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Ligand 2,6-dimethoxyphenol

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (39 results)

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Show Substrate (39 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.2

2,6-dimethoxy phenol + O2 = ?

724573

3fu7, 3D-view

1.10.3.2

2,6-dimethoxy phenol + O2 = ?

724573

3fu8, 3D-view

1.10.3.2

2,6-dimethoxyphenol + 4-aminoantipyrine + O2 = ? + H2O

655631

3fu7, 3D-view

1.10.3.2

2,6-dimethoxyphenol + 4-aminoantipyrine + O2 = ? + H2O

655631

3fu8, 3D-view

1.10.3.2

2,6-dimethoxyphenol + H2O = ?

655487

3fu7, 3D-view

1.10.3.2

2,6-dimethoxyphenol + H2O = ?

655487

3fu8, 3D-view

1.10.3.2

2,6-dimethoxyphenol + O2 = 3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O

674926, 673387, 673096, 671403, 671540, 673816, 671514, 671510, 684533, 676943, 671391, 671552, 671560, 675042

3fu7, 3D-view

1.10.3.2

2,6-dimethoxyphenol + O2 = 3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O

674926, 673387, 673096, 671403, 671540, 673816, 671514, 671510, 684533, 676943, 671391, 671552, 671560, 675042

3fu8, 3D-view

1.10.3.2

2,6-dimethoxyphenol + O2 = ?

741713, 687819, 696090, 743712, 712644, 724569, 684645, 695796, 724662, 741797, 689115, 711175, 696919, 737487, 696911, 696857, 743078, 725302, 742173, 686794, 684626, 684624, 698523, 697668, 701029, 697913, 741664, 711502, 712084, 743080, 724013, 695839, 725731, 726411, 726416, 726713, 742013, 742658, 743648, 743727, 741634, 743103, 743711, 743888, 742104, 743661, 741648, 742638, 743786, 746372, 747726, 711500, 743114, 742681, 743116, 743017

3fu7, 3D-view

1.10.3.2

2,6-dimethoxyphenol + O2 = ?

741713, 687819, 696090, 743712, 712644, 724569, 684645, 695796, 724662, 741797, 689115, 711175, 696919, 737487, 696911, 696857, 743078, 725302, 742173, 686794, 684626, 684624, 698523, 697668, 701029, 697913, 741664, 711502, 712084, 743080, 724013, 695839, 725731, 726411, 726416, 726713, 742013, 742658, 743648, 743727, 741634, 743103, 743711, 743888, 742104, 743661, 741648, 742638, 743786, 746372, 747726, 711500, 743114, 742681, 743116, 743017

3fu8, 3D-view

1.10.3.2

2,6-dimethoxyphenol + O2 = ? + H2O

396394, 656729, 655374, 396354, 396400, 656736, 396396, 396402, 654307, 687338, 656847, 657149, 654297, 655375, 688328, 684533, 655362, 655377

3fu7, 3D-view

1.10.3.2

2,6-dimethoxyphenol + O2 = ? + H2O

396394, 656729, 655374, 396354, 396400, 656736, 396396, 396402, 654307, 687338, 656847, 657149, 654297, 655375, 688328, 684533, 655362, 655377

3fu8, 3D-view

1.11.1.13

2,6-dimethoxyphenol + H+ + H2O2 = ?

439841

-

1.11.1.13

2,6-dimethoxyphenol + H2O2 + H+ = coerulignone + H2O

439847

-

1.11.1.13

2,6-dimethoxyphenol + H2O2 + Mn2+ = ?

699016

-

1.11.1.13

2,6-dimethoxyphenol + H2O2 = ?

702978, 439840, 439844, 658331, 660342, 711491, 698032, 686451, 658136, 660488, 699016

-

1.11.1.13

2,6-dimethoxyphenol + H2O2 = coerulignone + H2O

439850

-

1.11.1.13

2,6-dimethoxyphenol + Mn2+ + ? = ?

699016

-

1.11.1.13

2,6-dimethoxyphenol + Mn2+ + H2O2 = coerulignone + Mn3+ + H2O

439850

-

1.11.1.13

H2O2 + 2,6-dimethoxyphenol = H2O + ?

658572

-

1.11.1.13

Mn2+ + 2,6-dimethoxyphenol + H2O2 = ?

699074, 697641

-

1.11.1.16

2,6-dimethoxyphenol + H+ + H2O2 = ?

742337, 741480

-

1.11.1.16

2,6-dimethoxyphenol + H2O2 = ?

