodem, P.; Pieper, D.H.

J. Bacteriol.

189

1664-1674

684232

-

Polyphenol oxidase activity in dormant saffron (Crocus sativus L.) corm

2007

Saiedian, S.; Keyhani, E.; Keyhani, J.

Acta Physiol. Plant.

29

463-471

685018

18647136

Phenolic substrates and suicide inactivation of tyrosinase: kinetics and mechanism

2008

Munoz-Munoz, J.L.; Garcia-Molina, F.; Garcia-Ruiz, P.A.; Molina-Alarcon, M.; Tudela, J.; Garcia-Canovas, F.; Rodriguez-Lopez, J.N.

Biochem. J.

416

431-440

685422

18585431

Purification, characterization, and substrate specificity of two 2,3-dihydroxybiphenyl 1,2-dioxygenase from Rhodococcus sp. R04, showing their distinct stability at various temperature

2008

Yang, X.; Xie, F.; Zhang, G.; Shi, Y.; Qian, S.

Biochimie

90

1530-1538

685660

17617714

Purification and characterization of catechol 2,3-dioxygenase from the aniline degradation pathway of Acinetobacter sp. YAA and its mutant enzyme, which resists substrate inhibition

2007

Takeo, M.; Nishimura, M.; Shirai, M.; Takahashi, H.; Negoro, S.

Biosci. Biotechnol. Biochem.

71

1668-1675

685753

17823775

Tyrosinase activity in ionic liquids

2008

Yang, Z.; Yue, Y.J.; Xing, M.

Biotechnol. Lett.

30

153-158

686484

-

Partial characterization of lettuce (Lactuca sativa L.) polyphenol oxidase

2007

Dogan, S.; Salman, U.

Eur. Food Res. Technol.

226

93-103

686666

17651437

Functional interaction of diphenols with polyphenol oxidase. Molecular determinants of substrate/inhibitor specificity

2007

Kanade, S.R.; Suhas, V.L.; Chandra, N.; Gowda, L.R.

FEBS J.

274

4177-4187

686841

100505855

Characterization of polyphenol oxidase from broccoli (Brassica oleracea var. botrytis italica) florets

2007

Gawlik-Dziki, U.; Szymanowska, U.; Baraniak, B.

Food Chem.

105

1047-1053

686844

-

Characterization of polyphenoloxidase (PPO) and total phenolic contents in medlar (Mespilus germanica L.) fruit during ripening and over ripening

2007

Ayaz, F.A.; Demir, O.; Torun, H.; Kolcuoglu, Y.; Colak, A.

Food Chem.

106

291-298

686845

-

Characterization of polyphenol oxidase from butter lettuce (Lactuca sativa var. capitata L.)

2007

Gawlik-Dziki, U.; Zlotek, U.; Swieca, M.

Food Chem.

107

129-135

686847

26049223

Purification and kinetic characterization of polyphenol oxidase from Barbados cherry (Malpighia glabra L.)

2008

Kumar, V.B.; Mohan, T.C.; Murugan, K.

Food Chem.

110

328-333

687231

17407318

Effect of ionic detergents, nonionic detergents, and chaotropic agents on polyphenol oxidase activity from dormant saffron (Crocus sativus L.) corms

2007

Saeidian, S.; Keyhani, E.; Keyhani, J.

J. Agric. Food Chem.

55

3713-3719

687240

17628073

Characterization of polyphenol oxidase from the Manzanilla cultivar (Olea europaea pomiformis) and prevention of browning reactions in bruised olive fruits

2007

Segovia-Bravo, K.A.; Jaren-Galan, M.; Garcia-Garcia, P.; Garrido-Fernandez, A.

J. Agric. Food Chem.

55

6515-6520

687251

18361497

Latent and active polyphenol oxidase (PPO) in red clover (Trifolium pratense) and use of a low PPO mutant to study the role of PPO in proteolysis reduction

2008

Winters, A.L.; Minchin, F.R.; Michaelson-Yeates, T.P.; Lee, M.R.; Morris, P.

