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Ligand hydroquinone

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

KEGG

Aminobenzoate degradation, Benzoate degradation, Bisphenol degradation, Chemical carcinogenesis - reactive oxygen species, Chlorocyclohexane and chlorobenzene degradation, Microbial metabolism in diverse environments, Tyrosine metabolism more

MetaCyc

4-aminophenol degradation, 4-hydroxyacetophenone degradation, 4-nitrophenol degradation I, firefly bioluminescence, phenylacetate degradation II (anaerobic), quinate degradation I, shikimate degradation I, thiosulfate oxidation II (via tetrathionate) more

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (6 results)

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Show Natural Substrate (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.66

benzene-1,4-diol + O2 = (2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate

745802, 744430, 745331

-

1.14.18.3

methane + quinol + O2 = methanol + quinone + H2O

745305, 744325, 745389, 745730, 745857, 746420

-

1.7.5.1

nitrate + quinol = nitrite + quinone + H2O

696212, 697207, 700218, 700372, 698645, 395191

-

2.4.1.218

UDP-glucose + hydroquinone = UDP + hydroquinone-O-beta-D-glucopyranoside

658631, 735733

-

7.1.1.8

quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+

724562, 724549, 725396

-

7.1.1.8

quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + H+

743061, 743383, 742085

-

7.1.1.8

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (22 results)

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Show Natural Product (22 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.5.4

(S)-malate + quinone = oxaloacetate + quinol

0

-

1.1.99.18

cellobiose + 1,4-benzoquinone = cellobiono-1,5-lactone + reduced 1,4-benzoquinone

0

-

1.1.99.29

2,3-didehydro-D-glucose + 1,4-benzoquinone = 3-dehydro-D-glucose + hydroquinone

0

-

1.1.99.29

2-dehydro-D-xylose + 1,4-benzoquinone = 2,3-didehydro-D-xylose + hydroquinone

0

-

1.1.99.29

D-glucose + 1,4-benzoquinone = 2,3-didehydro-D-glucose + hydroquinone

0

-

1.1.99.29

D-xylose + 1,4-benzoquinone = 2-dehydro-D-xylose + hydroquinone

0

-

1.14.13.64

4-hydroxybenzoate + NAD(P)H + 2 H+ + O2 = hydroquinone + NAD(P)+ + H2O + CO2

0

-

1.14.13.64

4-hydroxybenzoate + NAD(P)H + H+ + O2 = hydroquinone + NAD(P)+ + H2O + CO2

0

-

1.14.13.64

4-hydroxybenzoate + NADH + 2 H+ + O2 = hydroquinone + NAD+ + H2O + CO2

0

-

1.1.99.29

4 entries

1.14.13.64

3 entries

1.2.5.1

pyruvate + quinone + H2O = acetate + CO2 + quinol

0

-

1.3.5.6

9,9'-dicis-zeta-carotene + 2 quinone = 7,9,7',9'-tetracis-lycopene + 2 quinol

0

-

1.3.5.6

zeta-carotene + 2 quinone = lycopene + 2 quinol

0

-

1.3.5.6

phytoene + quinone = 7,9,9'-tricis-neurosporene + quinol

0

-

1.3.5.6

3 entries

1.6.5.2

quinone + NAD(P)H = hydroquinone + NAD(P)+

394368, 394363

-

1.6.5.5

NADPH + H+ + 2 quinone = NADP+ + 2 semiquinone

0

-

1.8.5.4

HS- + quinone = polysulfide + quinol

0

-

1.8.5.4

sulfide + quinone = elemental sulfur + quinol

0

-

1.8.5.7

gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone = gamma-glutamylcysteine glutahione disulfide + hydroquinone

0

-

1.8.5.7

glutathione + 2-(glutathione-S-yl)-hydroquinone = glutathione disulfide + hydroquinone

0

-

1.8.5.4

2 entries

1.8.5.7

2 entries

1.8.5.8

hydrogen sulfide + glutathione + quinone = S-sulfanylglutathione + quinol

0

-

1.8.5.9

[DsbA protein] with reduced L-cysteine residues + quinone = [DsbA protein] carrying a disulfide bond + quinol

0

-

3.2.1.21

arbutin + H2O = 4-hydroxyphenol + beta-D-glucose

0

-

Substrate in Enzyme-catalyzed Reactions (79 results)

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Show Substrate (79 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.28

hydroquinone + inosine + O2 = p-quinone + 9-riburonosylhypoxanthine + H2O

287614

-

1.10.3.1

hydroquinone + O2 = ?

727645

-

1.10.3.1

p-hydroquinone + O2 = ?

684646

-

1.10.3.2

morpholine + 1,4-hydroquinone + O2 = 2,5-dimorpholin-4-yl-[1,4]benzoquinone

696873

-

1.10.3.2

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

699726

-

1.10.3.2

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

699726

-

1.10.3.2

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

699726

-

1.10.3.2

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

699726

-

1.10.3.2

benzenediol + thiobarbituric acid = 1,1'',3,3''-tetraethyl-2',3',6',7'-tetrahydroxy-2,2''-dithioxo-2H,2''H-dispiro[pyrimidine-5,9'-anthracene-10',5''-pyrimidine]-4,4'',6,6''(1H,1''H,3H,3''H)-tetrone

699726

-

1.10.3.2

hydroquinone + 4-aminoantipyrine + O2 = ? + H2O

655631

-

1.10.3.2

hydroquinone + O2 = ?

724569, 743704, 697664, 742682, 671404, 696857, 743078, 675232, 724573, 698284, 725731, 742658, 742104, 712724

-

1.10.3.2

hydroquinone + O2 = ? + H2O

655375, 655362, 655627

-

1.10.3.2

quinol + O2 = ? + H2O

396398, 396394, 396375, 396380, 396352, 396347, 396369, 396353, 396364, 396381, 396399

-

1.10.3.1

2 entries

1.10.3.2

10 entries

1.10.3.3

2 hydroquinone + O2 = 2 quinone + 2 H2O

439889

-

1.10.3.6

p-hydroquinone + O2 = ?

439884, 439882

-

1.11.1.13

1,4-benzenediol + 2 H+ + H2O2 = ? + 2 H2O

764875

-

1.11.1.13

hydroquinone + H2O2 = ?

658136

-

1.11.1.13

Mn2+ + hydroquinone = ?

660488

-

1.11.1.13

3 entries

1.11.1.16

1,4-benzohydroquinone + H2O2 = ? + H2O

664813

-

1.11.1.19

hydroquinone + H2O2 + H+ = ?

742882

-

1.11.1.5

hydroquinone + H2O2 = benzoquinone + H2O

394614

-

1.11.1.7

hydroquinone + H2O2 = ? + H2O

742414

-

1.13.11.2

hydroquinone + O2 = ?

724201

-

1.13.11.66

benzene-1,4-diol + O2 = (2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate

745802, 744430, 745331

-

1.13.11.66

hydroquinone + O2 = 4-hydroxymuconic acid semialdehyde

719179, 719693, 764851, 718555

-

1.13.11.66

hydroquinone + O2 = 4-hydroxymuconic semialdehyde

719714, 719327

-

1.13.11.66

hydroquinone + O2 = gamma-hydroxymuconic acid semialdehyde

719104

-

1.13.11.66

4 entries

1.14.13.2

hydroquinone + NADPH + H+ + O2 = ? + NADP+ + H2O

684919

-

1.14.13.7

4-hydroxyphenol + NADPH + H+ + O2 = ?

690215

-

1.14.13.7

4-hydroxyphenol + O2 + NADPH = ?

438782

-

1.14.13.7

hydroquinone + NADPH + H+ + O2 = ? + NADP+ + H2O

743011

-

1.14.13.7

quinol + NADPH + H+ + O2 = ? + NADP+ + H2O

764589

-

1.14.13.7

quinol + NADPH + O2 = ?