663675

-

1.11.1.16

Mn2+ + H2O2 + 2,6-dimethoxyphenol = ?

725688

-

1.11.1.16

syringol + H+ + H2O2 = ?

743092

-

1.11.1.16

syringol + H2O2 = ? + H2O

665470

-

1.11.1.19

2,6-dimethoxyphenol + H2O2 + H+ = ?

743804, 741485, 711709, 710921, 710922, 742940, 710965, 743089, 741854, 743148, 743731, 741578, 742684, 695785, 710967, 712519, 711063, 723971, 743647, 742674

3vxj, 3D-view

1.11.1.19

2,6-dimethoxyphenol + H2O2 + H+ = oxidized 2,6-dimethoxyphenol + H2O

711709

3vxj, 3D-view

1.11.1.19

2,6-dimethoxyphenol + H2O2 = ?

710977

3vxj, 3D-view

1.10.3.2

12 entries

1.11.1.13

9 entries

1.11.1.16

5 entries

1.11.1.19

3 entries

1.11.1.21

2,6-dimethoxyphenol + H2O2 = oxidized 2,6-dimethoxyphenol + H2O

439784

-

1.11.1.6

2,6-dimethoxyphenol + H2O2 = ? + H2O

439784

-

1.11.1.7

2,6-dimethoxyphenol + H2O2 = ?

695785

-

1.11.1.7

2,6-dimethoxyphenol + H2O2 = ? + H2O

725088

-

1.11.2.1

2,6-dimethoxyphenol + H2O2 = ?

710926, 741683, 742290

5oy2, 3D-view

1.11.2.1

2,6-dimethoxyphenol + H2O2 = oxidized 2,6-dimethoxyphenol + H2O

710924

5oy2, 3D-view

1.11.1.7

2 entries

1.11.2.1

2 entries

1.14.99.54

2,6-dimethoxyphenol + 2 H2O2 = coerulignone + 2 H2O

744556

-

1.14.99.56

2,6-dimethoxyphenol + 2 H2O2 = coerulignone + 2 H2O

744556

-

1.16.3.1

2,6-dimethoxyphenol + Cu(I) + O2 = ?

728744

-

1.3.3.5

2,6-dimethoxyphenol + O2 = ? + H2O

745422

-

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.1.61

3,5-Dimethoxy-4-hydroxybenzoate = 1,3-Dimethoxy-2-hydroxybenzene + CO2

-

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.13.3

activation of VirA increases in the absence of enzyme aas 285-293

740310

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.4

IC50: 0.0624 mM, monoamine oxidase A; IC50: above 0.5 mM, monoamine oxidase B

672530

-

3D Structure of Enzyme-Ligand-Complex (PDB) (10 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (10 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.10.3.2

3fu7, 3D-view

1.10.3.2

3fu8, 3D-view

1.10.3.2

3fu7, 3D-view

1.10.3.2

3fu8, 3D-view

1.10.3.2

3fu7, 3D-view

1.10.3.2

3fu8, 3D-view

1.10.3.2

3fu7, 3D-view

1.10.3.2

3fu8, 3D-view

1.10.3.2

8 entries

1.11.1.19

3vxj, 3D-view

1.11.2.1

5oy2, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (129 results)

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Show Turnover Number (129 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.10.3.2

