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Ligand pyrogallol

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for pyrogallol

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Roles as Enzyme Ligand

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

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Show Natural Substrate (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.35

1,2,3-trihydroxybenzene + O2 = (Z)-5-oxohex-2-enedioate

439436

-

1.14.18.1

pyrogallate + O2 = ?

745665

-

1.14.18.1

pyrogallol + O2 = ?

745136

-

1.14.18.1

pyrogallol + O2 = ? + 2 H2O

746276

-

1.14.18.1

3 entries

1.97.1.2

1,2,3,5-tetrahydroxybenzene + pyrogallol = ?

437674, 437677, 437680, 4734

4v4d, 3D-view

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

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.1.59

3,4,5-Trihydroxybenzoate = Pyrogallol + CO2

653152, 650639

-

4.1.1.59

gallic acid = pyrogallol + CO2

0

-

4.1.1.59

2 entries

Substrate in Enzyme-catalyzed Reactions (59 results)

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Show Substrate (59 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.1

pyrogallol + O2 = ?

658789, 674089, 675458, 673560, 658950, 675167, 744221, 440427, 658960, 658788, 659821, 699242, 744952, 675101, 673779, 440433, 440441, 440434, 440437, 706120, 701760, 713239

-

1.10.3.2

4 1,2,3-trihydroxybenzene + O2 = ?

726534

-

1.10.3.2

4 pyrogallol + O2 = ?

725692

-

1.10.3.2

benzene-1,2,3-triol + O2 = ?

724662

-

1.10.3.2

pyrogallol + 4-aminoantipyrine + O2 = ? + H2O

655631

-

1.10.3.2

pyrogallol + O2 = ?

396372, 396367, 396358, 701029, 396394, 396375, 696919, 396352, 696857, 396381, 743078, 724573, 671528, 684533, 712084, 725731, 742104, 743661, 763988, 686794, 712724, 741501, 743116

-

1.10.3.2

pyrogallol + O2 = ? + H2O

656729, 687338, 655375, 684533, 655362, 655919, 655377

-

1.10.3.2

6 entries

1.10.3.6

pyrogallol + ? = ?

439882

-

1.11.1.10

pyrogallol + chloride + H2O2 = ?

725151

-

1.11.1.10

pyrogallol + H2O2 = ?

713167

-

1.11.1.11

pyrogallol + H2O2 = 3-hydroxybenzo-1,2-quinone + H2O

439857, 439855, 439874, 439861, 439869, 439871, 439868, 439875, 439865, 439864, 439858, 439860, 439873

-

1.11.1.11

pyrogallol + H2O2 = ?

713220, 711139, 713299

-

1.11.1.11

pyrogallol + H2O2 = ? + H2O

654378

-

1.11.1.13

pyrogallol + H2O2 + Mn2+ = ?

699016

-

1.11.1.13

pyrogallol + H2O2 = ?

699016

-

1.11.1.13

pyrogallol + Mn2+ + ? = ?

699016

-

1.11.1.19

pyrogallol + H2O2 + H+ = ?

695785, 742674, 742684

-

1.11.1.19

pyrogallol + H2O2 + H+ = oxidized pyrogallol + H2O

764924, 764606, 742674

-

1.11.1.21

pyrogallol + H2O2 = ?

696108

-

1.11.1.21

pyrogallol + H2O2 = ? + H2O

714289, 685401, 715423, 439790, 714283, 439783, 724122, 714389, 686777, 654706

-

1.11.1.10

2 entries

1.11.1.11

3 entries

1.11.1.13

3 entries

1.11.1.19

2 entries

1.11.1.21

2 entries

1.11.1.24

H2O2 + pyrogallol = ?

764883

-

1.11.1.5

pyrogallol + H2O2 = ?

394614, 394616

-

1.11.1.6

pyrogallol + H2O2 = ? + H2O

439790, 439801

-

1.11.1.7

2 pyrogallol + H2O2 = ? + H2O

764055

-

1.11.1.7

pyrogallol + H2O2 = ?

695687

-

1.11.1.7

pyrogallol + H2O2 = ? + H2O

743175, 659619, 742414, 742733, 764054, 765164

-

1.11.1.7

pyrogallol + H2O2 = purpurogallin + H2O

439769, 671853, 674130, 439747, 439736, 699519, 698420, 671394, 684531, 695687, 695785

-

1.11.1.7

4 entries

1.11.2.3

pyrogallol + H2O2 = purpurogallin + H2O

671684

-

1.13.11.1

1,2,3-trihydroxybenzene + O2 = 2-hydroxymuconate

394998

3hhx, 3D-view

1.13.11.1

pyrogallol + O2 = ?

