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Ligand 3-methylcatechol

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 3-methylcatechol

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Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.243

2-methylphenol + NADH + H+ + O2 = 3-methylcatechol + NAD+ + H2O

0

-

Substrate in Enzyme-catalyzed Reactions (32 results)

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Show Substrate (32 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.1

2 3-methylcatechol + O2 = 2 3-methyl-1,2-benzoquinone + 2 H2O

744952

-

1.10.3.2

4-hydroxy-1,6-dimethylpyridin-2(1H)-one + 3-methyl-1,2-benzenediol = 7,8-dihydroxy-2,3,6-trimethyl[1]benzofuro[3,2-c]pyridin-1(2H)-one

699726

-

1.10.3.2

4-hydroxy-1-thiocoumarin + 3-methyl-1,2-benzenediol = 8,9-dihydroxy-10-methyl-6H-thiochromeno[4,3-b][1]benzofuran-6-one

699726

-

1.10.3.2

4-hydroxy-6-methylpyridin-2(1H)-one + 3-methyl-1,2-benzenediol = 7,8-dihydroxy-3,6-dimethyl[1]benzofuro[3,2-c]pyridin-1(2H)-one

699726

-

1.10.3.2

4-hydroxyquinolin-2(1H)-one + 3-methyl-1,2-benzenediol = 8,9-dihydroxy-10-methyl[1]benzofuro[3,2-c]quinolin-6(5H)-one

699726

-

1.10.3.2

3-methylcatechol + O2 = ?

396380

-

1.10.3.2

5 entries

1.11.1.19

3-methylcatechol + H2O2 + H+ = ?

765206

-

1.13.11.1

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

395005, 394983, 395006, 395002, 394998, 394989, 395001, 395008, 395003, 395009, 680483, 394995, 394996, 394987, 394990, 712893, 711314, 763927

3hjq, 3D-view

1.13.11.1

3-methylcatechol + O2 = 2-methyl-cis,cis-muconate

658329, 659536, 676763, 675335, 723960

3hjq, 3D-view

1.13.11.1

3-methylcatechol + O2 = ?

743243, 697533, 743749, 697245, 697316

3hjq, 3D-view

1.13.11.1

3-methylpyrocatechol + O2 = 2,3,5-trimethyl-cis-cis-muconate

395007

3hjq, 3D-view

1.13.11.1

4 entries

1.13.11.16

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

395596, 395595

-

1.13.11.2

3-methylcatechol + O2 = 2-hydroxy-3-methoxymuconate semialdehyde

763927

-

1.13.11.2

3-methylcatechol + O2 = 2-hydroxy-3-methylmuconate semialdehyde

659889, 659881, 657781, 685660, 677966

-

1.13.11.2

3-methylcatechol + O2 = 2-hydroxy-3-methylmuconate-6-semialdehyde

764859

-

1.13.11.2

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

439561, 439584, 439588, 439591, 396602, 439577, 439581, 439566, 439571, 439576, 439589, 439578, 7066, 741500, 743199, 765713, 439568, 680435, 677966, 743104, 743838, 743800, 765789, 765013, 765182

-

1.13.11.2

3-methylcatechol + O2 = 2-hydroxy-6-oxohepta-2,4-dienoic acid

673546

-

1.13.11.2

3-methylcatechol + O2 = ?

724201, 723819, 726474, 687854

-

1.13.11.2

3-methylcatechol + O2 = cis,cis-2-hydroxy-6-oxohepta-2,4-dienoate

4835

-

1.13.11.2

7 entries

1.13.11.25

3-methylcatechol = ?

439527

-

1.13.11.3

3-methylcatechol + O2 = 2-methylmuconate

439505, 439483, 439502, 439501

-

1.13.11.36

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

439432

-

1.13.11.37

3-methylcatechol + O2 = ?

742664

-

1.13.11.39

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

439410, 439412, 439413, 439415, 439402, 439420, 439407, 439409, 439416, 439417, 674226, 742574, 685422, 743118, 703749, 742643

1knf, 3D-view

1.13.11.39

3-methylcatechol + O2 = ?

725631, 659689, 659021, 659212, 724567, 724640

1knf, 3D-view

1.13.11.56

3-methylcatechol + O2 = 2-hydroxy-6-oxohepta-2,4-dienoic acid

698537

-

1.13.11.56

3-methylcatechol + O2 = ?