0.01

-

pH 7.6, 37°C, mutant M502F

674926

1.10.3.2

0.04

1.97

pH 7.0, 25°C

671403

1.10.3.2

0.058

-

25°C, pH 9.0

741648

1.10.3.2

0.1

-

recombinant mutant enzyme MmPPOA-637, pH 5.0, 25°C

746372

1.10.3.2

0.21

-

recombinant His-tagged mutant enzyme MmPPOA-637, pH 5.0, 25°C

746372

1.10.3.2

0.29

-

pH 3.4, 30°C, recombinant mutant D206E

676943

1.10.3.2

0.35

-

pH 5.0, 22-25°C

725731

1.10.3.2

0.42

-

pH 3.4, 30°C, recombinant mutant D206A

676943

1.10.3.2

0.51

-

pH 3.4, 30°C, recombinant wild-type enzyme

676943

1.10.3.2

0.66

-

pH 3.4, 30°C, recombinant mutant D206N

676943

1.10.3.2

0.92

-

recombinant wild-type enzyme MmPPOA-695, pH 5.0, 25°C

746372

1.10.3.2

1.55

-

pH 7.6, 37°C, mutant M502L

674926

1.10.3.2

1.74

-

recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C

746372

1.10.3.2

1.98

-

native wild-type enzyme, pH 5.0, 25°C

746372

1.10.3.2

2

8

pH 7.0

684645

1.10.3.2

2.3

-

pH 3.0, 37°C

743888

1.10.3.2

2.54

-

pH 4.5, 37°C

742638

1.10.3.2

2.93

-

pH 8.0, 70°C

743712

1.10.3.2

3

-

at 22°C, pH not specified in the publication

712644

1.10.3.2

3

6

pH 7.0, 25°C, wild-type CotA

696090

1.10.3.2

3.18

-

25°C, pH 6

684626

1.10.3.2

4.3

-

pH 4.0, 65°C

695839

1.10.3.2

4.5

-

pH 9.0, 25°C, mutant I494A

696090

1.10.3.2

6.45

-

pH 4.5, 37°C

743786

1.10.3.2

6.65

-

pH 7.6, 37°C, wild-type enzyme

674926

1.10.3.2

6.85

-

pH and temperature not specified in the publication

741664

1.10.3.2

6.91

-

pH 4.0, 25°C

671552

1.10.3.2

8.94

-

pH 7.0, 25°C

671403

1.10.3.2

9.08

-

pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae

697913

1.10.3.2

10.2

-

pH 4.5, 25°C, recombinant wild-type enzyme

697913

1.10.3.2

11

-

pH 7.0, 22°C, recombinant enzyme

724662

1.10.3.2

15

-

pH 5.5

671510

1.10.3.2

16.3

-

recombinant wild-type enzyme, pH 5.0, temperature not specified in the publication

724013

1.10.3.2

17

-

pH 7.0, 25°C, mutant L386A

696090

1.10.3.2

17.7

-

pH 3.8, 55°C

671391

1.10.3.2

23.2

-

21-23°C, pH not specified in the publication, wild-type enzyme

743727

1.10.3.2

26.4

-

recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication

724013

1.10.3.2

29

-

pH 7, holoCotA

687819

1.10.3.2

34

-

pH 7.0, 30°C

655375

1.10.3.2

34.4

-

pH 8.5, temperature not specified in the publication

742013

1.10.3.2

38.2

-

pH 5.0, temperature not specified in the publication

725302

1.10.3.2

38.5

-

recombinant enzyme, pH 3.0, 30°C

726411

1.10.3.2

38.8

-

21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)

743727

1.10.3.2

50

-

pH 4.8, 25°C

696911

1.10.3.2

50.3

-

pH 4.0, 25°C

743078

1.10.3.2

67

-

pH 6.0

656736

1.10.3.2

68

-

pH and temperature not specified in the publication

743080

1.10.3.2

73.15

-

pH 8.0, 85°C

743661

1.10.3.2

80.4

-

21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)

743727

1.10.3.2

81

-

pH 4.5, 25°C

654297

1.10.3.2

103

-

-

688328

1.10.3.2

109.2

-

pH 3.0, 50°C

726424

1.10.3.2

121

-

at 30°C in 100 mM sodium tartrate buffer (pH 4.5)