662875

-

1.14.13.7

quinol + O2 + NADPH = 1,2,4-trihydroxybenzene + NADP+ + H2O

394993, 438777

-

1.14.13.7

6 entries

1.14.14.20

quinol + O2 + NADPH = 1,2,4-trihydroxybenzene + NADP+ + H2O

438788

-

1.14.18.1

2 hydroquinone + O2 = 2 quinone + 2 H2O

636380, 636452

-

1.14.18.1

hydroquinone + O2 = ?

744490, 746222

-

1.14.18.1

p-hydroquinone + O2 = ?

684646

-

1.14.18.1

quinol + O2 = quinone + H2O

636399

-

1.14.18.1

4 entries

1.14.18.3

methane + quinol + O2 = methanol + quinone + H2O

745305, 744325, 745389, 745730, 745857, 746420

-

1.14.99.B10

cellohexaose + hydroquinone + O2 = oxidized cellobiose + oxidized cellotriose + benzoquinone + H2O

740726

-

1.14.99.B10

cellopentaose + hydroquinone + O2 = oxidized cellobiose + oxidized cellotriose + benzoquinone + H2O

740726

-

1.16.3.1

Fe(II) + hydroquinone + O2 = Fe(III) + ? + H2O

672085

-

1.16.3.1

hydroquinone + Fe2+ + O2 = ?

658983, 659524, 687084

-

1.14.99.B10

2 entries

1.16.3.1

2 entries

1.17.9.1

1,4-hydroxyquinone + acceptor + H2O = ?

437874

-

1.21.3.4

hydroquinone + O2 = ?

437825

-

1.21.3.5

hydroquinone + O2 = ?

437825

-

1.3.3.5

hydroquinone + O2 = ?

391019

-

1.3.5.1

fumarate + quinol = succinate + ubiquinone

391137, 391139

-

1.7.5.1

nitrate + quinol = nitrite + quinone

696212

-

1.7.5.1

nitrate + quinol = nitrite + quinone + H2O

700218, 696212, 697207, 700372, 698645, 395191

-

2.3.1.133

4-coumaroyl-CoA + hydroquinone = CoA + 1-(4-coumaroyl)hydroquinone

736977

-

2.3.1.133

4-coumaroyl-CoA + hydroquinone = CoA + 1-O-(4-coumaroyl)hydroquinone

736977

-

1.7.5.1

2 entries

2.3.1.133

2 entries

2.4.1.10

sucrose + hydroquinone = D-glucose + 4-hydroxyphenyl-beta-D-fructofuranoside

701838

-

2.4.1.218

CDP-glucose + hydroquinone = CDP + hydroquinone-O-beta-D-glucopyranoside

393094

-

2.4.1.218

TDP-glucose + hydroquinone = TDP + hydroquinone-O-beta-D-glucopyranoside

393094

-

2.4.1.218

UDP-alpha-D-glucose + hydroquinone = UDP + hydroquinone-O-beta-D-glucopyranoside

745691

-

2.4.1.218

UDP-glucose + hydroquinone = UDP + hydroquinone-O-beta-D-glucopyranoside

393093, 393095, 393094, 658631, 735733

-

2.4.1.218

4 entries

2.4.1.237

UDP-glucose + hydroquinone = UDP + hydroquinone O-beta-D-glucoside

489572

-

2.4.1.35

UDPglucose + hydroquinone = UDP + 4-beta-D-glucopyranosyloxyphenol

489104, 489101

-

2.4.1.4

sucrose + hydroquinone = D-fructose + alpha-arbutin

757357

-

2.4.1.4

sucrose + hydroquinone = D-fructose + hydroquinone alpha-glucopyranoside

756762

-

2.4.1.4

sucrose + hydroquinone = D-fructose + hydroquinone alpha-glucoside

757420

-

2.4.1.4

sucrose + hydroquinone = D-fructose + hydroquinone-O-alpha-D-glucopyranoside

718673

-

2.4.1.4

4 entries

2.4.1.5

sucrose + hydroquinone = D-fructose + 4-hydroxyphenyl-alpha-D-glucopyranoside

703495

-

2.4.1.7

sucrose + hydroquinone = D-fructose + ?

685688

-

2.4.1.7

sucrose + hydroquinone = D-fructose + alpha-arbutin

758280

-

2.4.1.7

2 entries

2.4.1.85

UDPglucose + hydroquinone = UDP + hydroquinone glucoside

489458

-

2.4.1.9

sucrose + hydroquinone = ?

720270

-

2.8.2.1

3'-phosphoadenylylsulfate + hydroquinone = adenosine 3',5'-bisphosphate + ?

645642

-

2.8.2.2

3'-phosphoadenylylsulfate + hydroquinone = adenosine 3',5'-bisphosphate + hydroquinone sulfate

739274

-

3.2.1.168

hydroquinone + hesperidin = 4-hydroxyphenyl-beta-D-rutinoside + hesperetin

753044

-

3.2.1.23

lactose + hydroquinone = hydroquinone galactoside + D-glucose

715223

-

3.2.1.8

hydroquinone + H2O = ?

696821

-

7.1.1.8

quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+

724562, 724549, 725396

-

7.1.1.8

quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + H+

743061, 743383, 742085

-

7.1.1.8

quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + H+ [side 2]

439995

-

7.1.1.8

quinol + 2 ferricytochrome c1 = quinone + 2 ferrocytochrome c1 + H+ [side 2]

440015, 440010, 395300

-

7.1.1.8

quinol + 2 horse heart ferricytochrome c1 = quinone + 2 horse heart ferrocytochrome c1 + H+ [side 2]

440012

-

7.1.1.8

5 entries

Product in Enzyme-catalyzed Reactions (144 results)

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Show Product (144 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.328

1,4-benzoquinone + NADPH + H+ = 1,4-benzoquinol + NADP+

0

-

1.1.3.10

D-galactose + 1,4-benzoquinone = 2-dehydro-D-galactose + 1,4-hydroquinone

0

-

1.1.3.10

D-glucose + 1,4-benzoquinone = 2-dehydro-D-glucose + 1,4-hydroquinone

0

-

1.1.3.10

D-ribose + 1,4-benzoquinone = 2-dehydro-D-ribose + 1,4-hydroquinone

0

-

1.1.3.10

D-xylose + 1,4-benzoquinone = 2-dehydro-D-xylose + 1,4-hydroquinone

0

-

1.1.3.10

L-arabinose + 1,4-benzoquinone = 2-dehydro-L-arabinose + 1,4-hydroquinone

0

-

1.1.3.10

D-galactose + 1,4-benzoquinone = 2-dehydro-D-galactose + hydroquinone

0

-

1.1.3.10

D-glucose + 1,4-benzoquinone = 2-dehydro-D-glucose + hydroquinone

0

-

1.1.3.10

7 entries

1.1.3.13

formaldehyde + p-benzoquinone = formic acid + p-benzoquinol

0

-

1.1.3.4

beta-D-glucose + 4-benzoquinone = D-glucono-1,5-lactone + 4-benzoquinol

0

-

1.1.3.4

beta-D-glucose + 1,4-benzoquinone = D-glucono-1,5-lactone + hydroquinone

0

-

1.1.3.4

beta-D-glucose + benzoquinone = D-glucono-1,5-lactone + hydroquinone

389797

-

1.1.3.4

3 entries

1.1.5.3

sn-glycerol 3-phosphate + quinone = glycerone phosphate + quinol

0

-

1.1.5.4

(S)-malate + quinone = oxaloacetate + quinol

0

-

1.1.5.9

D-glucose + 1,4-benzoquinone = D-glucono-1,5-lactone + 1,4-benzoquinol

0

-

1.1.99.18

lactose + 1,4-benzoquinone = 4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + 1,4-benzoquinol

0

-

1.1.99.18

beta-D-lactose + benzoquinone = lactobiono-1,5-lactone + benzoquinol

0

-

1.1.99.18

maltose + benzoquinone = maltono-1,5-lactone + benzoquinol

0

-

1.1.99.18

cellobiose + 1,4-benzoquinone = cellobiono-1,5-lactone + reduced 1,4-benzoquinone

