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Ligand 2-chloro-1,4-benzoquinone

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.99.29

D-glucose + 2-chloro-1,4-benzoquinone = ?

724070

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

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.167

2-chloro-4-nitrophenol + NADPH + H+ + O2 = 2-chloro-1,4-benzoquinone + nitrite + NADP+ + H2O

0

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Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Substrate (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.10

2-chloro-1,4-benzoquinone + O2 = ? + H2O2

699081

-

1.1.3.10

D-glucose + 2-chloro-1,4-benzoquinone = ?

724062

-

1.1.3.10

2 entries

1.1.99.29

D-glucose + 2-chloro-1,4-benzoquinone = ?

686685, 710969, 724070, 687883

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1.6.5.6

NADPH + H+ + chloro-1,4-benzoquinone = NADP+ + chlorohydroquinone

741687

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Product in Enzyme-catalyzed Reactions (8 results)

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Show Product (8 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.3

chlorohydroquinone + O2 = chloroquinone + H2O

439928

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1.11.1.16

2-chloro-1,4-dimethoxybenzene + H2O2 = 2-chloro-1,4-benzoquinone + H2O

0

-

1.14.13.167

2-chloro-4-nitrophenol + NADPH + H+ + O2 = 2-chloro-1,4-benzoquinone + nitrite + NADP+ + H2O

0

-

1.14.14.173

2,4-dichlorophenol + FADH2 + O2 = 2-chlorobenzoquinone + Cl- + FAD + H2O

0

-

1.14.14.173

2-chloro-4-bromophenol + FADH2 + O2 = 2-chlorobenzoquinone + Br- + FAD + H2O

0

-

1.14.14.173

2-chloro-4-nitrophenol + FADH2 + O2 = 2-chlorobenzoquinone + NO2- + FAD + H2O

0

-

1.14.14.173

3,4-dichlorophenol + FADH2 + O2 = 3-chlorobenzoquinone + Cl- + FAD + H2O

0

-

1.14.14.173

4 entries

1.8.5.7

glutathione + (glutathione-S-yl)-2-chloro-1,4-benzoquinone = glutathione disulfide + 2-chloro-1,4-benzoquinone

0

-

Inhibitor in Enzyme-catalyzed Reactions (4 results)

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Show Inhibitors (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.16.1.2

-

440098

-

3.4.24.69

-

733502

-

3.4.24.69

7% inhibition at 0.02 mM

734450

-

3.4.24.69

2 entries

6.5.1.2

-

710492

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.3.10

0.15

-

substrate 2-chloro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5

699081

1.1.3.10

16.3

-

pH 6.5, 30°C, recombinant enzyme

724062

1.1.99.29

12.9

-

recombinant enzyme, at pH 5.0 and 30°C

724070

1.1.99.29

12.9

-

recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0

710969

1.1.99.29

15.1

-

native enzyme, at pH 5.0 and 30°C

724070

1.1.99.29

15.1

-

native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0

710969

1.1.3.10

2 entries

1.1.99.29

4 entries

K_M Value (8 results)

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Show KM Value (8 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.3.10

0.31

-

substrate 2-chloro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5

699081

1.1.3.10

0.48

-

pH 6.5, 30°C, recombinant enzyme

724062

1.1.99.29

0.55

-

at 30°C with 50 mM glucose as susbtrate

687883

1.1.99.29

0.55

-

native enzyme, at pH 5.0 and 30°C

724070

1.1.99.29

0.55

-

native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0

710969

1.1.99.29

0.61

-

recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0

710969

1.1.99.29

0.62

-

recombinant enzyme, at pH 5.0 and 30°C

724070

1.1.99.29

1.6

-

at 30°C with 25 mM glucose as susbtrate

686685

1.1.3.10

2 entries

1.1.99.29

6 entries

References & Links

Literature References (12)

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Show Reference (12 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

439928

-

Ascorbate oxidase: Specificity and analytical application

1993

Sereikaite, J.; Iljaseviciene, D.; Dienys, G.; Danilcenko, H.; Gavrilova, V.

