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Ligand p-cresol

Basic Ligand Information

Molecular Structure

Related pathways

Pathway Source

Pathways

BRENDA

4-hydroxyphenylacetate degradation, aerobic toluene degradation, vitamin B1 metabolism

KEGG

Degradation of aromatic compounds, Microbial metabolism in diverse environments, Nitrotoluene degradation, Protein digestion and absorption, Toluene degradation

MetaCyc

4-methylphenol degradation to protocatechuate, 4-methylphenyl adenosylcobamide biosynthesis from adenosylcobinamide-GDP, L-tyrosine degradation IV (to 4-methylphenol), thiazole component of thiamine diphosphate biosynthesis I, toluene degradation II (aerobic) (via 4-methylcatechol), toluene degradation to 4-methylphenol more

Show all BRENDA pathways known for p-cresol

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Roles as Enzyme Ligand

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

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Show Natural Substrate (10 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.2

4-Methylphenol + O2 = ?

725137

-

1.14.14.20

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

736121

-

1.17.9.1

4-cresol + 2 acceptor + H2O = 4-hydroxybenzaldehyde + 2 reduced acceptor

687426

-

1.17.9.1

4-cresol + acceptor + H2O = 4-hydroxybenzaldehyde + reduced acceptor

437882, 658018, 658077, 658110, 658990

-

1.17.9.1

4-cresol + acceptor + H2O = 4-hydroxybenzyl alcohol + reduced acceptor

674335

-

1.17.9.1

4-cresol + azurin + H2O = 4-hydroxybenzaldehyde + reduced azurin

437869, 437871

-

1.17.9.1

4-cresol + nitrate + H2O = 4-hydroxybenzaldehyde + ?

288313

-

1.17.9.1

4-methylphenol + acceptor + H2O = 4-hydroxybenzaldehyde + reduced acceptor

715044

-

1.17.9.1

4-methylphenol + acceptor + H2O = 4-hydroxybenzaldehyde + reduced acceptor + H+

742539, 744141

-

1.17.9.1

7 entries

2.4.2.55

beta-nicotinate D-ribonucleotide + 4-cresol = nicotinate + 4-methylphenyl 5-phospho-alpha-D-ribofuranoside

723215

-

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

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Show Natural Product (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.7

3 toluene + 3 NADPH + 3 H+ + 3 O2 = 2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O

-

-

3.1.1.1

(E)-2-(2-(6-((4-acetoxybenzyl)oxy)-2,3-dihydro-1H-xanthen-4-yl)vinyl)-3,3-dimethyl-1-propyl-3H-indolium + H2O = (E)-2-(2-(6-hydroxy-2,3-dihydro-1H-xanthen-4-yl)vinyl)-3,3-dimethyl-1-propyl-3H-indol-1-ium + 4-methylphenol + acetate

-

-

3.1.6.1

p-cresol sulfate + H2O = p-cresol + sulfate

-

-

4.1.1.83

4-hydroxyphenylacetate + H+ = 4-cresol + CO2

-

-

4.1.99.19

L-tyrosine + S-adenosyl-L-methionine + NADPH = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + NADP+ + H+

-

-

Substrate in Enzyme-catalyzed Reactions (65 results)

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Show Substrate (65 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.38

4-Methylphenol + O2 = ?

10670

-

1.1.3.38

creosol + O2 = ?

656232

-

1.1.3.38

creosol + O2 = vanillin + ?

655761

-

1.1.3.38

creosol + O2 = vanillin + H2O

763609

-

1.1.3.38

p-cresol + O2 = ?

656232, 655540

-

1.1.3.38

5 entries

1.10.3.1

p-cresol + O2 = ?

701876, 745430

-

1.10.3.2

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

396358, 396341, 396394, 396352, 396357, 396354

-

1.10.3.2

p-cresol + O2 = ?

696857

-

1.10.3.2

p-cresol + O2 = ? + H2O

655627

-

1.11.1.11

p-cresol + cumene-hydroperoxide = 4a,9b-dihydro-8,9b-dimethyl-3(4H)-dibenzofuranone + 2,2'-dihydroxy-5,5'-dimethylbiphenyl + 1,1-dimethylbenzylalcohol + bis-(1-methyl-1-phenylethyl)peroxide

439877

-

1.11.1.11

p-cresol + H2O2 = 4a,9b-dihydro-8,9b-dimethyl-3(4H)-dibenzofuranone + 2,2'-dihydroxy-5,5'-dimethylbiphenyl + H2O

439877

-

1.10.3.2

3 entries

1.11.1.11

2 entries

1.11.1.7

4-methylphenol + H2O2 = ?

724400

-

1.11.2.6

4-cresol + H2O2 = 4-methylcatechol + H2O

726969

-

1.13.11.2

4-Methylphenol + O2 = ?

725137, 742377

-

1.13.11.3

4-cresol + O2 = ?

725655

-

1.14.12.11

4-cresol + NADH + H+ + O2 = (1R,2R)-6-methylcyclohexa-3,5-diene-1,2,3-triol + (2S)-4-methylcyclohexa-3,5-diene-1,1,2-triol + NAD+

743115

-

1.14.12.12

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

673725

-

1.14.13.166

4-cresol + NADH + H+ + O2 = 4-hydroxy-4-methyl-2,5-cyclohexadien-1-one + NAD+ + H2O

719711

-

1.14.13.236

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

740606

-

1.14.13.69

4-cresol + NADH + H+ + O2 = ?