0

-

1.1.99.18

cellopentaose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

cellotetraose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

cellotriose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

D-galactose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

D-glucose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

D-mannose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

D-xylose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

lactose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

maltose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

maltotetraose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

maltotriose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

mannopentaose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.18

xylobiose + 1,4-benzoquinone = 4-O-beta-D-xylopyranosyl-D-xylono-1,5-lactone + reduced 1,4-benzoquinone

0

-

1.1.99.18

xylotriose + 1,4-benzoquinone = ? + reduced 1,4-benzoquinone

0

-

1.1.99.29

D-glucose + 2 1,4-benzoquinone = 2,3-didehydro-D-glucose + 2 hydroquinone

0

-

1.1.99.29

D-xylose + 2 1,4-benzoquinone = 2,3-didehydro-D-xylose + 2 hydroquinone

0

-

1.1.99.29

2,3-didehydro-D-glucose + 1,4-benzoquinone = 3-dehydro-D-glucose + hydroquinone

0

-

1.1.99.29

2-dehydro-D-xylose + 1,4-benzoquinone = 2,3-didehydro-D-xylose + hydroquinone

0

-

1.1.99.29

3-dehydro-D-glucose + 1,4-benzoquinone = 2,3-didehydro-D-glucose + hydroquinone

0

-

1.1.99.29

aldopyranose + 1,4-benzoquinone = 2-aldoketose + hydroquinone

0

-

1.1.99.29

aldopyranose + quinone = 2-aldoketose + hydroquinone

0

-

1.1.99.29

alpha,alpha-trehalose + 1,4-benzoquinone = 3,3'-didehydro-alpha,alpha-trehalose + hydroquinone

0

-

1.1.99.29

D-allose + 1,4-benzoquinone = 2-dehydro-D-allose + hydroquinone

0

-

1.1.99.29

D-arabinose + 1,4-benzoquinone = 2-dehydro-D-arabinose + hydroquinone

0

-

1.1.99.29

D-galactose + 1,4-benzoquinone = 2-dehydro-D-galactose + hydroquinone

0

-

1.1.99.29

D-galactose + benzoquinone = 2,3-didehydro-D-galactose + hydroquinone

0

-

1.1.99.29

D-galactose + benzoquinone = 2-dehydro-D-galactose + hydroquinone

0

-

1.1.99.29

D-glucose + 1,4-benzoquinone = 2,3-didehydro-D-glucose + hydroquinone

0

-

1.1.99.29

D-glucose + 1,4-benzoquinone = 2-dehydro-D-glucose + hydroquinone

0

-

1.1.99.29

D-glucose + 1,4-benzoquinone = 3-dehydro-D-glucose + hydroquinone

0

-

1.1.99.29

D-glucose + benzoquinone = 2,3-didehydro-D-glucose + hydroquinone

0

-

1.1.99.29

D-ribose + 1,4-benzoquinone = 2-dehydro-D-ribose + hydroquinone

0

-

1.1.99.29

D-xylose + 1,4-benzoquinone = 2-dehydro-D-xylose + hydroquinone

0

-

1.1.99.29

erlose + 1,4-benzoquinone = 3-dehydroerlose + hydroquinone

0

-

1.1.99.29

L-arabinose + 1,4-benzoquinone = 2-dehydro-L-arabinose + hydroquinone

0

-

1.1.99.29

L-glucose + 1,4-benzoquinone = 2-dehydro-L-glucose + hydroquinone

0

-

1.1.99.29

L-sorbose + 1,4-benzoquinone = 2-dehydro-L-sorbose + hydroquinone

0

-

1.1.99.29

melizitose + 1,4-benzoquinone = 3-dehydromelizitose + hydroquinone

0

-

1.1.99.29

methyl-alpha-D-galactopyranoside + 1,4-benzoquinone = methyl-alpha-3-dehydro-D-galactopyranoside + hydroquinone

0

-

1.1.99.29

methyl-alpha-D-glucopyranoside + 1,4-benzoquinone = methyl-alpha-3-dehydro-D-glucopyranoside + hydroquinone

0

-

1.1.99.29

methyl-beta-D-glucopyranoside + 1,4-benzoquinone = methyl-beta-3-dehydro-D-glucopyranoside + hydroquinone

0

-

1.1.99.29

sucrose + 1,4-benzoquinone = 3'-dehydrosucrose + hydroquinone

0

-

1.1.99.18

18 entries

1.1.99.29

28 entries

1.10.3.9

H2O + 1,4-benzoquinone + hv = O2 + 1,4-benzoquinol

0

-

1.11.1.25

glutaredoxin + benzoquinone = glutaredoxin disulfide + H2O + hydroquinone

0

-

1.11.2.1

phenol + H2O2 = hydroquinone + catechol + H2O

0

-

1.14.12.12

phenol + NADH + O2 = catechol + hydroquinone + NAD+

0

-

1.14.13.114

4-hydroxybenzoate + NADH + H+ + O2 = hydroquinone + NAD+ + H2O + CO2

0

-

1.14.13.166

phenol + NADH + H+ + O2 = hydroquinone + ? + NAD+ + H2O

0

-

1.14.13.18

4-hydroxyphenoxyacetate + ? = hydroquinone + glycolate + ?

347714

-

1.14.13.25

benzene + NAD(P)H + H+ + O2 = phenol + hydroquinone + NAD(P)+ + H2O

438920, 438923

-

1.14.13.27

4-hydroxybenzoate + NAD(P)H + O2 = quinol + NAD(P)+ + H2O2 + CO2

438909

-

1.14.13.64

4-Hydroxybenzoate + NADH + O2 = 1,4-Dihydroxybenzene + NAD+ + CO2

7427, 7428

-

1.14.13.64

4-Hydroxybenzoate + NADPH + O2 = 1,4-Dihydroxybenzene + NADP+ + CO2

7427, 7428

-

1.14.13.64

4-hydroxybenzoate + NAD(P)H + 2 H+ + O2 = hydroquinone + NAD(P)+ + H2O + CO2

0

-

1.14.13.64

4-hydroxybenzoate + NAD(P)H + H+ + O2 = hydroquinone + NAD(P)+ + H2O + CO2

0

-

1.14.13.64

4-hydroxybenzoate + NADH + 2 H+ + O2 = hydroquinone + NAD+ + H2O + CO2

0

-

1.14.13.64

4-hydroxybenzoate + NADH + O2 = hydroquinone + NAD+ + CO2

0

-

1.14.13.64

4-hydroxybenzoate + NADPH + O2 = hydroquinone + NADP+ + CO2

0

-

1.14.13.64

protocatechuate + NADH + 2 H+ + O2 = hydroquinone + NAD+ + H2O + CO2

0

-

1.14.13.64

8 entries

1.14.13.8

4-chlorophenol + O2 = hydroquinone + H2O + Cl-

0

-

1.17.1.4

xanthine + p-benzoquinone + H2O = hypoxanthine + hydroquinone + ?