743243

3hhx, 3D-view

1.13.11.1

pyrogallol + O2 = alpha-hydroxymuconic acid

659536, 394989, 395001, 394987, 676763, 712893

3hhx, 3D-view

1.13.11.2

3-hydroxycatechol + O2 = 3-hydroxymuconic acid

439570, 439571

-

1.13.11.2

pyrogallol + O2 = ?

765713

-

1.13.11.1

3 entries

1.13.11.2

2 entries

1.13.11.3

pyrogallol + O2 = ?

725655, 439501, 439502, 439483

-

1.13.11.35

1,2,3-trihydroxybenzene + O2 = (Z)-5-oxohex-2-enedioate

439436

-

1.13.11.57

pyrogallol + O2 = ?

715355

-

1.14.14.20

pyrogallol + O2 + NADPH = ?

438788

-

1.14.18.1

pyrogallate + O2 = ?

745665

-

1.14.18.1

pyrogallate + O2 = ? + 2 H2O

745474

-

1.14.18.1

pyrogallol + 1/2 O2 = ?

687154, 687875, 684232, 686847, 689407, 686484, 685018

-

1.14.18.1

pyrogallol + O2 = ?

636410, 636370, 636399, 745136, 636383, 636372, 636373, 636452, 699242, 712618, 745665, 745557, 636443, 636434, 699628, 712619

-

1.14.18.1

pyrogallol + O2 = ? + 2 H2O

744824, 746276

-

1.14.18.1

5 entries

1.14.99.54

cellooligosaccharide + pyrogallol + O2 = ?

745861

-

1.14.99.56

cellooligosaccharide + pyrogallol + O2 = ?

745861

-

1.14.99.B10

xylooligosaccharide + pyrogallol + O2 = ? + H2O

745861

-

1.15.1.1

pyrogallol + ? = ?

675047, 671561, 673379

-

1.16.3.1

pyrogallol + Fe2+ + O2 = ?

438006

-

1.3.3.5

pyrogallol + O2 = ?

391019

-

1.97.1.2

1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene = 1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene

673091

4v4d, 3D-view

1.97.1.2

1,2,3,5-tetrahydroxybenzene + pyrogallol = ?

437674, 437677, 437680, 4734

4v4d, 3D-view

1.97.1.2

1,2,3,5-tetrahydroxybenzene + pyrogallol = phloroglucinol + 1,2,3,5-tetrahydroxybenzene

4734, 437677, 437678, 437679, 437680, 437674, 437676

4v4d, 3D-view

1.97.1.2

1,2,4,5-tetrahydroxybenzene + pyrogallol = hydroxyhydroquinone + 1,2,3,5-tetrahydroxybenzene

437676

4v4d, 3D-view

1.97.1.2

hydroxyhydroquinone + pyrogallol = resorcinol + 1,2,3,5-tetrahydroxybenzene

437676, 437674

4v4d, 3D-view

1.97.1.2

5 entries

2.1.1.6

S-adenosyl-L-methionine + pyrogallol = S-adenosyl-L-homocysteine + ?

658517

-

2.1.1.68

S-adenosyl-L-methionine + pyrogallol = ?

485542

-

2.4.1.358

UDP-alpha-D-glucose + pyrogallol = UDP + ?

748951

-

3.1.1.20

pyrogallol + H2O = ?

715957

-

3.2.1.168

pyrogallol + hesperidin = 2,3-dihydroxyphenyl beta-D-rutinoside + hesperetin

753044

-

3.2.1.8

pyrogallol + H2O = ?

696821

-

Product in Enzyme-catalyzed Reactions (7 results)

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Show Product (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.1

2,6-dihydroxybenzoate + NADH + 2 H+ + O2 = 1,2,3-trihydroxybenzene + NAD+ + H2O + CO2

0

-

1.14.13.1

2,3-dihydroxybenzoate + NADH + 2 H+ + O2 = pyrogallol + NAD+ + H2O + CO2

0

-

1.14.13.1

2,3-dihydroxybenzoate + NADH + O2 = pyrogallol + CO2 + H2O + NAD+

389999, 0, 439423

-

1.14.13.1

2,6-dihydroxybenzoate + NADH + O2 = pyrogallol + CO2 + H2O + NAD+

389999, 0, 439423

-

4.1.1.59

3,4,5-Trihydroxybenzoate = Pyrogallol + CO2

4728, 4729, 4730, 4734, 4731, 4732, 4733, 650639, 653152

-

4.1.1.59

gallic acid = pyrogallol + CO2

0

-

1.14.13.1

4 entries

4.1.1.59

2 entries

4.1.1.61

3,4,5-Trihydroxybenzoate = Pyrogallol + CO2

0

-

Inhibitor in Enzyme-catalyzed Reactions (22 results)

