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Ligand quinolin-8-ol

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Substrate (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.12.16

8-Hydroxyquinoline + NADH + O2 = ?

7068

-

1.3.99.17

8-hydroxyquinoline + acceptor + H2O = ?

673205

-

1.3.99.17

8-hydroxyquinoline + acceptor = ?

12570, 12571

-

2.4.1.17

8-hydroxyquinoline + UDPglucuronate = UDP + 8-hydroxyquinoline 8-O-glucuronide

488745

-

2.4.1.17

UDP-glucuronate + 8-hydroxyquinoline = UDP + 8-hydroxyquinoline beta-D-glucuronide

657537

-

1.3.99.17

2 entries

2.4.1.17

2 entries

2.4.1.218

UDP-glucose + 8-hydroxyquinoline = UDP + 8-hydroxyquinolin-beta-D-glucoside

658631

-

3.4.24.27

oxyquinoline + H2O = ?

699468

-

Activator in Enzyme-catalyzed Reactions (16 results)

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Show Activating Compound (16 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.6

1 mM, slight activation

636292

-

1.1.3.18

1 mM, relative activity 110%

348181

-

1.12.98.4

-

437779

-

1.13.11.2

-

724157

-

1.13.11.20

slight activation at 0.01 mM

439546

-

1.14.11.2

stimulates if it reaches an equimolar concentration with Fe2+

439198

-

1.2.3.4

0.4 mM concentration 400% activation

288394

-

1.7.2.6

1.5fold stimulation at 0.1 mM

394347

-

1.7.99.1

5% stimulation at 1 mM

394269

-

3.1.3.11

activates

170768

-

3.1.3.2

1 mM, enhances 36%

134745

-

3.5.1.4

18% activation aat 1 mM

733127

-

4.1.2.42

1 mM, 5% activation

748886

-

5.2.1.5

118% activity at 3 mM

714537

-

5.4.2.3

metal chelator required

3300

-

6.2.1.5

5 mM, enhances activity

805

-

Inhibitor in Enzyme-catalyzed Reactions (208 results)

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Show Inhibitors (208 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.107