644618

-

1.17.1.4

xanthine + p-benzoquinone + H2O = p-benzosemiquinone + urate

644618

-

1.17.1.4

2 entries

1.17.5.1

phenylacetyl-CoA + H2O + quinone = phenylglyoxylyl-CoA + quinol

644661, 0

-

1.17.5.B2

4,4'-dihydroxy-beta-carotene + benzoquinone = canthaxanthin + benzoquinol

0

-

1.17.5.B2

beta-carotene + benzoquinone + H2O = echinenone + benzoquinol + 2 H+

0

-

1.17.5.B2

2 entries

1.18.1.1

NADH + p-benzoquinone = NAD+ + p-benzoquinol

0

-

1.2.5.1

pyruvate + quinone + H2O = acetate + CO2 + quinol

0

-

1.2.5.3

CO + benzoquinone + H2O = CO2 + benzoquinol

0

-

1.3.2.3

L-galactono-1,4-lactone + 1,4-benzoquinone = L-ascorbate + reduced 1,4-benzoquinone

0

-

1.3.3.12

D-arabinono-1,4-lactone + 1,4-benzoquinone = ? + 1,4-benzoquinol

0

-

1.3.3.12

L-galactono-1,4-lactone + 1,4-benzoquinone = L-ascorbate + 1,4-benzoquinol

0

-

1.3.5.6

9,9'-dicis-zeta-carotene + 2 quinone = 7,9,7',9'-tetracis-lycopene + 2 quinol

0

-

1.3.5.6

zeta-carotene + 2 quinone = lycopene + 2 quinol

0

-

1.3.5.6

phytoene + quinone = 7,9,9'-tricis-neurosporene + quinol

0

-

1.3.3.12

2 entries

1.3.5.6

3 entries

1.5.1.30

1,4-benzoquinone + NADH + H+ = 1,4-benzoquinol + NAD+

0

-

1.6.5.10

NADPH + H+ + 1,4-benzoquinone = NADP+ + 1,4-benzohydroquinol

0

-

1.6.5.10

1,4-benzoquinone + NADPH + H+ = 1,4-benzoquinol + NADP+

0

-

1.6.5.10

benzoquinone + NADPH = benzohydroquinone + NADP+

0

-

1.6.5.10

benzoquinone + NADPH + H+ = benzoquinol + NADP+

0

-

1.6.5.10

NADPH + H+ + p-benzoquinone = NADP+ + p-benzohydroquinone

392826

-

1.6.5.10

NADPH + H+ + quinone = NADP+ + quinol

0

-

1.6.5.2

1,4-benzoquinone + NAD(P)H + H+ = 1,4-benzoquinol + NAD(P)+

0

-

1.6.5.2

1,4-benzoquinone + NADH + H+ = 1,4-benzoquinol + NAD+

0

-

1.6.5.2

benzoquinone + 2 NAD(P)H + H+ = benzohydroquinone + 2 NAD(P)+

394364, 394352, 394350, 394353, 0

-

1.6.5.2

p-benzoquinone + NADH = benzohydroquinone + NAD+

0

-

1.6.5.2

NADH + H+ + benzoquinone = NAD+ + benzoquinol

0

-

1.6.5.2

NADPH + H+ + benzoquinone = NADP+ + benzoquinol

0

-

1.6.5.2

NAD(P)H + H+ + quinone = NAD(P)+ + hydroquinone

0

-

1.6.5.2

quinone + NAD(P)H = hydroquinone + NAD(P)+

394368, 394363

-

1.6.5.2

p-benzoquinone + NADPH = p-benzohydroquinone + NADP+

0

-

1.6.5.5

1,4-benzoquinone + NADPH + H+ = 1,4-benzoquinol + NADP+

0

-

1.6.5.5

NADPH + H+ + 2 quinone = NADP+ + 2 semiquinone

0

-

1.6.5.6

NADPH + H+ + p-benzoquinone = NADP+ + hydroquinone

0

-

1.6.5.6

p-benzoquinone + NADPH = NADP+ + hydroquinone

0

-

1.6.5.10

6 entries

1.6.5.2

9 entries

1.6.5.5

2 entries

1.6.5.6

2 entries

1.7.1.1

benzoquinone + NADH = benzoquinol + NAD+

0

-

1.7.1.6

NADPH + H+ + 1,4-benzoquinone = NADP+ + 1,4-benzoquinol

394297

-

1.7.2.1

nitrite + reduced hydroquinone = nitric oxide + H2O + hydroquinone

0

-

1.8.1.4

1,4-benzoquinone + NADH = 1,4-benzoquinol + NAD+

0

-

1.8.5.4

HS- + quinone = polysulfide + quinol

0

-

1.8.5.4

sulfide + quinone = elemental sulfur + quinol

0

-

1.8.5.4

sulfide + quinone = sulfur + quinol

0

-

1.8.5.7

gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone = gamma-glutamylcysteine glutahione disulfide + hydroquinone

0

-

1.8.5.7

gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone = gamma-glutamylcysteine glutathione disulfide + hydroquinone

0

-

1.8.5.7

glutathione + 2-(glutathione-S-yl)-hydroquinone = glutathione disulfide + hydroquinone

0

-

1.8.5.4

3 entries

1.8.5.7

3 entries

1.8.5.8

hydrogen sulfide + glutathione + quinone = S-sulfanylglutathione + quinol

0

-

1.8.5.9

[DsbA protein] with reduced L-cysteine residues + quinone = [DsbA protein] carrying a disulfide bond + quinol

0

-

3.1.1.1

4-hydroxyphenyl acetate + H2O = 4-hydroxyphenol + acetate

0

-

3.1.6.1

hydroquinone sulfate + H2O = hydroquinone + sulfate

0

-

3.2.1.104

arbutin + H2O = D-glucose + benzene-1,4-diol

0

-

3.2.1.126

arbutin = benzene-1,4-diol + beta-D-glucose

0

-

3.2.1.21

(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O = 4-hydroxyphenol + beta-D-glucopyranose

171306, 326277, 326316, 326358, 0, 326301, 326293, 326328, 326295, 326287, 326304

-

3.2.1.21

arbutin + H2O = 4-hydroxyphenol + beta-D-glucose

0

-

3.2.1.21

arbutin + H2O = 4-hydroxyphenol + D-glucose

0

-

3.2.1.21

arbutin + H2O = beta-D-glucose + 4-hydroxyphenol

0

-

3.2.1.21

arbutin + H2O = hydroquinol + beta-D-glucose

0

-

3.2.1.21

5 entries

3.2.1.58

esculin + H2O = D-glucose + 4-hydroxyphenol

0

-

3.2.1.74

hydroquinone-beta-D-glucopyranoside + H2O = hydroquinone + D-glucose

136825

-

3.2.1.86

arbutin 6-phosphate + H2O = hydroquinone + D-glucose 6-phosphate

0

-

3.5.1.64

Nalpha-(4-hydroxybenzoyl)-L-Asp + H2O = 1,4-dihydroxybenzene + CO2 + L-Asp

0

-

4.1.1.46

2,5-dihydroxybenzoate = 4-hydroxyphenol + CO2

0

-

4.1.1.62

2,5-Dihydroxybenzoate = Hydroquinone + CO2

4728

-

7.1.1.2

NADH + H+ + 1,4-benzoquinone = NAD+ + 1,4-benzoquinol

0

-

7.1.1.2

benzoquinone + NADH + H+ = benzohydroquinone + NAD+

0

-

7.1.1.2

NADH + benzoquinone + H+ = NAD+ + benzoquinol

0

-

7.1.1.2

NADH + benzoquinone = NAD+ + benzoquinol

0

-

7.1.1.2

4 entries

Enzyme Cofactor/Cosubstrate (4 results)

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Show Cofactor (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.18.3

-

745389, 745857, 746420

-

1.14.18.3

quinone is predominantly used by pMMO in order to sustain its activity

745730

-

1.14.18.3

the cofactor receives electrons from NADH

744325

-

1.14.18.3

3 entries

7.1.1.8

antimycin-sensitive prosthetic group

440012

-

Activator in Enzyme-catalyzed Reactions (6 results)

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Show Activating Compound (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.99.1

-

438391

-

1.14.99.1

stimulates conversion of prostaglandin G1 to H1

438375

-

1.14.99.1

stimulates

438389

-

1.14.99.1

3 entries

1.2.3.4

0.1 mM concentration 123% activation

288392

-

3.2.1.4

2 mM, slight activation, cellulase I

393620

-

5.6.2.2

physiological precursor of 1,4-benzoquinone, a topoisomerase II poison, enhances cleavage activity, inhibits ligation activity, at 0.25 mM, alters the enzyme's cleavage site specificity, 1,4-hydroquinone has a higher inhibitory effect on ligation activity but a lower effect on cleavage activity compared to 1,4-benzoquinone