711500

1.10.3.2

180

-

pH 5.2, 45°C

673816

1.10.3.2

189

-

pH 4.5

656847

1.10.3.2

206

-

pH 5.0, isozyme Lac I

675042

1.10.3.2

218

-

pH 5.0, isozyme Lac II

675042

1.10.3.2

329

-

pH 4, 30°C

743711

1.10.3.2

347

-

pH 3.0, 25°C, laccase Lac-3.5

684624

1.10.3.2

365.6

-

pH 3.8, 55°C

671391

1.10.3.2

481

-

pH 3.0, 25°C, laccase Lac-4.8

684624

1.10.3.2

703.7

-

pH and temperature not specified in the publication

743648

1.10.3.2

1009.4

-

pH 8.0, 40°C

742104

1.10.3.2

1476

-

pH 4.0, 50°C

726416

1.10.3.2

20000

-

25°C, isozyme POXA3b

655374

1.10.3.2

23800

-

25°C, isozyme POXA3a

655374

1.11.1.13

3.98

-

-

660488

1.11.1.13

5.67

-

-

699016

1.11.1.13

5.67

-

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

699016

1.11.1.13

26.26

-

-

699016

1.11.1.13

26.26

-

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

69

-

30°C, pH 4.5

686451

1.11.1.13

70

-

Mn2+-independent activity

439841

1.11.1.13

200

-

MnP3

439840

1.11.1.13

320

-

Mn2+-dependent activity

439841

1.11.1.16

2.3

-

pH 4.5

394603

1.11.1.16

3

-

pH 3.0, isoenzyme PS3

665470

1.11.1.16

4.6

-

mutant E140G/P141G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

4.8

-

mutant P141G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

5.6

-

wild-type, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

6

-

pH 3.0, isoenzyme PS1

665470

1.11.1.16

6.2

-

mutant P76G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

7.6

-

mutant K215Q, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

9.3

-

mutant K176G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

9.5

-

mutant K215G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

9.8

-

mutant F142G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

10

-

mutant E140G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

10.6

-

absence of Mn2+, pH not specified in the publication, temperature not specified in the publication

724882

1.11.1.16

10.6

-

mutant K176D, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

17.3

-

mutant E140G/K176G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

20.4

-

mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

29.8

-

wild-type, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

30

-

presence of Mn2+, pH not specified in the publication, temperature not specified in the publication

724882

1.11.1.16

47.6

-

mutant W164S, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

50.2

-

mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

56.6

-

mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

58

-

mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication

724232

1.11.1.16

61

-

mutant E140G/P141G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

67

-

mutant E140G/K176G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

74.5

-

mutant K215Q, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

98

-

at pH 3.0 and 25°C

741480

1.11.1.16

98

-

wild-type, pH 3.5, temperature not specified in the publication

724232

1.11.1.16

141

-

mutant P141G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

231.6

-

mutant K176G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

293

-

mutant E140G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

54500

-

at 30°C and pH 4.5

743092

1.11.1.19

0.02

-

mutant enzyme E188K/H125R, at pH 4.3 and 25°C

741485

1.11.1.19

0.03

-

mutant enzyme H125R, at pH 4.3 and 25°C

741485

1.11.1.19

0.05

-

wild type enzyme, at pH 4.3 and 25°C

741485

1.11.1.19

0.09

-

mutant enzyme E188K, at pH 4.3 and 25°C

741485

1.11.1.19

0.097

-

at pH 4.0 and 30°C

742940

1.11.1.19

1.8

-

mutant enzyme A142V, at pH 5.5 and 25°C

741485

1.11.1.19

3.6

-

mutant enzyme E188K/A142V, at pH 5.5 and 25°C

741485

1.11.1.19

6

-

mutant enzyme E188K/A142V/H125Y, at pH 5.5 and 25°C

741485

1.11.1.19

60

-

at pH 4.5 and 30°C

741578

1.11.1.19

70.9

-

pH 3.0, temperature not specified in the publication

724033

1.11.1.19

89

-

manganese-independent peroxidase II, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C

710965

1.11.1.19

90

-

manganese-independent peroxidase I, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C

710965

1.11.1.19

120

-

wild type enzyme, at pH 3.0 and 25°C

741854

1.11.1.19

420

-

wild type enzyme, at pH 3.0 and 30°C

743731

1.11.2.1

2

-

in sodium phosphate-citrate buffer at pH 4.5 and 25°C

710926

1.11.2.1

68

-

mutant enzyme F12Y/A14V/R15GA21D/V57A/L67F/V75I/I248V/F311L, at pH 7.0, temperature not specified in the publication

742286

1.11.2.1

70

-

pH 5.5, 25°C

723912

1.11.2.1

108

-

at pH 7.0 in sodium phosphate/citrate buffer, at 25°C

710924

1.11.2.1

108

-

in sodium citrate buffer, pH 7.0, at 25°C

710955

1.11.2.1

142

-

mutant enzyme G241D/R257K, at pH 7.0, temperature not specified in the publication

742286

1.3.3.5

29

-

recombinant enzyme expressed in Escherichia coli strain BL21(DE3), pH 7.0, 37°C

745422

1.3.3.5

57

-

recombinant enzyme expressed in Escherichia coli strain BL21(DE3), pH 6.8, 37°C

745422

1.3.3.5

100

-

recombinant enzyme expressed in Escherichia coli strain Origami B(DE3), pH 7.0, 37°C

745422

1.10.3.2

66 entries

1.11.1.13

9 entries

1.11.1.16

31 entries

1.11.1.19

14 entries

1.11.2.1

6 entries

1.3.3.5

3 entries

K_M Value (179 results)

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Show KM Value (179 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.10.3.2

0.00086

-

Lac II, 70°C, pH 3.0

657149

1.10.3.2

0.00118

-

Lac I, 70°C, pH 3.0

657149

1.10.3.2

0.0052

-

pH 6.0

656736

1.10.3.2

0.0082

-

pH 8.0, 40°C

742104

1.10.3.2

0.0086

-

at 30°C in 100 mM sodium tartrate buffer (pH 4.5)