671530

-

1.14.13.7

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

742574

-

1.14.13.7

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

742395

-

1.14.13.7

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

671421

-

1.14.13.7

4-methyl-phenol + O2 + NADPH = ?

438783, 438789, 438793, 438778, 394993

-

1.14.13.7

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

658619

-

1.14.13.7

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

658619, 659881

-

1.14.13.7

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

662875

-

1.14.14.20

4-methyl-phenol + O2 + NADPH = ?

438788

-

1.14.14.20

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

736121

-

1.14.13.7

7 entries

1.14.14.20

2 entries

1.14.14.9

p-cresol + ? = ?

438894

-

1.14.18.1

4-cresol + O2 = ?

675101, 676649, 765984, 766033, 766928

-

1.14.18.1

4-Methylphenol + O2 = ?

726870

-

1.14.18.1

p-cresol + O2 + AH2 = 4-methyl-o-quinone + H2O + A

685662

-

1.14.18.1

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

684232, 687231

-

1.14.18.1

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

687875

-

1.14.18.1

p-cresol + O2 = 4-methyl-o-quinone + H2O

674090

-

1.14.18.1

p-cresol + O2 = 4-methylpyrocatechol + H2O

636352, 636393, 636359, 636378, 636373, 687875

-

1.14.18.1

p-cresol + O2 = ?

712619, 636429, 767974

-

1.14.18.1

8 entries

1.14.99.15

4-methylphenol + NADH + H+ + O2 = 4-hydroxymethylphenol + NAD+ + H2O

766486

-

1.17.9.1

4-cresol + 2 acceptor + H2O = 4-hydroxybenzaldehyde + 2 reduced acceptor

687426

-

1.17.9.1

4-cresol + acceptor + H2O = 4-hydroxybenzaldehyde + reduced acceptor

437867, 437868, 437870, 437872, 437873, 437875, 437876, 437877, 437878, 437879, 437880, 437883, 437884, 437886, 437864, 437874, 437865, 437869, 437871, 288313, 437866, 437882, 437885, 658018, 658077, 658110, 658990, 726788, 674335

-

1.17.9.1

4-cresol + acceptor + H2O = 4-hydroxybenzyl alcohol + reduced acceptor

674335

-

1.17.9.1

4-cresol + azurin + H2O = 4-hydroxybenzaldehyde + reduced azurin

437869, 437871

-

1.17.9.1

4-cresol + Fe3+ + H2O = 4-hydroxybenzaldehyde + Fe2+

687426

-

1.17.9.1

4-cresol + ferricenium + H2O = 4-hydroxybenzyl alcohol + ferrocenium

674335

-

1.17.9.1

4-cresol + NAD(P)+ + H2O = 4-hydroxybenzyl alcohol + NAD(P)H

674335

-

1.17.9.1

4-cresol + nitrate + H2O = 4-hydroxybenzaldehyde + ?

288313

-

1.17.9.1

4-cresol + phenazine methosulfate + H2O = 4-hydroxybenzyl alcohol + reduced phenazine methosulfate

674335, 437874

-

1.17.9.1

4-methylphenol + acceptor + H2O = 4-hydroxybenzaldehyde + reduced acceptor

715044

-

1.17.9.1

4-methylphenol + acceptor + H2O = 4-hydroxybenzaldehyde + reduced acceptor + H+

742539, 744141

-

1.17.9.1

4-methylphenol + phenazine methosulfate + H2O = 4-hydroxybenzaldehyde + reduced phenazine methosulfate + H+

744141

-

1.17.9.1

12 entries

2.1.1.25

S-adenosyl-L-methionine + p-methylphenol = S-adenosyl-L-homocysteine + p-methylanisole

485240

-

2.4.1.17

p-cresol + UDP-glucuronate = UDP + p-cresyl beta-D-glucuronide

779411

-

2.4.1.218

UDP-glucose + 4-methylphenol = UDP + (4-methylphenyl)-beta-D-glucopyranoside

393094

-

2.4.2.21

p-cresol + beta-nicotinate D-ribonucleotide = nicotinate + 4-hydroxyphenyl alpha-D-ribose 5-phosphate

721677, 723215

1JHU, 3D-view

2.4.2.21

p-cresol + beta-nicotinate D-ribonucleotide = nicotinate + 4-hydroxyphenyl alpha-D-ribose 5-phosphate

721677, 723215

1JHV, 3D-view

2.4.2.21

p-cresol + beta-nicotinate D-ribonucleotide = nicotinate + 4-hydroxyphenyl alpha-D-ribose 5-phosphate

721677, 723215

4HDM, 3D-view

2.4.2.21

p-cresol + beta-nicotinate D-ribonucleotide = nicotinate + 4-hydroxyphenyl alpha-D-ribose 5-phosphate

721677, 723215

4KQJ, 3D-view

2.4.2.21

p-cresol + beta-nicotinate D-ribonucleotide = nicotinate + 4-hydroxyphenyl alpha-D-ribose 5-phosphate