Appl. Biochem. Biotechnol.

43

153-160

440098

3680232

NADH diferric transferrin reductase in liver plasma membrane

1987

Sun, I.L.; Navas, P.; Crane, F.L.; Morre, D.J.; Löw, H.

J. Biol. Chem.

262

15915-15921

686685

17227387

Properties of pyranose dehydrogenase purified from the litter-degrading fungus Agaricus xanthoderma

2007

Kujawa, M.; Volc, J.; Halada, P.; Sedmera, P.; Divne, C.; Sygmund, C.; Leitner, C.; Peterbauer, C.; Haltrich, D.

FEBS J.

274

879-894

687883

18083263

Characterization of pyranose dehydrogenase from Agaricus meleagris and its application in the C-2 specific conversion of D-galactose

2008

Sygmund, C.; Kittl, R.; Volc, J.; Halada, P.; Kubatova, E.; Haltrich, D.; Peterbauer, C.K.

J. Biotechnol.

133

334-342

699081

19501263

Pyranose 2-oxidase from Phanerochaete chrysosporium--expression in E. coli and biochemical characterization

2009

Pisanelli, I.; Kujawa, M.; Spadiut, O.; Kittl, R.; Halada, P.; Volc, J.; Mozuch, M.D.; Kersten, P.; Haltrich, D.; Peterbauer, C.

J. Biotechnol.

142

97-106

710492

20214650

Toward the virtual screening of potential drugs in the homology modeled NAD+ dependent DNA ligase from Mycobacterium tuberculosis

2010

Singh, V.; Somvanshi, P.

Protein Pept. Lett.

17

269-276

710969

19888575

Heterologous expression of an Agaricus meleagris pyranose dehydrogenase-encoding gene in Aspergillus spp. and characterization of the recombinant enzyme

2010

Pisanelli, I.; Kujawa, M.; Gschnitzer, D.; Spadiut, O.; Seiboth, B.; Peterbauer, C.

Appl. Microbiol. Biotechnol.

86

599-606

724062

21968652

Heterologous expression and biochemical characterization of novel pyranose 2-oxidases from the ascomycetes Aspergillus nidulans and Aspergillus oryzae

2012

Pisanelli, I.; Wuehrer, P.; Reyes-Dominguez, Y.; Spadiut, O.; Haltrich, D.; Peterbauer, C.

Appl. Microbiol. Biotechnol.

93

1157-1166

724070

22080342

Simple and efficient expression of Agaricus meleagris pyranose dehydrogenase in Pichia pastoris

2012

Sygmund, C.; Gutmann, A.; Krondorfer, I.; Kujawa, M.; Glieder, A.; Pscheidt, B.; Haltrich, D.; Peterbauer, C.; Kittl, R.

Appl. Microbiol. Biotechnol.

94

695-704

733502

24984937

Benzoquinones as inhibitors of botulinum neurotoxin serotype A

2014

Bremer, P.; Hixon, M.; Janda, K.

Bioorg. Med. Chem.

22

3971-3981

734450

23815186

4-amino-7-chloroquinolines: Probing ligand efficiency provides botulinum neurotoxin serotype a light chain inhibitors with significant antiprotozoal activity

2013

Opsenica, I.; Tot, M.; Gomba, L.; Nuss, J.; Sciotti, R.; Bavari, S.; Burnett, J.; Solaja, B.

J. Med. Chem.

56

5860-5871

741687

25085488

The gene cluster for para-nitrophenol catabolism is responsible for 2-chloro-4-nitrophenol degradation in Burkholderia sp. strain SJ98

2014

Min, J.; Zhang, J.J.; Zhou, N.Y.

Appl. Environ. Microbiol.

80

6212-6222

Links to other databases for 2-chloro-1,4-benzoquinone

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Show Links (1 entry)

ChEBI

PubChem

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