661475

-

Inhibitor in Enzyme-catalyzed Reactions (34 results)

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Show Inhibitors (34 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.25

lower inhibitry potency, about 25% inhibition at 0.0025 mM

740771

-

1.1.1.39

-

286718

-

1.1.3.13

-

724083

-

1.1.3.13

1 mM, 30 min, strong

484925

-

1.1.3.13

2 entries

1.10.3.1

-

744955

-

1.11.1.7

98% inhibition at 1 mM

439733

-

1.13.11.27

4.7 mM, 50% inhibition

395375

-

1.13.12.16

-

639224

-

1.14.11.2

-

439194

-

1.14.13.81

-

636332

-

1.14.17.1

-

438609

-

1.14.18.1

-

636380, 685452, 685604, 696563, 699403, 711476, 744671, 746222

-

1.14.18.1

exhibits less tyrosinase-inhibitory activity than 3-hydroxyphloretin or catechol, very toxic to HEMn cell

689413

-

1.14.18.1

HQ, tyrosinase inhibitor

689440

-

1.14.18.1

shows membrane breaking and toxicity towards melanosomes, and induces hydroxyl free radicals

746229

-

1.14.18.1

tyrosinase inhibitor

689440

-

1.14.18.1

-

636399

-

1.14.18.1

6 entries

1.2.1.11

-

762956

-

1.3.1.57

tested at 1.0 mM and under N2, 31% inhibition

288477

-

1.6.5.2

shows noncompetitive inhibition in all conditions, it can bind to multiple enzyme forms or sites, even when either of the substrates (NADH or benzoquinone) is present at high concentrations

714189

-

2.4.1.21

5 mM, complete inhibition

488919

-

2.4.1.218

Glu274 is acting as an acidic backbone acceptor residue. Lys262, a basic amino acid from the active site of wheat Hydroquinone glucosyltransferase interacts with the hydroxyl group of hydroquinone and behaves as a side chain donor molecule. Asp264 is also observed as an interacting residue from the active site of hydroquinone glucosyltransferase. It binds to the hydroxyl group of hydroquinone inhibitor and donates hydrogen ion from its side chain group

735733

-

2.4.1.30

strongly inhibits in absence of 2-mercaptoethanol

489039, 489040

-

2.5.1.93

98% inhibition

738205

-

3.1.1.20

competitive

94249

-

3.2.1.35

irreversible inhibition

171410

-

3.5.4.1

-

718465

-

3.5.4.B9

-

718465

-

4.2.1.1

-

696622

4e3h, 3D-view

4.99.1.10

11% residual activity at 1 mM

743419

-

5.1.1.1

noncompetitive inhibition, has minimal cytotoxicity against mammalian cells. Hydroquinone binds near the active center of alanine racemase

747417

-

5.6.2.2

inhibition mechanism

661417

-

5.6.2.2

physiological precursor of 1,4-benzoquinone, a topoisomerase II poison, enhances cleavage activity, inhibits ligation activity, at 0.25 mM, alters the enzyme's cleavage site specificity, 1,4-hydroquinone has a higher inhibitory effect on ligation activity but a lower effect on cleavage activity compared to 1,4-benzoquinone

661475

-

5.6.2.2

hydroquinone inhibits topoII at the DNA binding stage as well as in the closed clamp stage in the catalytic cycle, thereby interfering with either the binding to, or the release of, DNA from the enzyme, inhibition mechanism, overview

703168

-

5.6.2.2

3 entries

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

3.5.1.5

5fse, 3D-view

4.2.1.1

4e3h, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (24 results)

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Show Turnover Number (24 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.10.3.2

0.051

-

pH 7.5, 37°C

742682

1.10.3.2

0.23

-

pH 7.0 37°C

743704

1.10.3.2

55

-

pH 7.0, 30°C

655375

1.10.3.2

443.8

-

pH 7.0, 40°C

742104

1.10.3.2

455

-

pH 4.5, 55°C

671404

1.10.3.2

5 entries

1.11.1.19

31

-

wild type enzyme, at pH 3.0 and 22°C

742882

1.13.11.66

2.1

-

pH 7.0, 25°C

719714

1.13.11.66

13.5

-

pH 7.0, 25°C

718555

1.13.11.66

2 entries

1.14.18.1

101.5

-

pH 7.0, 25°C

744490

1.16.3.1

0.39

-

mutant E185A, pH 6.0

659524

1.16.3.1

0.52

-

mutant E185A/Y354A, pH 6.0

659524

1.16.3.1

0.62

-

mutant D278A, pH 6.0

659524

1.16.3.1

0.85

-

wild-type, pH 6.0

659524

1.16.3.1

1.53

-

mutant E185A, pH 6.0

672085

1.16.3.1

1.57

-

mutant E185D, pH 6.0

659524

1.16.3.1

1.7

-

mutant Y354F, pH 6.0

659524

1.16.3.1

2.2

-

wild-type, pH 6.0

672085

1.16.3.1

2.3

-

mutant E185A/D409A, pH 6.0

672085

1.16.3.1

2.33

-

mutant D409A, pH 6.0

672085

1.16.3.1

2.81

-

mutant D283A, pH 6.0

672085

1.16.3.1

7.2

-

mutant Y354A, pH 6.0

659524

1.16.3.1

12 entries

1.6.5.10

1600

-

25°C, pH 6.5

655940

2.4.1.218

0.00038

-

pH 7.5, 30°C

745691

2.4.1.4

23.9

-

pH 7.0, 30°C

757357

K_M Value (46 results)

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Show KM Value (46 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.10.3.2

0.001

-

isoenzyme lac90

396398

1.10.3.2

0.029

-

-

396375

1.10.3.2

0.0686

-

pH 7.0, 40°C

742104

1.10.3.2

0.086

-

-

396399

1.10.3.2

0.11

-

-

396394

1.10.3.2

0.123

-

pH 7.0, 30°C

655375

1.10.3.2

1.25

-

-

396364

1.10.3.2

1.92

-

pH 7.0 37°C

743704

1.10.3.2

2.93

-

pH 6.5, 30°C

742658

1.10.3.2

11.33

-

pH 7.5, 37°C

742682

1.10.3.2

12

-

-

396380

1.10.3.2

11 entries

1.11.1.19

6.3

-

wild type enzyme, at pH 3.0 and 22°C

742882

1.13.11.66

0.0022

-

pH 7.0, 25°C

718555

1.13.11.66

0.037

-

pH 7.0, 25°C

719714

1.13.11.66

0.255

-

pH 7.4, temperature not specified in the publication

719327

1.14.18.1

0.92

-

pH 7.0, 25°C

744490

1.14.18.1

79

-

-

636399

1.16.3.1

0.018

-

mutant E185A

687084

1.16.3.1

0.019

-

mutant D283A

687084

1.16.3.1

0.025

-

wild-type

687084

1.16.3.1

0.03

-

mutant D409A

687084

1.16.3.1

0.03

-

mutant E185A/D409A

687084

1.16.3.1

3

-

wild-type, pH 6.0

659524

1.16.3.1

3

-

wild-type, pH 6.5, 25°C

658983

1.16.3.1

4.3

-

mutant D278A, pH 6.0

659524

1.16.3.1

4.6

-

mutant Y354A, pH 6.0

659524

1.16.3.1

4.6

-

mutant Y354A, pH 6.5, 25°C

658983

1.16.3.1

8.2

-

mutant E185D, pH 6.0

659524

1.16.3.1

8.2

-

mutant E185D, pH 6.5, 25°C

658983

1.16.3.1

12.7

-

mutant Y354F, pH 6.0

659524

1.16.3.1

12.7

-

mutant Y354F, pH 6.5, 25°C

658983

1.16.3.1

14.1

-

mutant E185A, pH 6.0

659524

1.16.3.1

14.1

-

mutant E185A, pH 6.5, 25°C

658983

1.16.3.1

16.9

-

mutant E185A/Y354A, pH 6.0

659524

1.16.3.1

18.2

-

mutant E185A, pH 6.0

672085

1.16.3.1

19.3

-

mutant D283A, pH 6.0

672085

1.16.3.1

25.5

-

wild-type, pH 6.0

672085

1.16.3.1

30.3

-

mutant D409A, pH 6.0

672085

1.16.3.1

30.5

-

mutant E185A/D409A, pH 6.0

672085

1.13.11.66

3 entries

1.14.18.1

2 entries

1.16.3.1

22 entries

1.21.3.4

60

-

-

437825

1.21.3.5

53

-

-

437825

1.6.5.10

647.5

-

25°C, pH 6.5

655940

2.4.1.218

0.43

-

pH 7.5, 30°C

745691

2.4.1.4

9.58

-

pH 7.0, 30°C

757357

2.8.2.1

0.6

-

isoenzyme II, pH 6.5, 37°C

645642

2.8.2.1

1.8

-

isoenzyme I, pH 6.5, 37°C

645642

2.8.2.1

2 entries

K_i Value (8 results)