721677, 723215

4KQK, 3D-view

2.4.2.21

5 entries

2.4.2.55

beta-nicotinate D-ribonucleotide + 4-cresol = nicotinate + 4-methylphenyl 5-phospho-alpha-D-ribofuranoside

723215

-

2.8.2.1

3'-phosphoadenylylsulfate + 4-methylphenol = adenosine 3',5'-bisphosphate + 4-methylphenyl sulfate

645642, 645671, 645677

-

2.8.2.2

3'-phosphoadenylylsulfate + p-cresol = adenosine 3',5'-bisphosphate + p-cresol sulfate

739274

-

2.8.2.22

4-nitrophenyl sulfate + 4-cresol = 4-nitrophenol + 4-cresol sulfate

723897

-

2.8.2.9

3'-phosphoadenylylsulfate + 4-methylphenol = adenosine 3',5'-bisphosphate + 4-methylphenyl sulfate

644817

-

4.1.99.11

p-cresol + fumarate = (4-hydroxybenzyl)succinic acid

663790

-

Product in Enzyme-catalyzed Reactions (26 results)

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Show Product (26 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.2.1

toluene + H2O2 = 4-cresol + 2-cresol + methyl 4-benzoquinone + H2O

-

-

1.11.2.1

toluene + H2O2 = 4-cresol + 2-cresol + methyl-4-benzoquinone + H2O

-

-

1.11.2.1

toluene + H2O2 = benzyl alcohol + benzaldehyde + benzoic acid + 2-cresol + 4-cresol + methylhydroquinone + H2O

-

-

1.11.2.1

toluene + H2O2 = o-cresol + p-cresol + H2O

-

-

1.14.13.236

toluene + NADH + H+ + O2 = 4-methylphenol + NAD+ + H2O

-

-

1.14.13.236

toluene + NADH + H+ + O2 = p-cresol + NAD+ + H2O

-

-

1.11.2.1

4 entries

1.14.13.236

2 entries

1.14.13.25

toluene + NAD(P)H + H+ + O2 = benzyl alcohol + p-cresol + NAD(P)+ + H2O

438920

-

1.14.13.7

3 toluene + 3 NADPH + 3 H+ + 3 O2 = 2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O

-

-

1.14.13.7

toluene + NADPH + H+ + O2 = o-cresol + m-cresol + p-cresol + NADP+

-

-

1.14.13.7

2 entries

1.7.1.17

Reactive black 5 + 2 NADH + 2 H+ = n-hydroxy-benzenamine + dimethyl phthalate + phenylethyl alcohol + 4-methylphenol + 3-(methylthio)propanoic acid methyl ester + 2 NAD+

-

-

3.1.1.1

(E)-2-(2-(6-((4-acetoxybenzyl)oxy)-2,3-dihydro-1H-xanthen-4-yl)vinyl)-3,3-dimethyl-1-propyl-3H-indolium + H2O = (E)-2-(2-(6-hydroxy-2,3-dihydro-1H-xanthen-4-yl)vinyl)-3,3-dimethyl-1-propyl-3H-indol-1-ium + 4-methylphenol + acetate

-

-

3.1.1.1

p-tolyl octanoate + H2O = p-toluol + octanoate

653767

-

3.1.1.2

4-methylphenyl acetate + H2O = 4-methylphenol + acetate

-

-

3.1.1.2

9-(4-methylphenoxycarbonyl)-10-methylacridinium triflate + H2O = 4-methylphenol + 10-methylacridinium trifluoromethanesulfonate

-

-

3.1.6.1

p-cresol sulfate + H2O = p-cresol + sulfate

-

-

3.1.6.1

p-cresyl sulfate + H2O = p-cresol + sulfate

-

-

3.1.1.1

2 entries

3.1.1.2

2 entries

3.1.6.1

2 entries

3.2.1.22

p-cresyl alpha-D-galactoside + H2O = p-cresol + D-galactose

-

-

3.2.1.37

p-methylphenyl beta-D-xyloside + H2O = p-methylphenol + beta-D-xylose

136305, 136304

-

3.4.22.7

N-methanesulfonylglycine 4-methylphenyl ester + H2O = N-methanesulfonylglycine + 4-methylphenol

-

-

3.5.1.3

p-methylphenyl glutarate + hydroxylamine = glutaramate + 4-methylphenol

-

-

4.1.1.119

4-hydroxyphenylacetate = p-cresol + CO2

-

-

4.1.1.83

4-hydroxyphenylacetate + H+ = 4-cresol + CO2

-

-

4.1.1.83

4-hydroxyphenylacetate = 4-cresol + CO2

-

-

4.1.1.83

(4-hydroxyphenyl)acetate + H+ = 4-methylphenol + CO2

-

-

4.1.99.19

L-tyrosine + S-adenosyl-L-methionine + NADPH = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + NADP+ + H+

-

-

4.1.99.19

L-tyrosine + S-adenosyl-L-methionine + reduced acceptor = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + acceptor + 2 H+

-

-

4.1.1.83

3 entries

4.1.99.19

2 entries

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.19.1

as well as other phenols, interact with desaturase system causing a stimulation of oxidation of reduced cytochrome b5

437653

-

Inhibitor in Enzyme-catalyzed Reactions (10 results)

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Show Inhibitors (10 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.38