711500

1.10.3.2

0.011

-

pH 4.5, 25°C, recombinant wild-type enzyme

697913

1.10.3.2

0.012

-

pH 7.0, 30°C

655375

1.10.3.2

0.016

-

pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae

697913

1.10.3.2

0.0255

-

pH 4.5, 25°C

654297

1.10.3.2

0.026

-

pH 4.5, 25°C

673096

1.10.3.2

0.026

-

pH 5.0, 22-25°C

725731

1.10.3.2

0.027

-

recombinant wild-type enzyme, pH 5.0, temperature not specified in the publication

724013

1.10.3.2

0.035

-

pH 7.6, 37°C, mutant M502F

674926

1.10.3.2

0.038

-

-

396402

1.10.3.2

0.048

-

pH 5.0, 22°C

654307

1.10.3.2

0.053

-

at 22°C, pH not specified in the publication

712644

1.10.3.2

0.0567

-

pH 7.0

684645

1.10.3.2

0.06

-

pH 7.6, 37°C, wild-type enzyme

674926

1.10.3.2

0.0678

-

25°C, pH 6

684626

1.10.3.2

0.07

-

in McIlvaine buffer (pH 4.0), at 30°C

712084

1.10.3.2

0.08

-

-

396394

1.10.3.2

0.08

-

pH 4.5, 37°C

742638

1.10.3.2

0.084

-

pH 3.0, 25°C, laccase Lac-4.8

684624

1.10.3.2

0.088

-

pH 3.0, 25°C, laccase Lac-3.5

684624

1.10.3.2

0.09

-

-

689115

1.10.3.2

0.096

-

pH 6.0, 50°C

737487

1.10.3.2

0.11

-

pH 4.5

656847

1.10.3.2

0.14

-

pH 3.4, 30°C, recombinant mutant D206A

676943

1.10.3.2

0.145

-

pH 7.6, 37°C, mutant M502L

674926

1.10.3.2

0.16

-

pH and temperature not specified in the publication

741664

1.10.3.2

0.172

-

recombinant wild-type enzyme MmPPOA-695, pH 5.0, 25°C

746372

1.10.3.2

0.19

-

pH 3.4, 30°C, recombinant wild-type enzyme

676943

1.10.3.2

0.2

-

pH 4.8, 25°C

696911

1.10.3.2

0.2

-

pH and temperature not specified in the publication

743648

1.10.3.2

0.203

-

pH 4.0, 25°C

671552

1.10.3.2

0.216

-

pH 7, holoCotA

687819

1.10.3.2

0.227

-

pH 7.0, 25°C, wild-type CotA

696090

1.10.3.2

0.23

-

isoform POXC, pH 3.0-5.0, 25°C

711175

1.10.3.2

0.26

-

isoform POXA1b, pH 4.0-5.0, 25°C

711175

1.10.3.2

0.266

-

pH 4.0, 65°C

695839

1.10.3.2

0.277

-

recombinant enzyme, pH 3.0, 30°C

726411

1.10.3.2

0.293

-

recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C

746372

1.10.3.2

0.302

-

pH 4.0, 25°C

743078

1.10.3.2

0.324

-

recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication

724013

1.10.3.2

0.351

-

30°C, pH 3.0

656729

1.10.3.2

0.37

-

pH 4.0, 50°C

726416

1.10.3.2

0.38

-

pH 8.5, temperature not specified in the publication

742013

1.10.3.2

0.393

-

pH 3.0, 50°C

726424

1.10.3.2

0.41

-

21-23°C, pH not specified in the publication, wild-type enzyme

743727

1.10.3.2

0.426

-

-

688328

1.10.3.2

0.43

-

pH 5.3, 22°C, recombinant truncated mutant POXA1bDELTA16

697668

1.10.3.2

0.43

-

pH 5.3, 22°C, recombinant truncated mutant POXA1bDELTA4

697668

1.10.3.2

0.43

-

pH 7.0, 25°C

671403

1.10.3.2

0.44

-

pH 4.5, 37°C

743786

1.10.3.2

0.48

-

-

684533

1.10.3.2

0.48

-

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

684533

1.10.3.2

0.5

-

pH and temperature not specified in the publication

743103

1.10.3.2

0.503

-

pH 5.0, temperature not specified in the publication

725302

1.10.3.2

0.57

-

pH 4.6, 45°C

655487

1.10.3.2

0.57

-

pH 5.3, 22°C, recombinant wild-type enzyme

697668

1.10.3.2

0.576

-

pH 7.0, 25°C, mutant L386A

696090

1.10.3.2

0.602

-

pH and temperature not specified in the publication

743080

1.10.3.2

0.68

-

pH 7.0, 22°C, recombinant enzyme

724662

1.10.3.2

0.74

-

isoform POXA2, pH 6.5, 25°C

711175

1.10.3.2

0.84

-

pH 8.0, 85°C

743661

1.10.3.2

1.026

-

pH 5.5

671510

1.10.3.2

1.176

-

in 100 mM citrate buffer, pH 4.5, at 37°C

711502

1.10.3.2

1.24

-

pH 8.0, 70°C

743712

1.10.3.2

1.26

-

pH 5.3, 22°C, recombinant truncated mutant POXA1bD205R

697668

1.10.3.2

1.295

-

pH 9.0, 25°C, mutant I494A

696090

1.10.3.2

1.413

-

recombinant mutant enzyme MmPPOA-637, pH 5.0, 25°C

746372

1.10.3.2

1.5

2

pH 3.0, 37°C

743888

1.10.3.2

1.63

-

pH 3.4, 30°C, recombinant mutant D206N

676943

1.10.3.2

1.67

-

pH 7.4, 37°C

741713

1.10.3.2

1.83

-

21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)

743727

1.10.3.2

1.98

-

native wild-type enzyme, pH 5.0, 25°C

746372

1.10.3.2

2.095

-

pH 4, 30°C

743711

1.10.3.2

2.1

-

isoform POXA1w, pH 3.0-5.0, 25°C

711175

1.10.3.2

2.16

-

21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)