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Show KI Value (8 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.11.2

14

-

-

439194

1.14.17.1

0.37

-

pH: 4.9

438609

1.14.17.1

1.05

-

pH: 5.9

438609

1.14.18.1

0.016

-

-

636399

1.14.18.1

0.09

-

-

636380

1.14.17.1

2 entries

1.14.18.1

2 entries

1.2.1.11

0.065

-

pH and temperature not specified in the publication

762956

4.2.1.1

0.0106

-

at pH 7.5 and 20°C

696622

5.1.1.1

0.212

-

pH 11.0, 35°C, recombinant His-tagged enzyme

747417

IC₅₀ Value (9 results)

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Show IC50 Value (9 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.10.3.1

0.044

-

pH 5.5, 25°C, with chlorogenic acid

744955

1.10.3.1

0.563

-

pH 5.5, 25°C, with 4-methylcatechol

744955

1.14.18.1

0.01348

-

value for inhibition of diphenolase activity using L-tyrosine as substrate, in 50 mM phosphate buffer, pH 6.5, at 37°C

711476

1.14.18.1

0.037

-

-

685604, 696563

1.14.18.1

0.0916

-

-

685452

1.14.18.1

1.09

-

value for inhibition of monophenolase activity using L-Dopa as substrate, in 50 mM phosphate buffer, pH 6.5, at 37°C

711476

1.10.3.1

2 entries

1.14.18.1

4 entries

3.5.4.1

0.0026

-

pH 7.4, 37°C

718465

3.5.4.B9

0.0026

-

at pH 7.8 and 37°C

718465

5.1.1.1

0.0185

-

pH 11.0, 35°C, recombinant His-tagged enzyme

747417

References & Links

Literature References (198)

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Show Reference (198 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4728

5309907

The non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic acid, protocatechuic acid and gallic acid by Klebsiella aerogenes (Aerobacter aerogenes)

1969

Grant, D.J.W.; Patel, J.C.

Antonie van Leeuwenhoek

35

325-343

7427

7926672

Catabolism of 4-hydroxybenzoate in Candida parapsilosis proceeds through initial oxidative decarboxylation by a FAD-dependent 4-hydroxybenzoate 1-hydroxylase

1994

van Berkel, W.J.H.; Eppink, M.H.M.; Middelhoven, W.J.; Vervoort, J.; Rietjens, I.M.C.M.

FEMS Microbiol. Lett.

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7428

9352916

Purification and properties of 4-hydroxybenzoate 1-hydroxylase (decarboxylating), a novel flavin adenine dinucleotide-dependent monooxygenase from Candida parapsilosis CBS604

1997

Eppink, M.H.M.; Boeren, S.A.; Vervoort, J.; van Berkel, W.J.H.

J. Bacteriol.

179

6680-6687

94249

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Hydrolizing pathway, substrate specificity and inhibition of tannin acyl hydrolase of Asp. oryzae No. 7

1972

Iibuchi, S.; Minoda, Y.; Yamada, K.

Agric. Biol. Chem.

36

1553-1562

136825

3093475

Isolation and characterization of a 1,4-beta-D-glucan glucohydrolase from the yeast, Torulopsis wickerhamii

1986

Himmel, M.E.; Tucker, M.P.; Lastick, S.M.; Oh, K.K.; Fox, J.W.; Spindler, D.D.; Grohmann, K.

J. Biol. Chem.

261

12948-12955

171306

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beta-Glucosidase and beta-galactosidase from the periplasmic space of Rhizobium trifolii cells

1982

Abe, M.; Higashi, S.

J. Gen. Appl. Microbiol.

28

551-562

171410

14943668

Hyaluronidases

1952

Meyer, K.; Rapport, M.M.

Adv. Enzymol. Relat. Subj. Biochem.

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199-236

286718

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Purification and properties of malic enzyme from Pseudomonas diminuta IFO-13182

1992

Suye, S.; Okada, Y.; Funada, A.; Kawagoe, M.; Inuta, S.

J. Ferment. Bioeng.

73

343-347

287614

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Laccase-like activity of nucleoside oxidase in the presence of nucleosides

1989

Isono, Y.; Hoshino, M.

Agric. Biol. Chem.

53

2197-2203

288392

-

Purification and characterization of oxalate oxidase from Pseudomonas sp. OX-53

1988

Koyama, H.

Agric. Biol. Chem.

52

743-748

288477

2925649

Purification and properties of phloroglucinol reductase from Eubacterium oxidoreducens G-41

1989

Haddock, J.D.; Ferry, J.G.

J. Biol. Chem.

264

4423 - 4427

326277

9675361

Characterization of the subsite structure of the beta-glucosidase from Aspergillus niger, an aspect of the mechanism of carbohydrate recognition

1998

Ohnishi, M.; Okada, G.; Yazaki, T.

Carbohydr. Res.

308

201-205

326287

7592339

Cloning, sequencing, and characterization of a membrane-associated Prevotella ruminicola B14 beta-glucosidase with cellodextrinase and cyanoglycosidase activities

1995

Wulff-Strobel, C.R.; Wilson, D.B.

J. Bacteriol.

177

5884-5890

326293

7925351

Purification and characterization of an extracellular beta-glucosidase with transglycosylation and exo-glucosidase activities from Fusarium oxysporum

1994

Christakopoulos, P.; Goodenough, P.W.; Kekos, D.; Macris, B.J.; Claeyssens, M.; Bhat, M.K.

Eur. J. Biochem.

224

379-385

326295

8486554

Purification and properties of the endocellular beta-glucosidase from Candida cacaoi Buckley and Van Uhden CBS 2020

1993

Drider, D.; Pommares, P.; Chemardin, P.; Arnaud, A.; Galzy, P.

J. Appl. Bacteriol.

74

473-479

326301

1599951

Purification and characterization of two extracellular beta-glucosidases from Trichoderma reesei

1992

Chen, H.; Hayn, M.; Esterbauer, H.

Biochim. Biophys. Acta

1121

54-60

326304

-

Purification and properties of a beta-glucosidase of Hanseniaspora vineae Van der Walt and Tscheuschner with the view to its utilization in fruit aroma libration

1989

Vasserot, Y.; Christiaens, H.; Chemardin, P.; Arnaud, A.; Galzy, P.

J. Appl. Bacteriol.

66

271-279

326316

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Purification of beta-D-glucosidase from Aspergillus niger

1988

McCleary, B.V.; Harrington, J.

Methods Enzymol.

160

575-583

326328

-

Purification and properties of an extracellular beta-glucosidase from the cellulolytic thermophile Clostridium stercorarium

1988

Bronnenmeier, K.; Staudenbauer, W.L.

Appl. Microbiol. Biotechnol.

28

380-386

326358

-

Fungal and other beta-D-glucosidases - their properties and applications

1982

Wiseman, A.

Enzyme Microb. Technol.