J. Agric. Food Chem.

56

2817-2824

687854

18023805

Purification and characterization of alkylcatechol 2,3-dioxygenase from butylphenol degradation pathway of Pseudomonas putida MT4

2007

Takeo, M.; Nishimura, M.; Takahashi, H.; Kitamura, C.; Kato, D.; Negoro, S.

J. Biosci. Bioeng.

104

309-314

695687

18649146

Purification and characterization of cell suspensions peroxidase from cotton (Gossypium hirsutum L.)

2008

Kouakou, T.H.; Due, E.A.; Kouadio, N.E.; Niamke, S.; Kouadio, Y.J.; Merillon, J.M.

Appl. Biochem. Biotechnol.

157

575-592

697245

-

Catechol 1,2-dioxygenase from alpha-naphthol degrading thermophilic Geobacillus sp. strain: Purification and properties

2009

Giedraityte, G.; Kalediene, L.

Cent. Eur. J. Biol.

4

68-73

697316

19301316

Fine-tuning of catalytic properties of catechol 1,2-dioxygenase by active site tailoring

2009

Caglio, R.; Valetti, F.; Caposio, P.; Gribaudo, G.; Pessione, E.; Giunta, C.

ChemBioChem

10

1015-1024

697533

19672496

Catalytic properties of catechol 1,2-dioxygenase from Acinetobacter radioresistens S13 immobilized on nanosponges

2009

Di Nardo, G.; Roggero, C.; Campolongo, S.; Valetti, F.; Trotta, F.; Gilardi, G.

Dalton Trans.

33

6507-6512

697664

-

Fermentation optimization and characterization of the laccase from Pleurotus ostreatus strain 10969

2009

Liu, L.; Lin, Z.; Zheng, T.; Lin, L.; Zheng, C.; Lin, Z.; Wang, S.; Wang, Z.

Enzyme Microb. Technol.

44

426-433

698436

19572544

In vitro study of red clover polyphenol oxidase activity, activation, and effect on measured lipase activity and lipolysis

2009

Van Ranst, G.; Fievez, V.; Vandewalle, M.; De Riek, J.; Van Bockstaele, E.

J. Agric. Food Chem.

57

6611-6617

698537

7204331

Naphthalene metabolism by pseudomonads: purification and properties of 1,2-dihydroxynaphthalene oxygenase

1980

Patel, T.R.; Barnsley, E.A.

J. Bacteriol.

143

668-673

698539

2050635

Purification and characterization of a 1,2-dihydroxynaphthalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids

1991

Kuhm, A.E.; Stolz, A.; Ngai, K.L.; Knackmuss, H.J.

J. Bacteriol.

173

3795-3802

699242

18830916

Differential in vitro inhibition of polyphenoloxidase from a wild edible mushroom Lactarius salmonicolor

2009

Dedeoglu, N.; Guler, O.O.

J. Enzyme Inhib. Med. Chem.

24

464-470

700667

18929376

Extraction, structural characterisation and evaluation of hydroxycinnamate esters of orchard grass (Dactylis glomerata) as substrates for polyphenol oxidase

2008

Parveen, I.; Winters, A.; Threadgill, M.D.; Hauck, B.; Morris, P.

Phytochemistry

69

2799-2806

701760

18795241

Purification and biochemical characterization of polyphenol oxidases from embryogenic and nonembryogenic cotton (Gossypium hirsutum L.) cells

2009

Kouakou, T.H.; Kouadio, Y.J.; Kouame, P.; Waffo-Teguo, P.; Decendit, A.; Merillon, J.M.

Appl. Biochem. Biotechnol.

158

285-301

702714

19097884

Characterization of catechol derivative removal by lignin peroxidase in aqueous mixture

2009

Cohen, S.; Belinky, P.A.; Hadar, Y.; Dosoretz, C.G.

Biores. Technol.

100

2247-2253

703749

19187202

Enzyme-substrate interaction and characterization of a 2,3-dihydroxybiphenyl 1,2-dioxygenase from Dyella ginsengisoli LA-4

2009

Li, A.; Qu, Y.; Zhou, J.; Ma, F.