743727

1.10.3.2

3.28

-

pH 3.4, 30°C, recombinant mutant D206E

676943

1.10.3.2

3.295

-

recombinant His-tagged mutant enzyme MmPPOA-637, pH 5.0, 25°C

746372

1.10.3.2

6.82

-

pH 6.5, 30°C

742658

1.10.3.2

7.3

-

-

687338

1.10.3.2

8.8

-

25°C, isozyme POXA3b

655374

1.10.3.2

8.8

-

isoform POXA3b, pH 5.5, 25°C

711175

1.10.3.2

10

-

pH 3.0, 23°C

742173

1.10.3.2

14

-

25°C, isozyme POXA3a

655374

1.10.3.2

14

-

isoform POXA3a, pH 5.5, 25°C

711175

1.10.3.2

47

-

pH 3.0, 23°C

742173

1.10.3.2

56

-

pH 5.2, 45°C

673816

1.11.1.13

-999

-

apparent Km, 216 microM/l, chromatographic MnP form 2

698032

1.11.1.13

-999

-

apparent Km, 417 microM/l, chromatographic MnP form 1

698032

1.11.1.13

-999

-

apparent Km, 516 microM/l, chromatographic MnP form 3

698032

1.11.1.13

0.00366

-

Mn2+-dependent activity

439841

1.11.1.13

0.0066

-

Mn2+-dependent activity, PCH6

439850

1.11.1.13

0.00847

-

-

660488

1.11.1.13

0.01

-

0.1 mM Mn2+, 0.1 mM H2O2

439847

1.11.1.13

0.011

-

0.1 mM Mn2+, 0.1 mM H2O2

439844

1.11.1.13

0.011

-

isoform BOS2, at pH 5.0 and 30°C

439850

1.11.1.13

0.011

-

Mn2+-dependent activity, BOS2

439850

1.11.1.13

0.011

-

Mn2+-dependent activity, PCH5

439850

1.11.1.13

0.018

-

Mn2+-dependent activity, PCH4

439850

1.11.1.13

0.0195

-

isoform BOS1, at pH 5.0 and 30°C

439850

1.11.1.13

0.0195

-

Mn2+-dependent activity, BOS1

439850

1.11.1.13

0.0286

-

30°C, pH 4.5

660342

1.11.1.13

0.076

-

-

699016

1.11.1.13

0.076

-

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

0.092

-

MnP3

439840

1.11.1.13

0.106

-

isoform BOS2, at pH 5.0 and 30°C

439850

1.11.1.13

0.106

-

Mn2+-independent activity, BOS2

439850

1.11.1.13

0.121

-

isoform BOS1, at pH 5.0 and 30°C

439850

1.11.1.13

0.121

-

Mn2+-independent activity, BOS1

439850

1.11.1.13

0.1229

-

30°C, pH 4.5

686451

1.11.1.13

0.1445

-

Mn2+-independent activity

439841

1.11.1.13

0.16

0.25

0.1 mM H2O2

439847

1.11.1.13

0.3

-

-

439841

1.11.1.13

0.95

-

0.1 mM H2O2

439844

1.11.1.13

6.954

-

-

699016

1.11.1.13

6.954

-

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

699016

1.11.1.16

0.01

-

presence of Mn2+, isoenzyme MP-1, pH 5.0

439847

1.11.1.16

0.01

-

presence of Mn2+, isoenzyme MP-2, pH 5.0

439847

1.11.1.16

0.036

-

mutant P76G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.0379

-

presence of Mn2+, pH 5.0, 30°C

726530

1.11.1.16

0.038

-

mutant K176D, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.041

-

pH 4.5

394603

1.11.1.16

0.0474

-

absence of Mn2+, pH 5.0, 30°C

726530

1.11.1.16

0.058

-

mutant K215G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.063

-

presence of Mn2+, pH 7.0, temperature not specified in the publication

724882

1.11.1.16

0.065

-

mutant F142G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.066

-

mutant E140G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.078

-

mutant K215Q, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.078