-

10672

-

1.10.3.3

-

439935

-

1.13.11.1

8% inhibition at 0.1 mM, 27.5% at 0.3 mM

723960

-

1.14.17.1

-

438615

-

1.14.17.1

mechanism of inhibition

438614

-

1.14.18.1

-

636373

-

1.14.18.1

competitive to catechol

636372

-

1.14.17.1

2 entries

1.14.18.1

2 entries

2.4.1.1

5 mM, 67% inhibition

488284

-

3.1.6.1

-

135531

-

4.3.1.24

-

775637

-

3D Structure of Enzyme-Ligand-Complex (PDB) (44 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (44 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.14.14.1

7Y0P, 3D-view

1.17.99.1

1DIQ, 3D-view

1.5.1.30

5K1Q, 3D-view

1.6.2.4

7Y0P, 3D-view

2.4.2.21

1JHU, 3D-view

2.4.2.21

1JHV, 3D-view

2.4.2.21

4HDM, 3D-view

2.4.2.21

4KQJ, 3D-view

2.4.2.21

4KQK, 3D-view

2.4.2.21

1JHU, 3D-view

2.4.2.21

1JHV, 3D-view

2.4.2.21

4HDM, 3D-view

2.4.2.21

4KQJ, 3D-view

2.4.2.21

4KQK, 3D-view

2.4.2.21

1JHU, 3D-view

2.4.2.21

1JHV, 3D-view

2.4.2.21

4HDM, 3D-view

2.4.2.21

4KQJ, 3D-view

2.4.2.21

4KQK, 3D-view

2.4.2.21

1JHU, 3D-view

2.4.2.21

1JHV, 3D-view

2.4.2.21

4HDM, 3D-view

2.4.2.21

4KQJ, 3D-view

2.4.2.21

4KQK, 3D-view

2.4.2.21

1JHU, 3D-view

2.4.2.21

1JHV, 3D-view

2.4.2.21

4HDM, 3D-view

2.4.2.21

4KQJ, 3D-view

2.4.2.21

4KQK, 3D-view

2.4.2.21

1JHU, 3D-view

2.4.2.21

1JHV, 3D-view

2.4.2.21

4HDM, 3D-view

2.4.2.21

4KQJ, 3D-view

2.4.2.21

4KQK, 3D-view

2.4.2.21

1JHU, 3D-view

2.4.2.21

1JHV, 3D-view

2.4.2.21

4HDM, 3D-view

2.4.2.21

4KQJ, 3D-view

2.4.2.21

4KQK, 3D-view

2.4.2.21

1JHU, 3D-view

2.4.2.21

1JHV, 3D-view

2.4.2.21

4HDM, 3D-view

2.4.2.21

4KQJ, 3D-view

2.4.2.21

4KQK, 3D-view

2.4.2.21

40 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (38 results)

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Show Turnover Number (38 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.3.38