698539

-

1.13.11.39

2 entries

1.13.11.56

2 entries

1.14.12.11

3-methylbenzene-1,2-diol + NADH + H+ + O2 = (4R,5S)-4,5-dihydroxy-3-methylcyclohex-2-en-1-one + NAD+

713169

-

1.14.18.1

3-methylcatechol + O2 = 3-methyl-o-benzoquinone + H2O

636399

-

1.14.99.54

regenerated amorphous cellulose + 3-methylcatechol + O2 = 3-methyl-o-benzoquinone + H2O

744131

-

1.14.99.54

regenerated amorphous cellulose + 3-methylcatechol + O2 = ? + 3-methyl-o-benzoquinone + H2O

744131

-

1.14.99.54

2 entries

3.7.1.8

3-methylcatechol + H2O = ?

247041

-

Product in Enzyme-catalyzed Reactions (27 results)

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Show Product (27 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.12.12

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

0

-

1.14.12.12

o-cresol + NADH + O2 = methylhydroquinone + 3-methylcatechol + NAD+

0

-

1.14.12.23

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

0

-

1.14.12.23

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

0

-

1.14.12.23

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

0

-

1.14.13.1

3-methylsalicylate + NADH + O2 = 1,2-dihydroxy-3-methylbenzene + CO2 + NAD+ + H2O

0

-

1.14.13.1

3-methylsalicylate + NADH + O2 = 1,2-dihydroxy-3-methylbenzene + NAD+ + H2O + CO2

0

-

1.14.13.1

3-methylsalicylate + NADH + H+ + O2 = 3-methylbenzene-1,2-diol + NAD+ + H2O + CO2

0

-

1.14.13.1

3-methylsalicylate + NADH + 2 H+ + O2 = 3-methylcatechol + NAD+ + H2O + CO2

0

-

1.14.13.1

3-methylsalicylate + NADH + H+ + O2 = 3-methylcatechol + NAD+ + H2O + CO2

0

-

1.14.12.12

2 entries

1.14.12.23

3 entries

1.14.13.1

5 entries

1.14.13.236

o-cresol + NADH + H+ + O2 = 3-methylcatechol + NAD+ + H2O

0

-

1.14.13.243

2-methylphenol + NADH + H+ + O2 = 3-methylcatechol + NAD+ + H2O

0

-

1.14.13.31

3-methyl-2-nitrophenol + NADPH + O2 = 3-methylcatechol + NADP+ + H2O

0

-

1.14.13.44

2-methylphenol + NADH + O2 = 1,2-dihydroxy-3-methylbenzene + NAD+ + H2O

0

-

1.14.13.6

3-cresol + NADH + O2 = 3-methylcatechol + NAD+ + H2O

0, 438808, 438806

-

1.14.13.7

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

0

-

1.14.13.7

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

0

-

1.14.13.7

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

0

-

1.14.13.7

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

0

-

1.14.13.7

o-cresol + NADH + H+ + O2 = 3-methylcatechol + NAD+ + H2O

0

-

1.14.13.7

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

0

-

1.3.1.119

3-methylbenzene cis-dihydrodiol + NAD+ = 3-methylcatechol + NADH + H+

0

-

1.3.1.119

cis-toluene dihydrodiol + NAD+ = 3-methylcatechol + NADH + H+

0

-

1.3.1.25

3-methyl-4,5-cyclohexadiene-cis-1,2-diol-1-carboxylic acid + NAD+ = 3-methylcatechol + CO2 + NADH

644712

-

1.3.1.25

3-methyldihydrodihydroxybenzoate + NAD+ = 3-methylcatechol + CO2 + NADH

0

-

1.14.13.7

6 entries

1.3.1.119

2 entries

1.3.1.25

2 entries

1.3.1.29

cis-toluene dihydrodiol + NAD+ = 3-methyl-1,2-dihydroxybenzene + NADH

390642, 390643, 390641

-

1.3.1.68

1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate + NAD+ = 3-methylcatechol + NADH + CO2

0

-

Inhibitor in Enzyme-catalyzed Reactions (8 results)

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Show Inhibitors (8 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.1