-

wild-type, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.1

-

mutant K176G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.104

-

mutant E140G/P141G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.119

-

mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.14

-

at 30°C and pH 4.5

743092

1.11.1.16

0.155

-

mutant P141G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.16

-

absence of Mn2+, isoenzyme MP-1, pH 3.0

439847

1.11.1.16

0.189

-

mutant E140G/K176G, high efficiency site, pH 3.5, 25°C

725499

1.11.1.16

0.2

-

pH 3.0, isoenzyme PS1

665470

1.11.1.16

0.25

-

absence of Mn2+, isoenzyme MP-2, pH 3.0

439847

1.11.1.16

0.345

-

absence of Mn2+, pH not specified in the publication, temperature not specified in the publication

724882

1.11.1.16

1

-

pH 3.0, isoenzyme PS3

665470

1.11.1.16

2.38

-

mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

2.56

-

mutant K215Q, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

2.97

-

mutant E140G/K176G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

3.33

-

mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

6.5

-

mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication

724232

1.11.1.16

10.5

-

wild-type, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

16

-

mutant E140G/P141G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

32

-

at pH 3.0 and 25°C

741480

1.11.1.16

32

-

wild-type, pH 3.5, temperature not specified in the publication

724232

1.11.1.16

36.2

-

mutant K176G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

37.4

-

mutant E140G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

37.6

-

mutant W164S, low efficiency site, pH 3.5, 25°C

725499

1.11.1.16

76

-

mutant P141G, low efficiency site, pH 3.5, 25°C

725499

1.11.1.19

0.023

-

manganese-independent peroxidase II, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C

710965

1.11.1.19

0.023

-

mutant enzyme E188K/H125R, at pH 4.3 and 25°C

741485

1.11.1.19

0.027

-

manganese-independent peroxidase I, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C

710965

1.11.1.19

0.042

-

mutant enzyme E188K/A142V, at pH 5.5 and 25°C

741485

1.11.1.19

0.058

-

mutant enzyme E188K/A142V/H125Y, at pH 5.5 and 25°C

741485

1.11.1.19

0.06

-

mutant enzyme E188K, at pH 4.3 and 25°C

741485

1.11.1.19

0.07

-

wild type enzyme, at pH 4.3 and 25°C

741485

1.11.1.19

0.0726

-

pH 3.0, temperature not specified in the publication

724033

1.11.1.19

0.08

-

mutant enzyme H125R, at pH 4.3 and 25°C

741485

1.11.1.19

0.25

-

mutant enzyme A142V, at pH 5.5 and 25°C

741485

1.11.1.19

0.703

-

wild type enzyme, at pH 3.0 and 25°C

741854

1.11.1.19

1.227

-

at pH 4.5 and 30°C

741578

1.11.1.19

1.32

-

wild type enzyme, at pH 3.0 and 30°C

743731

1.11.1.19

1.46

-

at pH 4.0 and 30°C

742940

1.11.2.1

0.126

-

mutant enzyme F12Y/A14V/R15GA21D/V57A/L67F/V75I/I248V/F311L, at pH 7.0, temperature not specified in the publication