FEMS Microbiol. Lett.

292

231-239

706120

18675435

A wounding-induced PPO from cowpea (Vigna unguiculata) seedlings

2008

Pinto, M.S.; Siqueira, F.P.; Oliveira, A.E.; Fernandes, K.V.

Phytochemistry

69

2297-2302

711314

20869471

X-ray crystallography, mass spectrometry and single crystal microspectrophotometry: A multidisciplinary characterization of catechol 1,2 dioxygenase

2011

Micalella, C.; Martignon, S.; Bruno, S.; Pioselli, B.; Caglio, R.; Valetti, F.; Pessione, E.; Giunta, C.; Rizzi, M.

Biochim. Biophys. Acta

1814

817-823

711787

20462518

Detection and characterization of phenoloxidase in the freshwater planarian Dugesia japonica

2010

Pang, Q.; Liu, X.; Zhao, B.; Jiang, Y.; Su, F.; Zhang, X.; Nie, M.; Zhang, M.; Sun, H.

Comp. Biochem. Physiol. B

157

54-58

712053

100525555

Purification and characterisation of a polyphenol oxidase from Boletus erythropus and investigation of its catalytic efficiency in selected organic solvents

2010

Oezel, A.; Colak, A.; Arslan, O.; Yildirim, M.

Food Chem.

119

1044-1049

712219

20073467

Polyphenol oxidase activity from three sicilian artichoke [Cynara cardunculus L. var. scolymus L. (Fiori)] cultivars: studies and technological application on minimally processed production

2010

Todaro, A.; Peluso, O.; Catalano, A.E.; Mauromicale, G.; Spagna, G.

J. Agric. Food Chem.

58

1714-1718

712619

100067033

Characterization of polyphenol oxidase from rooster potato (Solanum tuberosum cv Rooster)

2010

Ni Eidhin, D.; Degn, P.; Obeirne, D.

J. Food Biochem.

34

13-30

712893

20040374

Catechol 1,2-dioxygenase from the Gram-positive Rhodococcus opacus 1CP: Quantitative structure/activity relationship and the crystal structures of native enzyme and catechols adducts

2010

Matera, I.; Ferraroni, M.; Kolomytseva, M.; Golovleva, L.; Scozzafava, A.; Briganti, F.

J. Struct. Biol.

170

548-564

713239

21087780

Purification and partial biochemical characterization of polyphenol oxidase from mamey (Pouteria sapota)

2011

Palma-Orozco, G.; Ortiz-Moreno, A.; Dorantes-Alvarez, L.; Sampedro, J.G.; Najera, H.

Phytochemistry

72

82-88

713302

21530289

Enzyme characterisation, isolation and cDNA cloning of polyphenol oxidase in the hearts of palm of three commercially important species

2011

Shimizu, M.M.; Melo, G.A.; Brombini Dos Santos, A.; Bottcher, A.; Cesarino, I.; Araujo, P.; Magalhaes Silva Moura, J.C.; Mazzafera, P.

Plant Physiol. Biochem.

49

970-977

713387

21442554

Purification and biochemical characterization of ionically unbound polyphenol oxidase from Musa paradisiaca leaf

2011

Diwakar, S.K.; Mishra, S.K.

Prep. Biochem. Biotechnol.

41

187-200

719711

17720792

Cloning of a gene cluster involved in the catabolism of p-nitrophenol by Arthrobacter sp. strain JS443 and characterization of the p-nitrophenol monooxygenase

2007

Perry, L.; Zylstra, G.

J. Bacteriol.

189

7563-7572

722493

8892823

2-Aminophenol 1,6-dioxygenase: a novel aromatic ring cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45

1996

Lendenmann, U.; Spain, J.C.

J. Bacteriol.

178

6227-6232

722603

9169437

Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme

1997

Takenaka, S.; Murakami, S.; Shinke, R.; Hatakeyama, K.; Yukawa, H.; Aoki, K.