-

394983, 394987

3hjq, 3D-view

1.13.11.1

at concentration at 20 microM and above

395002

3hjq, 3D-view

1.13.11.1

2 entries

1.13.11.2

suicide inhibition

439588

-

1.13.11.39

-

439411

1knf, 3D-view

1.13.11.56

0.0005 mM, 76% inhibition, competitive inhibitor

698537

-

1.13.11.74

complete inhibition at 0.05 mM

722493

-

1.13.11.74

noncompetitive inhibition

722603

-

1.13.11.74

2 entries

4.1.1.55

weak

4714

-

3D Structure of Enzyme-Ligand-Complex (PDB) (2 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (2 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.13.11.1

3hjq, 3D-view

1.13.11.39

1knf, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (33 results)

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Show Turnover Number (33 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.13.11.1

0.4

-

-

395008

1.13.11.1

0.52

-

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

711314

1.13.11.1

0.8

-

pH not specified in the publication, 25°C

680483

1.13.11.1

1.1

-

-

676763

1.13.11.1

1.59

-

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

711314

1.13.11.1

2.3

-

pH not specified in the publication, 25°C

680483

1.13.11.1

9.5

-

-

395005

1.13.11.1

10.62

-

in 50 mM Tris/HCl, pH 7.2, 25°C

712893

1.13.11.1

8 entries

1.13.11.16

3.6

-

-

395595

1.13.11.2

0.2

-

pH 7.4, 32.5°C

765789

1.13.11.2

0.58

-

pH 7.5,25 °C

726474

1.13.11.2

2.6

-

mutant T249G

673546

1.13.11.2

5.2

-

pH 7.5, 60°C

726474

1.13.11.2

6.3

-

mutant T249A

673546

1.13.11.2

17

-

strain 1YB2, pH 7.5, 25°C

659889

1.13.11.2

25

-

strain 1YdBTEX2, pH 7.5, 25°C

659889

1.13.11.2

60.5

-

mutant T249S

673546

1.13.11.2

118

-

wildtype

673546

1.13.11.2

150

-

pH and temperature not specified in the publication

743199

1.13.11.2

190

-

-

439588

1.13.11.2

200

-

pH not specified in the publication, temperature not specified in the publication

764859

1.13.11.2

490

-

-

439588

1.13.11.39

3

-

25°C

685422

1.13.11.39

4.4

-

25°C, pH 7.5

659021

1.13.11.39

8

-

25°C

685422

1.13.11.39

9.8

-

25°C, pH 7.5

659021

1.13.11.39

10.15

-

pH 7.5, 30°C

725631

1.13.11.39

12.02

-

pH 7.5, 30°C

725631

1.13.11.39

13.6

-

25°C, pH 7.5

659021

1.13.11.39

14

-

60°C

685422

1.13.11.39

16

-

pH 8.0, 20°C

703749

1.13.11.39

21.63

-

pH 7.5, 30°C

725631

1.13.11.39

44

-

pH 9.0, 40°C, recombinant enzyme

724640

1.13.11.2

13 entries

1.13.11.39

11 entries

K_M Value (54 results)

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Show KM Value (54 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.10.3.1

1.31

-

pH 5.6, 25°C, MES buffer

744952

1.10.3.1

3.69

-

pH 5.4, 25°C, sodium acetate buffer

744952

1.13.11.1

0.001

-

pH not specified in the publication, 25°C

680483

1.13.11.1

0.0017

-

-

395005

1.13.11.1

0.00225

-

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

711314

1.13.11.1

0.00225

-

wild-type enzyme

697316

1.13.11.1

0.0032

-

-

676763

1.13.11.1

0.0037

-

-

395008

1.13.11.1

0.0048

-

at pH 7.2 and 45°C

743243

1.13.11.1

0.0056

-

pH not specified in the publication, 25°C

680483

1.13.11.1

0.00595

-

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

711314

1.13.11.1

0.00595

-

mutant L69A

697316

1.13.11.1

0.0065

-

in 50 mM Tris/HCl, pH 7.2, 25°C

712893

1.13.11.1

0.009

-

-

395002

1.13.11.1

0.286

-

-

697245

1.13.11.16

0.09

-

-

395595

1.13.11.16

0.13

-

-

395596

1.13.11.2

0.001

-

-

439581

1.13.11.2

0.0015

-

strain 1YB2, pH 7.5, 25°C

659889

1.13.11.2

0.00164

-

-

439589

1.13.11.2

0.0017

-

pH 7.5,25 °C

726474

1.13.11.2

0.0018

-

-

439588

1.13.11.2

0.0024

-

-

439588

1.13.11.2

0.0032

-

strain 1YdBTEX2, pH 7.5, 25°C

659889

1.13.11.2

0.0036

-

pH 7.5, 60°C

726474

1.13.11.2

0.0038

-

wildtype

673546

1.13.11.2

0.01

-

metapyrocatechase 2

439568

1.13.11.2

0.0106

-

-

439566

1.13.11.2

0.0115

-

mutant T249S

673546

1.13.11.2

0.0143

-

mutant T249A

673546

1.13.11.2

0.0266

-

mutant T249G

673546

1.13.11.2

0.03

-

pH and temperature not specified in the publication

743199

1.13.11.2

0.035

-

pH not specified in the publication, temperature not specified in the publication