0.0002

-

pH 7.5, 25°C, mutant enzyme D170E

655540

1.1.3.38

0.003

-

pH 8, 25°C, wild-type enzyme

656232

1.1.3.38

0.005

-

-

10670

1.1.3.38

0.005

-

pH 10, 25°C, wild-type enzyme

656232

1.1.3.38

0.01

-

pH 8, 25°C, mutant enzyme T505S

656232

1.1.3.38

0.013

-

pH 10, 25°C, mutant enzyme F454Y

656232

1.1.3.38

0.013

-

pH 8, 25°C, wild-type enzyme

656232

1.1.3.38

0.015

-

pH 10, 25°C, mutant enzyme A429V

656232

1.1.3.38

0.015

-

pH 8, 25°C, mutant enzyme I237T/M437L

656232

1.1.3.38

0.016

-

pH 8, 25°C, mutant enzyme E502G

656232

1.1.3.38

0.017

-

pH 10, 25°C, mutant enzyme T505S

656232

1.1.3.38

0.017

-

pH 8, 25°C, mutant enzyme F454Y

656232

1.1.3.38

0.018

-

pH 8, 25°C, mutant enzyme A429V

656232

1.1.3.38

0.019

-

pH 10, 25°C, mutant enzyme F93Y/P189S/I238T

656232

1.1.3.38

0.02

-

pH 10, 25°C, mutant enzyme E502G

656232

1.1.3.38

0.02

-

pH 10, 25°C, mutant enzyme I238T

656232

1.1.3.38

0.02

-

pH 7.5, 25°C, wild-type enzyme

656232

1.1.3.38

0.021

-

pH 10, 25°C, mutant enzyme I237T/M437L

656232

1.1.3.38

0.022

-

pH 8, 25°C, mutant enzyme I238T

656232

1.1.3.38

0.07

-

pH 10, 25°C, mutant enzyme I238T

656232

1.1.3.38

0.07

-

pH 7.4, 25°C

655761

1.1.3.38

0.09

-

pH 10, 25°C, mutant enzyme E502G

656232

1.1.3.38

0.1

-

pH 10, 25°C, mutant enzyme F454Y

656232

1.1.3.38

0.1

-

pH 10, 25°C, mutant enzyme T505S

656232

1.1.3.38

0.1

-

pH 7.5, 25°C, mutant enzyme E502G

656232

1.1.3.38

0.12

-

pH 7.5, 25°C, mutant enzyme T505S

656232

1.1.3.38

0.14

-

pH 7.5, 25°C, mutant enzyme F454Y

656232

1.1.3.38

0.17

-

pH 7.5, 25°C, mutant enzyme I238T

656232

1.1.3.38

28 entries

1.14.13.7

0.77

-

25°C, recombinant enzyme

671421

1.14.18.1

14.76

-

pH and temperature not specified in the publication

726870

1.14.18.1

107

-

-

685662

1.17.9.1

2.4

-

R474K mutant enzyme, pH 7, 25°C

658077

1.17.9.1

3.8

-

Y384F mutant enzyme, pH 7, 25°C

658018

1.17.9.1

20

-

2’-deoxy-FAD cofactor, pH 7, 25°C

658990

1.17.9.1

121

-

FAD cofactor, pH 7, 25°C

658990

1.17.9.1

121

-

native enzyme, pH 7, 25°C

658018, 658077

1.14.18.1

2 entries

1.17.9.1

5 entries

2.8.2.2

0.000128

-

at pH 7.5 and 30°C

739274

2.8.2.9

0.02

-

pH 5.5, 37°C

644817

K_M Value (43 results)

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Show KM Value (43 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.3.38

0.001

-

pH 10, 25°C, mutant enzyme I238T

656232

1.1.3.38

0.001

-

pH 10, 25°C, mutant enzyme T505S

656232

1.1.3.38

0.002

-

pH 10, 25°C, mutant enzyme F454Y

656232

1.1.3.38

0.002

-

pH 10, 25°C, wild-type enzyme

656232

1.1.3.38

0.013

-

pH 7.5, 25°C, mutant enzyme F454Y

656232

1.1.3.38

0.02

-

pH 7.5, 25°C, wild-type enzyme

656232

1.1.3.38

0.027

-

pH 7.5, 25°C, mutant enzyme E502G

656232

1.1.3.38

0.031

-

-

10670

1.1.3.38

0.031

-

pH 7.5, 25°C, mutant enzyme T505S

656232

1.1.3.38

0.031

-

pH 7.5, 25°C, wild-type enzyme

656232

1.1.3.38

0.041

-

pH 7.5, 25°C, mutant enzyme I238T

656232

1.1.3.38

0.05

-

pH 7.4, 25°C

655761

1.1.3.38

12 entries

1.10.3.2

2.2

-

-

396394

1.13.11.3

0.014

-

pH 7.5, 38°C

725655

1.14.13.7

0.0006

-

25°C, recombinant enzyme

671421

1.14.18.1

0.001

-

isoenzyme A3

636429

1.14.18.1

0.001

-

isoenzyme B1

636429

1.14.18.1

0.001

-

isoenzyme B2

636429

1.14.18.1

0.001

-

isoenzyme B3

636429

1.14.18.1

0.001

-

isozyme A3, B1, B2, or B3, at pH 6,0 and 30°C

636429

1.14.18.1

0.002

-

isoenzyme A1

636429

1.14.18.1

0.002

-

isozyme A1, at pH 6.0 and 30°C

636429

1.14.18.1

0.003

-

isoenzyme A2

636429

1.14.18.1

0.003

-

isozyme A2, at pH 6.0 and 30°C

636429

1.14.18.1

0.38

-

pH and temperature not specified in the publication

726870

1.14.18.1

0.5

-

-

636359

1.14.18.1

0.65

-

-

636393

1.14.18.1

2

-

-

636352

1.14.18.1

2.2

-

pH 7.0, 25°C

674090

1.14.18.1

30.6

-

-

685662

1.14.18.1

130

-

detected in dormant saffron corms

684232

1.17.9.1

0.0017

-

-

687426

1.17.9.1

0.0036

-

hydroxylase B

437880

1.17.9.1

0.0073

-

-

437864

1.17.9.1

0.015

-

hydroxylase B, 4-hydroxybenzyl alcohol

437880

1.17.9.1

0.016

-

hydroxylase A

437880

1.17.9.1

0.11

-

-

288313

2.4.1.17

0.0503

-

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

779411

2.4.1.17

0.0584

-

S50 value, n is 1.6, pH not specified in the publication, temperature not specified in the publication

779411

2.8.2.1

2.2

-

isoenzyme II, pH 6.5, 37°C

645642

2.8.2.1

2.9

-

isoenzyme I, pH 6.5, 37°C

645642

1.14.18.1

16 entries

1.17.9.1

6 entries

2.4.1.17

2 entries

2.8.2.1

2 entries

2.8.2.2

0.494

-

at pH 7.5 and 30°C

739274

2.8.2.9

1.2

-

pH 5.5, 37°C

644817

K_i Value (3 results)

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Show KI Value (3 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.10.3.3

18

-

at pH 7.0

439935

1.14.18.1

0.88

-

competitive vs. catechol

636372

1.14.18.1

0.9

-

uncompetitive vs. pyrogallol

636372

1.14.18.1

2 entries

References & Links

Literature References (124)

top print hide

Show Reference (124 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

10670

9654070

Kinetic mechanism of vanillyl-alcohol oxidase with short-chain 4-alkylphenols

1998

Fraaije, M.W.; van der Heuvel, R.H.H.; Roelofs, J.C.A.A.; van Berkel, W.J.H.