J. Biol. Chem.

272

14727-14732

723819

22826823

Characterization of catechol 2,3-dioxygenase from Planococcus sp. strain S5 induced by high phenol concentration

2012

Hupert-Kocurek, K.; Guzik, U.; Wojcieszynska, D.

Acta Biochim. Pol.

59

345-351

723960

23536173

High activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production

2013

Guzik, U.; Hupert-Kocurek, K.; Sitnik, M.; Wojcieszynska, D.

Antonie van Leeuwenhoek

103

1297-1307

724201

-

Properties of catechol 2,3-dioxygenase from crude extract of Stenotrophomonas maltophilia strain KB2 immobilized in calcium alginate hydrogels

2012

Wojcieszynska, D.; Hupert-Kocurek, K.; Jankowska, A.; Guzik, U.

Biochem. Eng. J.

66

1-7

724567

21924604

Optimization of 2,3-dihydroxybiphenyl 1,2-dioxygenase expression and its application for biosensor

2011

Zhang, Q.; Qu, Y.; Zhou, J.; Zhang, X.; Zhou, H.; Ma, Q.; Li, X.

Biores. Technol.

102

10553-10560

724662

21266052

Bacillus pumilus laccase: a heat stable enzyme with a wide substrate spectrum

2011

Reiss, R.; Ihssen, J.; Thoeny-Meyer, L.

BMC Biotechnol.

11

9-9

725631

23948567

Cloning of three 2,3-dihydroxybiphenyl-1,2-dioxygenase genes from Achromobacter sp. BP3 and the analysis of their roles in the biodegradation of biphenyl

2013

Cao, L.; Gao, Y.; Wu, G.; Li, M.; Xu, J.; He, J.; Li, S.; Hong, Q.

J. Hazard. Mater.

261

246-252

725647

22687491

Screening chelating inhibitors of HIF-prolyl hydroxylase domain 2 (PHD2) and factor inhibiting HIF (FIH)

2012

Flagg, S.C.; Martin, C.B.; Taabazuing, C.Y.; Holmes, B.E.; Knapp, M.J.

J. Inorg. Biochem.

113

25-30

725655

-

Purification and characterization of protocatechuate 3,4-dioxygenase from Pseudomonas pseudoalcaligenes KF707

2013

Sim, H.; Jung, M.; Cho, Y.

J. Korean Soc. Appl. Biol. Chem.

56

401-408

726187

22814940

Site-directed mutagenesis of a tetrameric dandelion polyphenol oxidase (PPO-6) reveals the site of subunit interaction

2012

Dirks-Hofmeister, M.E.; Inlow, J.K.; Moerschbacher, B.M.

Plant Mol. Biol.

80

203-217

726474

15921893

The thermophilic archaeon Sulfolobus solfataricus is able to grow on phenol

2005

Izzo, V.; Notomista, E.; Picardi, A.; Pennacchio, F.; di Donato, A.

Res. Microbiol.

156

677-689

727645

23770035

Expression pattern and substrate specificity of Clonorchis sinensis tyrosinases

2013

Bae, Y.A.; Cai, G.B.; Kim, S.H.; Sohn, W.M.; Kong, Y.

Int. J. Parasitol.

43

891-900

728714

-

Purification and comparative characterization of monophenolase and diphenolase activities from a wild edible mushroom (Macrolepiota gracilenta)

2012

Kolcuoglu, Y.

Process Biochem.

47

2449-2454

741500

25337606

Altering substrate specificity of catechol 2,3-dioxygenase from Planococcus sp. strain S5 by random mutagenesis

2014

Hupert-Kocurek, K.; Wojcieszynska, D.; Guzik, U.

Acta Biochim. Pol.

61

705-710

742574

-

Multistep conversion of cresols by phenol hydroxylase and 2,3-dihydroxy-biphenyl 1,2-dioxygenase

2014

Shi, S.; Ma, F.; Sun, T.; Li, A.; Zhou, J.; Qu, Y.

Front. Environ. Sci. Eng.