764859

1.13.11.2

0.06

-

metapyrocatechase 1

439568

1.13.11.2

0.418

-

pH 7.4, 32.5°C

765789

1.10.3.1

2 entries

1.13.11.1

13 entries

1.13.11.16

2 entries

1.13.11.2

18 entries

1.13.11.36

0.017

-

-

439432

1.13.11.39

0.001

-

60°C, pH 7.5

659212

1.13.11.39

0.0021

-

pH 7.5, 30°C

725631

1.13.11.39

0.024

-

pH 9.0, 25°C, recombinant His-tagged enzyme

742643

1.13.11.39

0.0616

-

pH 7.5, 30°C

725631

1.13.11.39

0.0688

-

pH 8.0, 20°C

703749

1.13.11.39

0.097

-

Glu79His mutant

439417

1.13.11.39

0.1

-

25°C, pH 7.5

659021

1.13.11.39

0.1306

-

pH 7.5, 30°C

725631

1.13.11.39

0.18

-

-

439417

1.13.11.39

0.19

-

-

439407

1.13.11.39

0.49

-

pH 9.0, 40°C, recombinant enzyme

724640

1.13.11.39

1.1

-

60°C

685422

1.13.11.39

1.23

-

25°C, pH 7.5

659021

1.13.11.39

1.94

-

25°C, pH 7.5

659021

1.13.11.39

2.1

-

25°C

685422

1.13.11.39

14.6

-

25°C

685422

1.13.11.39

16 entries

1.13.11.56

0.15

-

pH 6.2, 25°C

698537

1.14.18.1

20

-

-

636399

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.74

0.0068

-

pH and temperature not specified in the publication

722603

References & Links

Literature References (116)

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Show Reference (116 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4714

29563

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

1978

Nakazawa, T.; Hayashi, E.

Appl. Environ. Microbiol.

36

264-269

4835

1856161

Genetic organization and regulation of a meta cleaveage pathway for catechols produced from catabolism of toluene, benzene, phenol, and cresols by Pseudomonas pickettii PKO1

1991

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

J. Bacteriol.

173

4587-4594

7066

8075807

3-Sulfocatechol 2,3-dioxygenase and other dioxygenases (EC 1.13.11.2 and EC 1.14.12.) in the degradative pathways of 2-aminobenzenesulfonic, benzenesulfonic and 4-toluenesulfonic acids in Alcaligenes sp. strain O-1

1994

Junker, F.; Leisinger, T.; Cook, A.M.

Microbiology

140

1713-1722

247041

-

Purification and some propertiees of a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolyzing enzyme from Pseudomonas cruciviae S93 B1 involved in the degradation of biphenyl

1986

Omori, T.; Sugimura, K.; Ishigooka, H.; Minoda, Y.

Agric. Biol. Chem.

50

931-937

390641

4369091

Purification and properties of (plus)-cis-naphthalene dihydrodiol dehydrogenase of Pseudomonas putida

1974

Patel, T.R.; Gibson, D.T.

J. Bacteriol.

119

879-888

390642

62750

Bacterial cis-dihydrodiol dehydrogenases: comparison of physicochemical and immunological protperties

1976

Patel, T.R.; Gibson, D.T.

J. Bacteriol.

128

842-850

390643

8434923

Metabolism of tetralin (1,2,3,4-tetrahydronaphthalene) in Corynebacterium sp. strain C125

1993

Sikkema, J.; De Bont, J.A.M.

Appl. Environ. Microbiol.

59

567-572

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

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

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

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

395595

8399388

Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli

1993

Bugg, T.D.

Biochim. Biophys. Acta

1202

258-264

395596

8752345

Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases

1996

Spence, E.L.; Kawamukai, M.; Sanvoisin, J.; Braven, H.; Bugg, T.D.