Eur. J. Biochem.

253

712-719

10672

9261083

Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity

1997

Mattevi, A.; Fraaije, M.W.; Mozzarelli, A.; Olivi, L.; Coda, A.; van Berkel, W.J.H.

Structure

5

907-920

135531

7744061

Purification and characterization of the arylsulfatase synthesized by Pseudomonas aeruginosa PAO during growth in sulfate-free medium and cloning of the arylsulfatase gene (atsA)

1995

Beil, S.; Kehrli, H.; James, P.; Staudenmann, W.; Cook, A.M.; Leisinger, T.; Kertesz, M.A.

Eur. J. Biochem.

229

385-294

136304

-

Purification and some properties of beta-xylosidase from Trichoderma viride

1984

Matsuo, M.; Yasui, T.

Agric. Biol. Chem.

48

1845-1852

136305

-

Purification and some properties of beta-xylosidase from Eimericella nidulans

1984

Matsuo, M.; Yasui, T.

Agric. Biol. Chem.

48

1853-1860

288313

2722739

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

1989

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

J. Bacteriol.

171

2956-2962

393094

11937332

Arbutin synthase, a novel member of the NRD1beta glycosyltransferase family, is a unique multifunctional enzyme converting various natural products and xenobiotics

2002

Hefner, T.; Arend, J.; Warzecha, H.; Siems, K.; Stöckigt, J.

Bioorg. Med. Chem.

10

1731-1741

394993

3783431

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

1986

Krug, M.; Straube, G.

J. Basic Microbiol.

26

271-281

396341

-

Polyphenol oxidases in plants - recent progress

1987

Mayer, A.M.

Phytochemistry

26

11-20

396352

-

Purification and properties of two laccase isoenzymes produced by Botrytis cinerea

1987

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

Appl. Biochem. Biotechnol.

15

213-225

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

396357

-

Molecular properties of extracellular Botrytis cinerea laccase

1984

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

Phytochemistry

23

2713-2717

396358

6847630

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

1983

Bligny, R.; Douce, R.

Biochem. J.

209

489-496

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

437653

6105888

Inhibition of the microsomal stearoyl coenyme A desaturation by divalent copper and its chelates

1980

Sreekrishna, K.; Joshi, V.C.

Biochim. Biophys. Acta

619

267-273

437864

588247

The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida

1977

Hopper, D.J.; Taylor, D.G.

Biochem. J.

167

155-162

437865

736904

Incorporation of [18O]water in the formation of p-hydroxybenzyl alcohol by the p-cresol methylhydroxylase from Pseudomonas putida

1978

Hopper, D.J.

Biochem. J.

175

345-347

437866

7391034

8 alpha-O-Tyrosyl-FAD: a new form of covalently bound flavin from p-cresol methylhydroxylase

1980

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

J. Biol. Chem.

255

6553-6555

437867

7248267

8 alpha-(O-Tyrosyl)flavin adenine dinucleotide, the prosthetic group of bacterial p-cresol methylhydroxylase

1981

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

Biochemistry

20

3068-3075

437868

6309572

Redox potential of the cytochrome c in the flavocytochrome p-cresol methylhydroxylase

1983

Hopper, D.J.

FEBS Lett.

161

100-102

437869

-

Azurin from Pseudomonas putida: an electron acceptor for p-cresol methylhydroxylase

1984

Causer, M.J.; Hopper, D.J.; McIntire, W.S.; Singer, T.P.

Biochem. Soc. Trans.

12

1131-1132

437870

6083780

Stereochemistry of 1-(4-hydroxyphenyl)ethanol produced by hydroxylation of 4-ethylphenol by p-cresol methylhydroxylase

1984

McIntire, W.; Hopper, D.J.; Craig, J.C.; Everhart, E.T.; Webster, R.V.; Causer, M.J.; Singer, T.P.

Biochem. J.

224

617-621

437871

3920077

Periplasmic location of p-cresol methylhydroxylase in Pseudomonas putida

1985

Hopper, D.J.; Jones, M.R.; Causer, M.J.

FEBS Lett.

182

485-488

437872

2990445

Laser-flash-photolysis studies of p-cresol methylhydroxylase. Electron-transfer properties of the flavin and haem components

1985

Bhattacharyya, A.; Tollin, G.; McIntire, W.; Singer, T.P.

Biochem. J.

228

337-345

437873

4020868

Preliminary X-ray study of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida N.C.I.B. 9869

1985

Shamala, N.; Lim, L.W.; Mathews, F.S.

J. Mol. Biol.

183

517-518

437874

2990444

p-Cresol methylhydroxylase. assay and general properties

1985

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

Biochem. J.

228

325-335

437875

4074695

Resolution of the flavocytochrome p-cresol methylhydroxylase into subunits and reconstitution of the enzyme

1985

Koerber, S.C.; McIntire, W.; Bohmont, C.; Singer, T.P.

Biochemistry

24

5276-5280

437876

7929007

Cloning, sequencing, and expression of the structural genes for the cytochrome and flavoprotein subunits of p-cresol methylhydroxylase from two strains of Pseudomonas putida

1994

Kim, J.; Fuller, J.H.; Cecchini, G.; McIntire, W.S.