8

539-546

742691

27765568

Biochemical characterization of an extremely stable pH-versatile laccase from Sporothrix carnis CPF-05

2017

Olajuyigbe, F.M.; Fatokun, C.O.

Int. J. Biol. Macromol.

94

535-543

743104

-

A single amino acid substitution within catalytically non-active N-terminal domain of catechol 2,3-dioxygenase (C23O) increases enzyme activity towards 4-chlorocatechol

2015

Hupert-Kocurek, K.; Wojcieszylska, D.; Guzik, U.; Borowski, T.

J. Mol. Catal. B

122

64-71

743243

-

Catechol 1,2-dioxygenase induced in Rhodococcus opacus strain 1CP cultured in the presence of 3-hydroxybenzoate

2016

Subbotina, N.; Kolomytseva, M.; Baskunov, B.; Golovlev, L.

Microbiology (Russian Federation)

85

638-641

743749

26563518

Purification and characterization of catechol 1,2-dioxygenase from Acinetobacter sp. Y64 strain and Escherichia coli transformants

2015

Lin, J.; Milase, R.N.

Protein J.

34

421-433

743800

26621792

Isolation and characterization of two novel halotolerant catechol 2,3-dioxygenases from a halophilic bacterial consortium

2015

Guo, G.; Fang, T.; Wang, C.; Huang, Y.; Tian, F.; Cui, Q.; Wang, H.

Sci. Rep.

5

17603

743838

24693238

Activity of a carboxyl-terminal truncated form of catechol 2,3-dioxygenase from Planococcus sp. S5

2014

Hupert-Kocurek, K.; Wojcieszylska, D.; Guzik, U.

Sci. World J.

2014

598518

744661

28040055

Purification and characterization of polyphenol oxidase from corn tassel

2016

Gul Guven, R.; Aslan, N.; Guven, K.; Matpan Bekler, F.; Acer, O.

Cell. Mol. Biol.

62

6-11

744824

-

Effect of harvest year on biochemical properties of Narince grape (Vitis vinifera l. cv. Narince) polyphenol oxidase

2014

Uemit Uenal, M.; Sener, A.

Eur. Food Res. Technol.

238

613-619

744954

25863612

Purification and structural analysis of membrane-bound polyphenol oxidase from Fuji apple

2015

Liu, F.; Zhao, J.H.; Wen, X.; Ni, Y.Y.

Food Chem.

183

72-77

744955

26616939

Characterization of polyphenol oxidase from Cape gooseberry (Physalis peruviana L.) fruit

2016

Bravo, K.; Osorio, E.

Food Chem.

197

185-190

745136

25211397

Purification and partial biochemical characterization of polyphenol oxidase from mango (Mangifera indica cv. Manila)

2014

Palma-Orozco, G.; Marrufo-Hernandez, N.A.; Sampedro, J.G.; Najera, H.

J. Agric. Food Chem.

62

9832-9840

745557

-

Extraction, partial purification and characterization of polyphenol oxidase from Solanum lycocarpum fruits

2014

Batista, K.; Batista, G.; Alves, G.; Fernandes, K.

J. Mol. Catal. B

102

211-217

745746

25189462

Human tyrosinase produced in insect cells a landmark for the screening of new drugs addressing its activity

2015

Fogal, S.; Carotti, M.; Giaretta, L.; Lanciai, F.; Nogara, L.; Bubacco, L.; Bergantino, E.

Mol. Biotechnol.

57

45-57

746276

-

Polyphenoloxidase activity and browning in fresh-cut Rocha pear as affected by pH, phenolic substrates, and antibrowning additives

2014

Gomes, M.; Vieira, T.; Fundo, J.; Almeida, D.

Postharvest Biol. Technol.

91

32-38

746341

-

Characterization, purification, and temperature/pressure stability of polyphenol oxidase extracted from plums (Prunus domestica)

2017

Ionita, E.; Gurgu, L.; Aprodu, I.; Stanciuc, N.; Dalmadi, I.; Bahrim, G.; Rapeanu, G.

Process Biochem.

56

177-185