J. Bacteriol.

178

5249-5256

396380

-

A laccase-like enzyme in peaches

1968

Mayer, A.M.; Harel, E.

Phytochemistry

7

1253-1256

396602

-

Assay of enzymes of aromatic metabolism

1971

Gibson, D.T.

Methods Microbiol.

6A

463-478

438806

220242

The stereochemistry of NADH utilization by the flavoenzyme monooxygenase orcinol hydroxylase

1979

Ryerson, C.C.; Walsh, C.

J. Biol. Chem.

254

4349-4351

438808

1280

Bacterial metabolism of resorcinylic compounds: purification and properties of orcinol hydroxylase and resorcinol hydroxylase from Pseudomonas putida ORC

1976

Ohta, Y.; Ribbons, D.W.

Eur. J. Biochem.

61

259-269

439402

-

Enzymatic dioxygenation of biphenyl-2,3-diol and 3-isopropylcatechol

1986

Ishigooka, H.; Yoshida, Y.; Omori, T.; Minoda, Y.

Agric. Biol. Chem.

50

1045-1046

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

439413

8633883

Purification of 2,3-dihydroxybiphenyl 1,2-dioxygenase from Pseudomonas putida OU83 and characterization of the gene (bphC)

1996

Khan, A.A.; Wang, R.F.; Nawaz, M.S.; Cao, W.W.; Cerniglia, C.E.

Appl. Environ. Microbiol.

62

1825-1830

439415

9857017

Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol

1998

Vaillancourt, F.H.; Han, S.; Fortin, P.D.; Bolin, J.T.; Eltis, L.D.

J. Biol. Chem.

273

34887-34895

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

439417

10438749

Catalytic properties of the 3-chlorocatechol-oxidizing 2,3-dihydroxybiphenyl 1,2-dioxygenase from Sphingomonas sp. strain BN6

1999

Riegert, U.; Heiss, G.; Kuhm, A.E.; Mueller, C.; Contzen, M.; Knackmuss, H.J.; Stolz, A.

J. Bacteriol.

181

4812-4817

439420

11707443

The mechanism-based inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase by catecholic substrates

2002

Vaillancourt, F.H.; Labbe, G.; Drouin, N.M.; Fortin, P.D.; Eltis, L.D.

J. Biol. Chem.

277

2019-2027

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

439483

4967959

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

1968

Fujisawa, H.; Hayaishi, O.

J. Biol. Chem.

243

2673-2681

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

636399

-

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

1978

Chaplin, M.F.

Phytochemistry

17

1897-1899

644712

10217792

Adenosylcobalamin-mediated methyl transfer by toluate cis-dihydrodiol dehydrogenase of the TOL plasmid pWW0

1999

Lee, J.Y.; Park, H.S.; Kim, H.S.

J. Bacteriol.

181

2953-2957

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

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

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

659689

-

Purification and characterization of 2,3-dihydroxybiphenyl 1,2-dioxygenase from Comamonas sp. SMN4

2003

Lee, N.; Lee, J.M.; Min, K.H.; Kwon, D.Y.

J. Microbiol. Biotechnol.

13

487-494

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

673546

16734718

The role of residue Thr249 in modulating the catalytic efficiency and substrate specificity of catechol-2,3-dioxygenase from Pseudomonas stutzeri OX1

2006

Siani, L.; Viggiani, A.; Notomista, E.; Pezzella, A.; Di Donato, A.

FEBS J.

273

2963-2976

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

675335

-

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

2006

Cha, C.

J. Microbiol. Biotechnol.

16

778-785

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

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

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

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

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

699726

19739645

The laccase-catalyzed domino reaction between catechols and heterocyclic 1,3-dicarbonyls and the unambiguous structure elucidation of the products by NMR spectroscopy and X-ray crystal structure analysis

2009

Hajdok, S.; Conrad, J.; Leutbecher, H.; Strobel, S.; Schleid, T.; Beifuss, U.

J. Org. Chem.

74

7230-7237

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

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

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

713169

21221457

Dioxygenase-catalysed cis-dihydroxylation of meta-substituted phenols to yield cyclohexenone cis-diol and derived enantiopure cis-triol metabolites

2011

Boyd, D.R.; Sharma, N.D.; Stevenson, P.J.; Blain, M.; McRoberts, C.; Hamilton, J.T.; Argudo, J.M.; Mundi, H.; Kulakov, L.A.; Allen, C.C.