4

73-78

347714

234937

Metabolic function and properties of 4-hydroxyphenylacetic acid 1-hydroxylase from Pseudomonas acidovorans

1975

Hareland, W.A.; Crawford, R.L.; Chapman, P.J.; Dagley, S.

J. Bacteriol.

121

272-285

389797

-

Preparative production of hydroquinone from benzoquinone catalysed by immobilized D-glucose oxidase

1982

Alberti, B.N.; Klibanov, A.M.

Enzyme Microb. Technol.

4

47-49

391019

-

Purification and some properties of bilirubin oxidase of Myrotheticum verrucaria MT-1

1982

Tanaka, N.; Murao, S.

Agric. Biol. Chem.

46

2499-2503

391137

10486141

Comparison of catalytic activity and inhibitors of quinone reactions of succinate dehydrogenase (Succinate-ubiquinone oxidoreductase) and fumarate reductase (Menaquinol-fumarate oxidoreductase) from Escherichia coli

1999

Maklashina, E.; Cecchini, G.

Arch. Biochem. Biophys.

369

223-232

391139

11532445

Succinate: quinone oxidoreductases - what can we learn from Wolinella succinogenes quinol:fumarate reductase?

2001

Lancaster, C.R.D.

FEBS Lett.

504

133-141

392826

4388793

Purification and properties of three separate menadione reductases from hog liver

1969

Koli, A.K.; Yearby, C.; Scott, W.; Donaldson, K.O.

J. Biol. Chem.

244

621-629

393093

10680170

Hydroquinone:O-glucosyltransferase from cultivated Rauvolfia cells: enrichment and partial amino acid sequences

2000

Arend, J.; Warzecha, H.; Stöckigt, J.

Phytochemistry

53

187-193

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

393095

11505382

Utilizing genetically engineered bacteria to produce plant-specific glucosides

2001

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

Biotechnol. Bioeng.

76

126-131

393620

4215808

Studies on cellulase produced by the phytopathogens. Purification and enzymatic properties of cellulase of Fusarium moniliforme

1974

Matsumoto, K.; Endo, Y.; Tamiya, N.; Kano, M.; Miyauchi, K.; Abe, J.

J. Biochem.

76

563-572

394297

91608

Rat liver cytosolic azoreductase. Electron transport properties and the mechanism of dicumarol inhibition of the purified enzyme

1979

Huang, M.T.; Miwa, G.T.; Cronheim, N.; Lu, A.Y.H.

J. Biol. Chem.

254

11223-11227

394350

13846011

The reduction of vitamin K1 by an enzyme from dog liver

1960

Wosilait, W.D.

J. Biol. Chem.

235

1196-1201

394352

-

Vitamin K-Reduktase, Darstellung und eigenschaften

1960

Märki, F.; Martius, C.

Biochem. Z.

333

111-135

394353

7407710

Menadione reductase from Clostridium tyrobutyricum

1980

Petitdemange, H.; Marczak, R.; Raval, G.; Gay, R.

Can. J. Microbiol.

26

324-329

394363

6803779

Vitamin K1 hydroquinone formation catalyzed by DT-diaphorase

1982

Fasco, M.J.; Principe, L.M.

Biochem. Biophys. Res. Commun.

104

187-192

394364

2418014

Purification and characterization of two isofunctional forms of NAD(P)H: quinone reductase from mouse liver

1986

Prochaska, H.J.; Talalay, P.

J. Biol. Chem.

261

1372-1378

394368

-

Isolation and characterization of NAD(P)H-dehydrogenases from seeds of the castor bean

1983

Viljoen, C.C.; Cloete, F.; Botes, D.P.; Kruger, H.

Phytochemistry

22

365-370

394614

-

Cytochrome C peroxidase

1976

Yonetani, T.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

13

345-361

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

395191

11560477

Catalytic protein film voltammetry from a respiratory nitrate reductase provides evidence for complex electrochemical modulation of enzyme activity

2001

Anderson, L.J.; Richardson, D.J.; Butt, J.N.

Biochemistry

40

11294-11307

395300

6307358

Comparative aspects of quinol-cytochrome c/plastocyanin oxidoreductases

1983

Hauska, G.; Hurt, E.; Gabellini, N.; Lockau, W.

Biochim. Biophys. Acta

726

97-133

395375

7118918

Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874

1982

Lindstedt, S.; Rundgren, M.

J. Biol. Chem.

257

11922-11931

396347

-

Purification and properties of polyphenol oxidase from Chaetomium thermophile, a thermophilic fungus

1986

Ishigami, T.; Yamada, Y.

J. Gen. Appl. Microbiol.

32

293-301

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

396353

-

Laccases of Rigidoporus lignosus and Phellinus noxius

1986

Geiger, J.P.; Rio, B.; Nandris, D.; Nicole, M.

Appl. Biochem. Biotechnol.

12

121-133

396364

-

Properties of laccase in Schinus molle

1981

Bar-Nun, N.; Mayer, A.M.; Sharon, N.

Phytochemistry

20

407-408

396369

-

Laccase in Anacardiaceae

1978

Joel, D.M.; Marbach, I.; Mayer, A.M.

Phytochemistry

17

796-797

396375

-

Purification and properties of laccase from Ganoderma lucidum

1972

Lalitha Kumari, H.; Sirsi, M.

Arch. Mikrobiol.

84

350-357

396380

-

A laccase-like enzyme in peaches

1968

Mayer, A.M.; Harel, E.

Phytochemistry

7

1253-1256

396381

4863037

A fungal laccase, its properties and reconstitution from its protein and copper

1967

Iwasaki, H.; Matsubara, T.; Mori, T.

J. Biochem.

61

814-816

396394

-

Substrate specificity of laccase from Lentinus edodes

1996

D'Annibale, A.; Celletti, D.; Felici, M.; Di Mattia, E.; Giovannozzi-Sermanni, G.

Acta Biotechnol.

16

257-270

396398

9914531

Biochemical characterization, molecular cloning and expression of laccases - a divergent gene family - in poplar

1999

Ranocha, P.; McDougall, G.; Hawkins, S.; Sterjiades, R.; Borderies, G.; Stewart, D.; Cabanes-MacHeteau, M.; Boudet, A.M.; Goffner, D.

Eur. J. Biochem.

259

485-495

396399

11563958

Laccases from Basidiomycetes: Physicochemical characteristics and substrate specificity towards methoxyphenolic compounds

2001

Smirnov, S.A.; Koroleva, O.V.; Gavrilova, V.P.; Belova, A.B.; Klyachko, N.L.

Biochemistry (Moscow)

66

774-779

437825

7049104

Enzymatic synthesis of (+)- and (-)-bisdechlorogeodin with sulochrin oxidase from Penicillium frequentans and Oospora sulphurea-ochracea

1982

Nordlöv, H.; Gatenbeck, S.

Arch. Microbiol.

131

208-211

437874

2990444

p-Cresol methylhydroxylase. assay and general properties

1985

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

Biochem. J.

228

325-335

438375

816795

Purification of prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes

1976

Miyamoto, T.; Ogino, N.; Yamamoto, S.; Hayaishi, O.

J. Biol. Chem.

251

2629-2636

438389

7235

Biosynthesis of prostaglandins in rabbit kidney medulla. Properties of prostaglandin synthase

1976

Tai, H.H.; Tai, C.L.; Hollander, C.S.

Biochem. J.

154

257-264

438391

4831906

Characterization of prostaglandin synthetase in guinea pig lung. Isolation of a new prostaglandin derivative from arachidonic acid

1974

Parkes, D.G.; Eling, T.E.

Biochemistry

13

2598-2604

438609

7378421

Inhibition of dopamine-beta-hydroxylase by alternative electron donors

1980

Rosenberg, R.C.; Gimble, J.M.; Lovenberg, W.

Biochim. Biophys. Acta

613

62-72

438777

4146224

Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum

1973

Neujahr, H.Y.; Gaal, A.

Eur. J. Biochem.

35

386-400

438782

3997809

Effect of substrate and pH on the oxidative half-reaction of phenol hydroxylase

1985

Detmer, K.; Massey, V.