742286

1.11.2.1

0.133

-

pH 5.5, 25°C

723912

1.11.2.1

0.298

-

at pH 7.0 in sodium phosphate/citrate buffer, at 25°C

710924

1.11.2.1

0.298

-

in sodium citrate buffer, pH 7.0, at 25°C

710955

1.11.2.1

0.342

-

in sodium phosphate-citrate buffer at pH 4.5 and 25°C

710926

1.11.2.1

0.866

-

mutant enzyme G241D/R257K, at pH 7.0, temperature not specified in the publication

742286

1.3.3.5

0.216

-

recombinant enzyme expressed in Escherichia coli strain BL21(DE3), pH 7.0, 37°C

745422

1.3.3.5

0.774

-

recombinant enzyme expressed in Escherichia coli strain Origami B(DE3), pH 7.0, 37°C

745422

1.3.3.5

0.822

-

recombinant enzyme expressed in Escherichia coli strain BL21(DE3), pH 6.8, 37°C

745422

1.10.3.2

90 entries

1.11.1.13

29 entries

1.11.1.16

37 entries

1.11.1.19

14 entries

1.11.2.1

6 entries

1.3.3.5

3 entries

IC₅₀ Value (2 results)

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Show IC50 Value (2 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.4.3.4

0.0624

-

IC50: 0.0624 mM, monoamine oxidase A

672530

1.4.3.4

0.5

-

IC50: above 0.5 mM, monoamine oxidase B

672530

1.4.3.4

2 entries

References & Links

Literature References (155)

top print hide

Show Reference (155 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

394603

9624124

Characterization of a novel manganese peroxidase-lignin peroxidase hybrid isozyme produced by Bjerkandera species strain BOS55 in the absence of manganese

1998

Mester, T.; Field, J.A.

J. Biol. Chem.

273

15412-15417

396354

-

Soluble and immobilized laccase as catalysts for the transformation of substituted phenols

1986

Shuttleworth, K.L.; Bollag, J.M.

Enzyme Microb. Technol.

8

171-177

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

396396

11916665

Induction, isolation, and characterization of two laccases from the white rot basidiomycete Coriolopsis rigida

2002

Saparrat, M.C.N.; Guillen, F.; Arambarri, A.M.; Martinez, A.T.; Martinez, M.J.

Appl. Environ. Microbiol.

68

1534-1540

396400

12111146

Purification and characterisation of a novel laccase from the ascomycete Melanocarpus albomyces

2002

Kiiskinen, L.L.; Viikari, L.; Kruus, K.

Appl. Microbiol. Biotechnol.

59

198-204

396402

11488603

Characterization of a novel laccase produced by the wood-rotting fungus Phellinus ribis

2001

Min, K.L.; Kim, Y.H.; Kim, Y.W.; Jung, H.S.; Hah, Y.C.

Arch. Biochem. Biophys.

392

279-286

439784

8631329

Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum

1996

Fraaije, M.W.; Roubroeks, H.P.; Hagen, W.R.; Van Berkel, W.J.

Eur. J. Biochem.

235

192-198

439840

10729203

Manganese peroxidase isoenzymes produced by Pleurotus ostreatus grown on wood sadwust

2000

Giardina, P.; Palmieri, G.; Fontanella, B.; Rivieccio, V; Sannia, G.

Arch. Biochem. Biophys.

376

171-179

439841

12070683

Purification, characterization, and chemical modification of manganese peroxidase from Bjerkandera adusta UAMH 8258

2002

Wang, Y.; Vazquez-Duhalt, R.; Pickard, M.A.

Curr. Microbiol.

45

77-87

439844

9165096

Biochemical and molecular characterization of a manganese peroxidase isoenzyme from Pleurotus ostreatus

1997

Sarkar, S.; Martinez, A.T.; Martinez, M.J.

Biochim. Biophys. Acta

1339

23-30

439847

8647081

Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii

1996

Martinez, M.J.; Ruiz-Duenas, F.J.; Guillen, F.; Martinez, A.T.

Eur. J. Biochem.

237

424-432

439850

10682282

Different fungal manganese-oxidizing peroxidases: A comparison between Bjerkandera sp. and Phanerochaete chrysosporium

2000

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2008

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Molecular characterization of a novel DyP-type peroxidase from the cyanobacterium Anabaena sp. PCC 7120

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Characterization of a novel dye-decolorizing peroxidase (DyP)-type enzyme from Irpex lacteus and its application in enzymatic hydrolysis of wheat straw

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Biochemical characteristics of a textile dye degrading extracellular laccase from a Bacillus sp. ADR

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