J. Bacteriol.

176

6349-6361

437877

3460061

Structure of an intermolecular electron-transfer complex: p-cresol methylhydroxylase at 6.0-A resolution

1986

Shamala, N.; Lim, L.W.; Mathews, F.S.; McIntire, W.; Singer, T.P.; Hopper, D.J.

Proc. Natl. Acad. Sci. USA

83

4626-4630

437878

3790500

Amino acid and sequence analysis of the cytochrome and flavoprotein subunits of p-cresol methylhydroxylase

1986

McIntire, W.; Singer, T.P.; Smith, A.J.; Mathews, F.S.

Biochemistry

25

5975-5981

437879

3651440

Steady-state and stopped-flow kinetic measurements of the primary deuterium isotope effect in the reaction catalyzed by p-cresol methylhydroxylase

1987

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

Biochemistry

26

4107-4117

437880

743215

p-Cresol and 3,5-xylenol methylhydroxylases in Pseudomonas putida N.C.I.B. 9896

1978

Keat, M.J.; Hopper, D.J.

Biochem. J.

175

649-658

437882

10623531

Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: Gated substrate entry and proton relays support the proposed catalytic mechanism

2000

Cunane, L.M.; Chen, Z.W.; Shamala, N.; Mathews, F.S.; Cronin, C.N.; McIntire, W.S.

J. Mol. Biol.

295

357-374

437883

10600124

Properties of p-cresol methylhydroxylase flavoprotein overproduced by Escherichia coli

1999

Engst, S.; Kuusk, V.; Efimov, I.; Cronin, C.N.; McIntire, W.S.

Biochemistry

38

16620-16628

437884

8537385

The cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit of p-cresol methylhydroxylase

1995

Kim, J.; Fuller, J.H.; Kuusk, V.; Cunane, L.; Chen, Z.; Mathews, F.S.; McIntire, W.S.

J. Biol. Chem.

270

31202-31209

437885

11329284

Effects of noncovalent and covalent FAD binding on the redox and catalytic properties of p-cresol methylhydroxylase

2001

Efimov, I.; Cronin, C.N.; McIntire, W.S.

Biochemistry

40

2155-2166

437886

10833393

Heterologous expression in Pseudomonas aeruginosa and purification of the 9.2-kDa c-type cytochrome subunit of p-cresol methylhydroxylase

2000

Cronin, C.N.; McIntire, W.S.

Protein Expr. Purif.

19

74-83

438614

3242615

Inactivation of dopamine beta-hydroxylase by p-cresol: isolation and characterization of covalently modified active site peptides

1988

DeWolf, W.E.; Carr, S.A.; Varrichio, A.; Goodhart, P.J.; Mentzer, M.A.; Roberts, G.D.; Southan, C.; Dolle, R.E.; Kruse, L.I.

Biochemistry

27

9093-9101

438615

3801416

Design and kinetic characterization of multisubstrate inhibitors of dopamine beta-hydroxylase

1986

Kruse, L.I.; DeWolf, W.E.; Chambers, P.A.; Goodhart, P.J.

Biochemistry

25

7271-7278

438778

14478080

Phenol hydroxylase

1962

Nakagawa, H.; Takeda, Y.

Biochim. Biophys. Acta

62

423-426

438783

569150

Phenol hydroxylase from yeast. Reaction with phenol derivatives

1978

Neujahr, H.Y.; Kjellen, K.G.

J. Biol. Chem.

253

8835-8841

438788

3430338

Phenol hydroxylase from Rhodococcus sp. P 1

1987

Straube, G.

J. Basic Microbiol.

27

229-232

438789

3606624

In situ and in vitro kinetics of phenol hydroxylase

1987

Mörtberg, M.; Neujahr, H.Y.

Biochem. Biophys. Res. Commun.

146

41-46

438793

1429434

Phenol hydroxylase from Trichosporon cutaneum: gene cloning, sequence analysis, and functional expression in Escherichia coli

1992

Kaelin, M.; Neujahr, H.Y.; Weissmahr, R.N.; Sejlitz, T.; Joehl, R.; Fiechter, A.; Reiser, J.

J. Bacteriol.

174

7112-7120

438894

8458860

Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range

1993

Prieto, M.A.; Perez-Aranda, A.; Garcia, J.L.

J. Bacteriol.

175

2162-2167

438920

411486

The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds

1977

Colby, J.; Stirling, D.I.; Dalton, H.

Biochem. J.

165

395-402

439877

11356136

Engineering the active site of ascorbate peroxidase

2001

Lloyd Raven, E.; Celik, A.; Cullis, P.M.; Sangar, R.; Sutcliffe, M.J.

Biochem. Soc. Trans.

29

105-111

439935

9125505

Inhibition of ascorbate oxidase by phenolic compounds. Enzymatic and spectroscopic studies

1997

Gaspard, S.; Monzani, E.; Casella, L.; Gullotti, M.; Maritano, S.; Marchesini, A.

Biochemistry

36

4852-4859

485240

5657870

Phenol-O-methyltransferase

1968

Axelrod, J.; Daly, J.

Biochim. Biophys. Acta

159

472-478

488284

-

Aromatic compounds as allosteric inhibitors of glycogen phosphorylase b

1974

Soman, G.; Philip, G.