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Show Inhibitors (22 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.6

-

725146

-

1.13.11.1

-

394987

3hhx, 3D-view

1.13.11.37

mixed inhibition

439429

-

1.13.11.56

0.0005 mM, 76% inhibition

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

1.13.12.16

-

639224

-

1.14.11.2

-

439194

-

1.14.11.4

most potent

439156

-

1.14.18.1

enzyme-inhibitor interaction measurement by SPR

745133

-

2.1.1.6

-

441516, 441525, 686194

-

2.1.1.6

70-100% inhibition at 0.2 mM

441515

-

2.1.1.6

2 entries

2.7.7.48

-

672464

-

3.1.1.20

-

729424

-

3.1.1.20

95% residual activity at 1 mM

714559

-

3.1.1.20

competitive; i.e. pyrogallol

94249

-

3.1.1.20

3 entries

3.4.15.1

-

731965

-

3.4.24.82

-

708082

-

3.4.24.B12

-

708082

-

4.1.3.4

a mixed-type noncompetitive inhibitor

727117

-

4.2.1.1

-

748307

-

4.8.1.2

slight inhibition

650189

-

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

3hhx, 3D-view

1.97.1.2

4v4d, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (22 results)

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Show Turnover Number (22 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.10.3.1

1263

-

-

675458

1.10.3.2

10

-

pH 7.0, 30°C

655375

1.10.3.2

1231.3

-

pH 8.0, 40°C

742104

1.10.3.2

2 entries

1.11.1.10

26.56

-

in 50 mM phosphate buffer pH 2.75 at 30°C, with 20 mM KCl

725151

1.11.1.11

160

-

wild-type, Cys32Ser mutant and DTNB-modified enzyme

439873

1.11.1.13

9.98

-

-

699016

1.11.1.13

9.98

-

in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C

699016

1.11.1.13

20.95

-

-

699016

1.11.1.13

20.95

-

in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C

699016

1.11.1.13

4 entries

1.11.1.19

7.9

-

at pH 4.0 and 25°C

764924

1.11.1.21

27

-

pH 4.0, 23°C

685401

1.11.1.21

44

-

pH 4.5, 23°C

685401

1.11.1.21

56

-

pH 5.0, 23°C

685401

1.11.1.21

64

-

pH 5.5, 23°C

685401

1.11.1.21

69

-

pH 6.0, 23°C

685401

1.11.1.21

630

-

pH 5.0, 23°C

724122

1.11.1.21

6 entries

1.11.1.5

8

-

-

394616

1.11.1.7

102.5

-

30°C, pH 5.5, isoenzyme E5

671394

1.11.1.7

230

-

pH 5.0, 16°C

743175

1.11.1.7

2 entries

1.13.11.1

2.41

-

in 50 mM Tris/HCl, pH 7.2, 25°C

712893

1.14.18.1

9.7

-

-

636370

1.14.18.1

1280

-

-

685018

1.14.18.1

2 entries

K_M Value (64 results)

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Show KM Value (64 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.10.3.1