Org. Biomol. Chem.

9

1479-1490

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

724640

21898128

Isolation, characterization and docking studies of 2,3-dihydroxybiphenyl 1,2-dioxygenase from an activated sludge metagenome

2012

Gou, M.; Qu, Y.; Xu, B.; Zhou, J.; Li, X.; Zhou, H.

Biotechnol. Lett.

34

117-123

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

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

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

742643

27784944

Characteristics of a recombinant 2,3-dihydroxybiphenyl 1,2-dioxygenase from Comamonas sp. expressed in Escherichia coli

2016

Lee, N.; Kwon, D.Y.

Indian J. Microbiol.

56

467-475

742664

-

Decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 and its structure characterization

2014

Kwon, D.; Suma, Y.; Tiwari, M.; Choi, J.; Kang, L.; Lee, J.; Kim, H.

Int. Biodeter. Biodegrad.

95

67-75

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

743118

-

Catalytic properties of 2,3-dihydroxybiphenyl 1,2-dioxygenase from Dyella ginsengisoli LA-4 immobilized on mesoporous silica SBA-15

2014

Qu, Y.; Kong, C.; Zhou, H.; Shen, E.; Wang, J.; Shen, W.; Zhang, X.; Zhang, Z.; Ma, Q.; Zhou, J.

J. Mol. Catal. B

99

136-142

743199

-

Cloning and kinetic properties of Catechol 2,3-dioxygenase from novel alkaliphilic BTEX-degrading Pseudomonas sp. HB01

2014

Hassan, H.; Zein Eldein, A.; Rizk, N.

Life Sci. J.

11

376-384

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

744131

29196788

Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases

2018

Frommhagen, M.; Westphal, A.; Hilgers, R.; Koetsier, M.; Hinz, S.; Visser, J.; Gruppen, H.; van Berkel, W.; Kabel, M.

Appl. Microbiol. Biotechnol.

102

1281-1295

744952

25308684

Characterization of polyphenol oxidase activity in Ataulfo mango

2015

Cheema, S.; Sommerhalter, M.

Food Chem.

171

382-387

763927

29959655

Versatile catechol dioxygenases in Sphingobium scionense WP01T

2018

Muthu, M.; Ophir, Y.; Macdonald, L.J.; Vaidya, A.; Lloyd-Jones, G.

Antonie van Leeuwenhoek

111

2293-2301

764859

28847603

Isolation and characterization of three novel catechol 2,3-dioxygenase from three novel haloalkaliphilic BTEX-degrading Pseudomonas strains

2017

Hassan, H.A.; Aly, A.A.

Int. J. Biol. Macromol.

106

1107

765013

29380863

Catechol 2,3-dioxygenase from a new phenolic compound degrader Thauera sp. K11 purification and biochemical characterization

2018

Xi, L.; Liu, D.; Wang, L.; Qiao, N.; Liu, J.

J. Basic Microbiol.

58

255-262

765182

32036315

Insights into the binding interaction of substrate with catechol 2,3-dioxygenase from biophysics point of view

2020

Zeng, X.H.; Du, H.; Zhao, H.M.; Xiang, L.; Feng, N.X.; Li, H.; Li, Y.W.; Cai, Q.Y.; Mo, C.H.; Wong, M.H.; He, Z.L.

J. Hazard. Mater.

391

122211

765206

34740038

Discovery and characterization of a novel Dyp-type peroxidase from a marine actinobacterium isolated from Trondheim fjord, Norway

2022

Cordas, C.M.; Nguyen, G.S.; Valerio, G.N.; Jonsson, M.; Soellner, K.; Aune, I.H.; Wentzel, A.; Moura, J.J.G.

J. Inorg. Biochem.

226

111651

765713

-

Expression and characterization of catechol 1,2-dioxygenase from Oceanimonas marisflavi 102-Na3

2021

Li, J.; Li, Z.; Cao, M.; Liu, J.

Protein Expr. Purif.

188

105964

765789

34907211

A novel Bacillus ligniniphilus catechol 2,3-dioxygenase shows unique substrate preference and metal requirement

2021

Adewale, P.; Lang, A.; Huang, F.; Zhu, D.; Sun, J.; Ngadi, M.; Yang, T.C.

Sci. Rep.

11

23982

Links to other databases for 3-methylcatechol

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