Biochim. Biophys. Acta

358

359-362

636352

-

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

1989

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

Phytochemistry

28

1321-1325

636359

-

Characterization of catecholase and cresolase activities of monastrell grape polyphenol oxidase

1988

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

Phytochemistry

27

319-321

636372

-

Properties of polyphenol oxidase from tubers of the yam Dioscora bulbifera

1982

Anosike, E.O.; Ayaebene, A.O.

Phytochemistry

21

1889-1893

636373

-

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

1981

Anosike, E.O.; Ayaebene, A.O.

Phytochemistry

20

2625-2628

636378

-

Partial purification and characterization of the soluble polyphenol oxidases from suspension cultures of Papaver somniferum

1984

Hsu, A.F.; Kalan, E.B.; Bills, D.D.

Plant Sci. Lett.

34

315-322

636393

-

Monophenolase activity of avocado polyphenol oxidase

1980

Kahn, V.; Pomerantz, S.H.

Phytochemistry

19

379-385

636429

8987542

Purification and properties of tyrosinase isozymes from the gill of Lentinus edodes fruiting body

1996

Kanda, K.; Sato, T.; Ishii, S.; Enei, H.; Ejiri, S.

Biosci. Biotechnol. Biochem.

60

1273-1278

644817

6946725

Aryl sulfotransferase IV from rat liver

1981

Sekura, R.D.; Jakoby, W.B.

Arch. Biochem. Biophys.

211

352-359

645642

447677

Phenol sulfotransferases

1979

Sekura, R.D.; Jakoby, W.B.

J. Biol. Chem.

254

5658-5663

645671

10608851

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

1999

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

J. Biol. Chem.

274

37862-37868

645677

10617600

Sulfation of 'estrogenic' alkylphenols and 17beta-estradiol by human platelet phenol sulfotransferases

2000

Harris, R.M.; Waring, R.H.; Kirk, C.J.; Hughes, P.J.

J. Biol. Chem.

275

159-166

653767

12880765

Cloning, heterologous expression, renaturation, and characterization of a cold-adapted esterase with unique primary structure from a psychrotroph Pseudomonas sp. strain B11-1

2003

Suzuki, T.; Nakayama, T.; Choo, D.W.; Hirano, Y.; Kurihara, T.; Nishino, T.; Esaki, N.

Protein Expr. Purif.

30

171-178

655540

10996306

Direction of the reactivity of vanillyl-alcohol oxidase with 4-alkylphenols

2000

van den Heuvel, R.H.; Fraaije, M.W.; van Berkel, W.J.

FEBS Lett.

481

109-112

655627

14568157

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

2003

Iyer, G.; Chattoo, B.B.

FEMS Microbiol. Lett.

227

121-126

655761

11409992

Enzymatic synthesis of vanillin

2001

van den Heuvel, R.H.; Fraaije, M.W.; Laane, C.; van Berkel, W.J.

J. Agric. Food Chem.

49

2954-2958

656232

15169773

Laboratory-evolved vanillyl-alcohol oxidase produces natural vanillin

2004

van den Heuvel, R.H.; van den Berg, W.A.; Rovida, S.; van Berkel, W.J.

J. Biol. Chem.

279

33492-33500

658018

15301551

A study of the spectral and redox properties and covalent flavinylation of the flavoprotein component of p-cresol methylhydroxylase reconstituted with FAD analogues

2004

Efimov, I.; McIntire, W.S.

Biochemistry

43

10532-10546

658077

15147198

Insight into covalent flavinylation and catalysis from redox, spectral, and kinetic analyses of the R474K mutant of the flavoprotein subunit of p-cresol methylhydroxylase

2004

Efimov, I.; Cronin, C.N.; Bergmann, D.J.; Kuusk, V.; McIntire, W.S.

Biochemistry

43

6138-6148

658110

15723539

p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit

2005

Cunane, L.M.; Chen, Z.W.; McIntire, W.S.; Mathews, F.S.

Biochemistry

44

2963-2973

658619

12752444

The oxygenase component of phenol hydroxylase from Acinetobacter radioresistens S13

2003

Divari, S.; Valetti, F.; Caposio, P.; Pessione, E.; Cavaletto, M.; Griva, E.; Gribaudo, G.; Gilardi, G.; Giunta, C.

Eur. J. Biochem.

270

2244-2253

658990

15643899

Relationship between charge-transfer interactions, redox potentials, and catalysis for different forms of the flavoprotein component of p-cresol methylhydroxylase

2005

Efimov, I.; McIntire, W.S.

J. Am. Chem. Soc.

127

732-741

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

662875

10589844

Characterization of a high-affinity phenol hydroxylase from Comamonas testosteroni R5 by gene cloning, and expression in Pseudomonas aeruginosa PAO1c

1999

Teramoto, M.; Futamata, H.; Harayama, S.; Watanabe, K.

Mol. Gen. Genet.

262

552-558

663790

14689166

Substrate specificities and electron paramagnetic resonance properties of benzylsuccinate synthases in anaerobic toluene and m-xylene metabolism

2004

Verfürth, K.; Pierik, A.J.; Leutwein, C.; Zorn, S.; Heider, J.

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Links to other databases for p-cresol

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