0.79

-

pH 6.0, 25°C, MES buffer

744952

1.10.3.1

0.83

-

pH 5.8, 25°C, sodium phosphate buffer

744952

1.10.3.1

1

-

pH 3.5, 25°C

675101

1.10.3.1

1.26

-

pH 5.4, 25°C, MES buffer

744952

1.10.3.1

1.3

-

isozyme PPO 1, in 0.2 M sodium phosphate buffer pH 7.0, 25°C

713239

1.10.3.1

2.16

-

-

675458

1.10.3.1

3.42

-

pH 9.0, 25°C

674089

1.10.3.1

3.9

-

-

658789

1.10.3.1

5.2

-

-

658960

1.10.3.1

7.31

-

pH 5.6, 25°C, sodium acetate buffer

744952

1.10.3.1

9.465

-

-

699242

1.10.3.1

12.5

-

-

440434

1.10.3.1

19.6

-

pH 6.8, 25°C

744221

1.10.3.2

0.0145

-

pH 8.0, 40°C

742104

1.10.3.2

0.023

-

pH 7.0, 30°C

655375

1.10.3.2

0.03

-

-

396394

1.10.3.2

0.32

-

-

684533

1.10.3.2

0.32

-

in 50 mM sodium malonate buffer, pH 4.5 at 37°C

684533

1.10.3.2

0.56

-

in McIlvaine buffer (pH 4.0), at 30°C

712084

1.10.3.2

24.6

-

30°C, pH 3.0

656729

1.10.3.1

13 entries

1.10.3.2

7 entries

1.11.1.10

0.089

-

in 50 mM phosphate buffer pH 2.75 at 30°C, with 20 mM KCl

725151

1.11.1.11

2.4

-

recombinant enzyme

439864

1.11.1.11

9.6

-

-

439858

1.11.1.13

0.293

-

-

699016

1.11.1.13

0.293

-

in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C

699016

1.11.1.13

3.74

-

-

699016

1.11.1.13

3.74

-

in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C

699016

1.11.1.11

2 entries

1.11.1.13

4 entries

1.11.1.19

119

-

at pH 4.0 and 25°C

764924

1.11.1.21

0.2

-

pH 5.0, 23°C

724122

1.11.1.21

0.31

-

peroxidatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C

715423

1.11.1.21

1.1

-

pH 4.0, 23°C

685401

1.11.1.21

1.1

-

pH 4.5, 23°C

685401

1.11.1.21

1.3

-

pH 5.0, 23°C

685401

1.11.1.21

1.5

-

pH 5.5, 23°C

685401

1.11.1.21

1.6

-

pH 6.0, 23°C

685401

1.11.1.21

7 entries

1.11.1.5

5

-

-

394616

1.11.1.7

0.29

-

at pH 5.5

698420

1.11.1.7

0.449

-

pH 5.0, 16°C

743175

1.11.1.7

1.2

-

-

659619

1.11.1.7

1.63

-

at pH 6.0

698420

1.11.1.7

2

3

in 50 mM sodium acetate buffer, at pH 5.5

684531

1.11.1.7

2.5

-

30°C, pH 5.0

674130

1.11.1.7

23.8

-

-

439769

1.11.1.7

55.4

-

30°C, pH 5.5, isoenzyme E5

671394

1.13.11.1

0.0045

-

in 50 mM Tris/HCl, pH 7.2, 25°C

712893

1.13.11.1

0.0093

-

at pH 7.2 and 45°C

743243

1.11.1.7

8 entries

1.13.11.1

2 entries

1.13.11.3

0.014

-

pH 7.5, 38°C

725655

1.14.18.1

0.11

-

pH 8.5, 15°C

745474

1.14.18.1

0.3

-

detected in dormant saffron corms

684232

1.14.18.1

0.7

-

-

636410

1.14.18.1

1.11

-

-

636370

1.14.18.1

1.24

-

-

686847

1.14.18.1

1.4

-

Lineweaver-Burk plot of pyrogallol oxidation by the mushroom PPO

687154

1.14.18.1

1.7

-

-

636399

1.14.18.1

1.96

-

-

685018

1.14.18.1

2.77

-

pH 7.0, 25°C

745136

1.14.18.1

5.8

-

pH 5.6, 37°C

745665

1.14.18.1

6.3

-

-

636373

1.14.18.1

8

-

pH 5.6, 37°C

745665

1.14.18.1

20.11

-

pH 6.5, 28°C

745557

1.14.18.1

57

-

at pH 7.0, 30°C

712618

1.14.18.1

3000

-

-

686484

1.14.18.1

15 entries

1.16.3.1

0.0579

-

-

438006

3.1.1.20

16.94

-

pH 5.0, 45°C

715957

K_i Value (10 results)

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Show KI Value (10 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.37

0.00069

-

-

439429

1.13.11.74

0.0084

-

pH and temperature not specified in the publication

722603

1.14.11.2

0.03

-

-

439194

3.4.24.82

0.00634

-

pH 7.5, 37°C, substrate: C6-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-Gly-Thr-Lys(7-methoxycoumarin-4-yl)-Gly-Glu–Leu–Glu–Gly-Arg–Gly-Thr-Lys(Dnp)-Gly-Ile-Ser-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-NH2

708082

3.4.24.82

0.041

-

pH 7.5, 37°C, substrate: Lys(7-methoxycoumarin-4-yl)-Lys-Gln-Glu-Phe-Arg-Gly-Gln-Thr-Lys(Dnp)-NH2

708082

3.4.24.B12

0.00363

-

pH 7.5, 37°C, substrate: C6-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-Gly-Thr-Lys(7-methoxycoumarin-4-yl)-Gly-Glu–Leu–Glu–Gly-Arg–Gly-Thr-Lys(Dnp)-Gly-Ile-Ser-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-NH2

708082

3.4.24.B12

0.037

-

pH 7.5, 37°C, substrate: Lys(7-methoxycoumarin-4-yl)-Lys-Gln-Glu-Phe-Arg-Gly-Gln-Thr-Lys(Dnp)-NH2