J. Biol. Chem.

260

5998-6005

438788

3430338

Phenol hydroxylase from Rhodococcus sp. P 1

1987

Straube, G.

J. Basic Microbiol.

27

229-232

438909

3489713

Purification and properties of 4-aminobenzoate hydroxylase, a new monooxygenase from Agaricus bisporus

1986

Tsuji, H.; Ogawa, T.; Bando, N.; Sasaoka, K.

J. Biol. Chem.

261

13203-13209

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

438923

-

Soluble methane monooxygenase from Methylococcus capsulatus Bath

1990

Pilkington, S.J.; Dalton, H.

Methods Enzymol.

188

181-190

439194

3011801

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

1986

Majamaa, K.; Gunzler, V.; Hanauske-Abel, H.M.; Myllylä, R.; Kivirikko, K.I.

J. Biol. Chem.

261

7819-7823

439733

11557069

Characterization of peroxidase-mediated chlorophyll bleaching in strawberry fruit

2001

Martinez, G.A.; Civello, P.M.; Chaves, A.R.; Anon, M.C.

Phytochemistry

58

379-387

439882

6825839

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

1983

Han, M.H.; Seong, B.L.; Son, H.J.; Mheen, T.I.

FEBS Lett.

151

36-40

439884

-

Enzymatic oxidation of rifamycins by a microorganism of the genus Humicola

1985

Seong, B.L.; Son, H.J.; Mheen, T.I.; Park, Y.H.; Han, M.H.

J. Ferment. Technol.

63

515-522

439889

-

Ascorbic acid oxidase

1963

Stark, G.R.; Dawson, C.R.

The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbäck, K. , eds. )

8

297-311

439995

3017970

Purification of a three-subunit ubiquinol-cytochrome c oxidoreductase complex from Paracoccus denitrificans [published erratum appears in J Biol Chem 1986 Nov 25;261(33):15813]

1986

Yang, X.; Trumpower, B.L.

J. Biol. Chem.

261

12282-12289

440010

2548618

The Rhodospirillum rubrum cytochrome bc1 complex: peptide composition, prosthetic group content and quinone binding

1989

Kriauciunas, A.; Yu, L.; Yu, C.A.; Wynn, R.M.; Knaff, D.B.

Biochim. Biophys. Acta

976

70-76

440012

2161250

Large-scale purification and characterization of a highly active four-subunit cytochrome bc1 complex from Rhodobacter sphaeroides

1990

Andrews, K.M.; Crofts, A.R.; Gennis, R.B.

Biochemistry

29

2645-2651

440015

2163487

Cytochrome bc1 complexes of microorganisms

1990

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101-129

484925

9142745

Purification and properties of alcohol oxidase from Candida methanosorbosa M-2003

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Curr. Microbiol.

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374-377

488919

14298833

Studies on adenosine diphosphate D-glucose:alpha-(1-4)-glucan alpha4-glucosyltransferase of sweet-corn endosperm

1965

Frydman, R.B.; Cardini, C.E.

Biochim. Biophys. Acta

96

294-303

489039

6066291

beta-1,3-Oligoglucan:orthophosphate glucosyltransferases from Euglena gracilis. I. Isolation and some properties of a beta-1,3-oligoglucan phosphorylase

1967

Marechal, L.R.

Biochim. Biophys. Acta

146

417-430

489040

6066292

beta-1,3-Oligoglucan: orthophosphate glucosyltransferases from Euglena gracilis. II. Comparative studies between laminaribiose- and beta-1,3-oligoglucan phosphorylase

1967

Marechal, L.R.

Biochim. Biophys. Acta

146

431-442

489101

-

Phenol beta-glucosyltransferases in six species of insects: Properties and tissue localization

1993

Ahmad, S.A.; Hopkins, T.L.

Comp. Biochem. Physiol. B

104B

515-519

489104

11846783

Characterization of a novel silkworm (Bombyx mori) phenol UDP-glucosyltransferase

2002

Luque, T.; Okano, K.; O'Reilly, D.R.

Eur. J. Biochem.

269

819-825

489458

4416442

The purification and properties of a uridine diphosphate glucose: aldehyde cyanohydrin beta-glucosyltransferase from sorghum seedlings

1974

Reay, P.F.; Conn, E.E.

J. Biol. Chem.

249

5826-5830

489572

-

UDP-D-glucose:flavonol 3-O- and 7-O-glucosyl transferases from young leaves of Paederia seandens var. mairei

1993

Ishikura, N.; Yang, Z.Q.; Teramoto, S.

Z. Naturforsch. C

48

563-569

636332

-

Further observations on the magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase system

1993

Whyte, B.J.; Castelfranco, P.A.

Biochem. J.

290

355-359

636380

-

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

1984

Tremolieres, M.; Bieth, J.G.

Phytochemistry

23

501-505

636399

-

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

1978

Chaplin, M.F.

Phytochemistry

17

1897-1899

636452

-

Phenoloxidase activity and its role in cuticular sclerotization in a mole crab Emerita asiatica Milne Edwards

1982

Nellaiappan, K.; Thangaraj, T.; Ramalingam, K.

J. Exp. Mar. Biol. Ecol.

61

75-83

639224

201619

Properties of 2-nitropropane dioxygenase of Hansenula mrakii. Formation and participation of superoxide

1978

Kido, T.; Soda, K.; Asada, K.

J. Biol. Chem.

253

226-232

644618

6959993

Preparation of bovine milk xanthine oxidase as a dehydrogenase form

1982

Nakamura, M.; Yamazaki, I.

J. Biochem.

92

1279-1286

644661

10336636

Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica

1999

Rhee, S.K.; Fuchs, G.

Eur. J. Biochem.

262

507-515

645642

447677

Phenol sulfotransferases

1979

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

J. Biol. Chem.

254

5658-5663

655362

-

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

2002

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

Enzyme Microb. Technol.

30

161-168

655375

-

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

2003

Saito, T.; Hong, P.; Kato, K.; Okazaki, M.; Inagaki, H.; Maeda, S.; Yokogawa, Y.

Enzyme Microb. Technol.

33

520-526

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

655631

14757242

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

2004

Sulistyaningdyah, W.T.; Ogawa, J.; Tanaka, H.; Maeda, C.; Shimizu, S.

FEMS Microbiol. Lett.

230

209-214

655940

14536026

Molecular cloning and characterization of an NADPH quinone oxidoreductase from Kluyveromyces marxianus

2003

Kim, W.H.; Chung, J.H.; Back, J.H.; Choi, J.; Cha, J.H.; Koh, H.Y.; Han, Y.S.

J. Biochem. Mol. Biol.

36

442-449

658136

14606947

Hybrid Mn-peroxidase from the ligninolytic fungus Panus tigrinus 8/18. Isolation, substrate specificity, and catalytic cycle

2003

Lisov, A.V.; Leontievsky, A.A.; Golovleva, L.A.

Biochemistry

68

1027-1035

658631

12542702

Probing suggested catalytic domains of glycosyltransferases by site-directed mutagenesis

2003

Hefner, T.; Stockigt, J.

Eur. J. Biochem.

270

533-538

658983

15161286

Ferrous binding to the multicopper oxidases Saccharomyces cerevisiae Fet3p and human ceruloplasmin: Contributions to Ferroxidase Activity

2004

Quintanar, L.; Gebhard, M.; Wang, T.P.; Kosman, D.J.; Solomon, E.I.

J. Am. Chem. Soc.

126

6579-6589

659524

12684851

Targeted suppression of the ferroxidase and iron trafficking activities of the multicopper oxidase Fet3p from Saccharomyces cerevisiae

2003

Wang, T.P.; Quintanar, L.; Severance, S.; Solomon, E.I.; Kosman, D.J.

J. Biol. Inorg. Chem.

8

611-620

660488

12437216

Characterization of manganese-dependent peroxidase isoenzymes from the ligninolytic fungus Phanerochaete flavido-alba

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