708082

3.4.24.82

2 entries

3.4.24.B12

2 entries

4.1.3.4

0.0074

-

pH 7.5, 37°C

727117

4.2.1.1

0.00054

-

pH 8.3, 22°C

748307

4.2.1.1

0.00741

-

pH 8.3, 22°C

748307

4.2.1.1

2 entries

IC₅₀ Value (6 results)

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Show IC50 Value (6 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.11.1.6

0.0018

-

pH 7.0, 23°C

725146

2.7.7.48

0.01

-

-

672464

3.4.15.1

1.12

-

37°C, pH not specified in the publication

731965

3.4.15.1

1.12

-

pH not specified in the publication, 37°C

731965

3.4.15.1

2 entries

3.4.24.82

0.005

-

pH 7.5, 37°C

708082

4.1.3.4

0.0615

-

pH 7.5, 37°C

727117

References & Links

Literature References (209)

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Show Reference (209 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4728

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1969

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Isolation and identification of a pyrogallol producing bacterium from soil

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Initial steps of catabolism of trihydroxybenzenes in Pelobacter acidigallici

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439194

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

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Inhibition analysis of hydroxyquinol-cleaving dioxygenases from the chlorophenol-degrading Azotobacter sp. GP1 and Streptomyces rochei 303

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439501

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1980

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Biochemistry

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439502

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Protocatechuate 3,4-dioxygenase from Nocardia erythropolis

1984

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Peroxidase from human cervical mucus. The isolation and characterisation

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Catalase form Comamonas compransoris

1982

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439855

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Purification, properties, and distribution of ascorbate peroxidase in legume root nodules

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Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase

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439858

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Purification and some properties of L-ascorbic-acid-specific peroxidase in Euglena gracilis Z

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439860

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Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical

1987

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Plant Cell Physiol.

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439861

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Cytosolic ascorbate peroxidase in seedlings and leaves of maize (Zea mays)

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Plant Cell Physiol.

34

713-721

439864

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Heterologous expression and characterization of soybean cytosolic ascorbate peroxidase

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328

1-8

439865

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Plant Sci.

120

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439868

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Purification and characterization of ascorbate peroxidase in roots of Japanese radish

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Plant Sci.

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439869

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Identification of two cytosolic ascorbate peroxidase cDNAs from soybean leaves and characterization of their products by functional expression in E. coli

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Purification and characterization of ascorbate peroxidase in Chlorella vulgaris

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439873

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Identification of two electron-transfer sites in ascorbate peroxidase using chemical modification, enzyme kinetics, and crystallography

1998

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Biochemistry

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Molecular characterization and physiological role of ascorbate peroxidase from halotolerant Chlamydomonas sp. W80 strain

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439875

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Purification and characterization of an ascorbate peroxidase from potato tuber mitochondria

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Rifamycin B oxidase from Monocillium spp., a new type of diphenol oxidase

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FEBS Lett.

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440427

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Purification and characterization of polyphenol oxidase from banana (Musa sapientum L.) pulp

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Partial purification and characterization of polyphenol oxidase from banana (Musa sapientum L.) peel

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Solubilization and partial purification of particulate catechol-O-methyltransferase from rat liver

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441516

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Kinetics and inhibition studies of catechol O-methyltransferase from the yeast Candida tropicalis

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Purification and properties of caffeic acid O-methyltransferase from alfalfa root nodules

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636370

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Extracellular tyrosinase from Streptomyces sp. KY-453: purification and some enzymatic properties

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Properties of polyphenol oxidase from tubers of the yam Dioscora bulbifera

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636373

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Purification and some properties of polyphenol oxidase from the yam tubers, Dioscorea bulbifera

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Phytochemistry

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636383

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Purification and some properties of o-diphenolase from white yam tubers

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Phytochemistry

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636399

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

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Phytochemistry

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Tea catechol oxidase: isolation, purification and kinetic characterization

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Phytochemistry

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636434

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Biochemistry

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

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Purification and characterization of an extracellular laccase of a fungus (family Chaetomiaceae) isolated from soil

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An acid-stable laccase from Sclerotium rolfsii with potential for wool dye decolorization

2003

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Characterization of alkaliphilic laccase activity in the culture supernatant of Myrothecium verrucaria 24G-4 in comparison with bilirubin oxidase

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

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2003

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

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

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Purification and characterization of polyphenol oxidase from Henry chestnuts (Castanea henryi)

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Production and characterization of laccase from Cyathus bulleri and its use in decolourization of recalcitrant textile dyes

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