-

80781

-

1.1.1.107

1 mM, 78% inhibition

655029

-

1.1.1.112

1 mM, 84% inhibition, 0.1 mM, 40% inhibition

285762

-

1.1.1.112

competitive inhibition vs. indanol

285758

-

1.1.1.107

2 entries

1.1.1.112

2 entries

1.1.1.14

-

285889

-

1.1.1.156

complete inhibition at 10 mM

286040

-

1.1.1.183

50% decrease at 0.67 mM

286130

-

1.1.1.184

1mM, 45% residual activity

725727

-

1.1.1.198

57% inhibition at 1 mM

286163

-

1.1.1.202

-

389488

-

1.1.1.6

-

636287

-

1.1.1.6

-

636293

-

1.1.1.6

1 mM, 10 mM

636292

-

1.1.1.6

3 entries

1.1.1.71

1 mM, 100% inhibition with NAD+ as cofactor, 40% with NADP+ as cofactor

287280

-

1.1.1.75

nearly complete inhibition at 2.5 mM

287299

-

1.1.1.B3

2 mM, 18% residual activity

689823

-

1.1.1.B4

1 mM, 55% residual activity

687864

-

1.1.3.10

-

389640

-

1.1.3.10

13.3% inhibition

389640

-

1.1.3.10

weak inhibitor

389635

-

1.1.3.10

3 entries

1.1.3.13

1 mM, 6% inhibition

484911

-

1.1.3.15

5-17% inhibition at 1 mM

389694

-

1.1.3.15

50% inhibition at 0.05 mM

389675

-

1.1.3.15

8-17% inhibition at 1 mM

389698

-

1.1.3.15

3 entries

1.1.3.19

-

389729

-

1.1.3.39

50% inhibition at 2 mM

287628

-

1.1.3.4

-

389828

-

1.1.3.4

11% inhibition at 10 mM

389806

-

1.1.3.4

2 entries

1.1.3.49

1 mM, 56% residual activity

739691

-

1.1.3.6

1 mM, 30 min at 4°C, 20% inhibition

656321

-

1.1.3.6

1 mM, 30 min at 4°C, 29% inhibition

656316

-

1.1.3.6

2 entries

1.1.3.9

1 mM, 50% inhibition

687852

-

1.1.3.B4

7.9% inhibition at 1 mM

738559

-

1.1.99.14

80% residual activity at 1 mM

725738

-

1.10.3.1

-

440427

-

1.10.3.2

-

396379

-

1.10.3.2

70% inhibition at 1 mM

396381

-

1.10.3.3

-

439889

-

1.10.3.3

1 mM, 42% inhibition of enzyme from soluble fraction

439893

-

1.10.3.2

2 entries

1.10.3.3

2 entries

1.10.3.4

-

713565

-

1.13.11.15

-

439614

-

1.13.11.15

no inhibition

439605

-

1.13.11.17

0.001 mM, 48% inhibition

395578

-

1.13.11.17

0.5 mM, 40% inhibition

395577

-

1.13.11.15

2 entries

1.13.11.17

2 entries

1.13.11.19

complete inhibition at 7.5 mM

396415

-

1.13.11.2

weak

439563

-

1.13.11.20

59% inhibition at 0.1 mM

439546

-

1.13.11.20

with protein-A: 100% inhibition at 0.1 mM, without protein-A: 99% inhibition at 0.1 mM

439548

-

1.13.11.24

-

439533

-

1.13.11.24

at 1 mM or more

439531

-

1.13.11.25

-

439527

-

1.13.11.25

1 mM, 90% inhibition after 10 min, noncompetitive inhibition

396333

-

1.13.11.20

2 entries

1.13.11.24

2 entries

1.13.11.25

2 entries

1.13.11.28

reversible by addition of Cu2+

439515, 439516

-

1.13.11.31

1 mM, 35% inhibition

395417

-

1.13.11.34

0.01 mM, 59% inhibition

439461

-

1.13.11.39

5 mM 30 min

439414

-

1.13.11.41

-

724599

-

1.13.11.52

-

712694

-

1.13.11.55

Fe3+-specific chelator, strong inhibition

697350

-

1.13.11.56

-

698537

-

1.13.11.63

-

713952

-

1.13.11.88

1 mM, 90% loss of activity

749754

-

1.13.12.16

strong inhibition

639223

-

1.13.12.2

-

440277

-

1.13.12.9

slight

439318

-

1.13.99.1

-

6866, 6874

-

1.14.11.2

inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture

439198

-

1.14.13.25

-

438922

-

1.14.13.25

compound C not inhibited

438938

-

1.14.13.35

23% inhibition at 0.5 mM, 37% inhibition at 1 mM

438873

-

1.14.13.35

30% inhibition at 0.5 mM, 40% inhibition at 1 mM

438867

-

1.14.13.35

37% inhibition at 1 mM

438877

-

1.14.13.25

2 entries

1.14.13.35

3 entries

1.14.13.69

-

285340

-

1.14.14.21

-

736522

-

1.14.14.22

88% inhibition at 1 mM

736529

-

1.14.14.92

5 mM, complete inhibition

440256

-

1.14.15.24

5% residual activity at 1 mM

714293

-

1.14.15.3

1 mM, 2 min 100% inhibition

285362

-

1.14.15.3

no inhibition

285373

-

1.14.15.3

2 entries

1.14.16.1

-

438714

-

1.14.16.4

-

438658, 438661

-

1.14.16.5

-

438648

-

1.14.16.5

1.0 mM, 15% inhibition, reaction with RS-batyl alcohol and 6-methyl-5,6,7,8-tetrahydropterin; reaction with RS-batyl alcohol and 6-methyl-5,6,7,8-tetrahydropterin

438651

-

1.14.16.5

2 entries

1.14.16.6

0.5 mM, 60% inhibition

639294

-

1.14.17.4

-

639299

-

1.14.18.1

1.3 mM, 50% inhibition

636403

-

1.14.18.1

3 mM, 44% inhibition

636338

-

1.14.18.1

2 entries

1.14.19.22

76% residual activity at 1 mM

731267

-

1.14.99.1

-

438389

-

1.14.99.15

-

438348, 438350

-

1.14.99.24

-

438296

-

1.17.4.1

-

437918

-

1.18.1.1

-

437860

-

1.2.1.39

34% inhibition in the presence of 1 mM

690567

-

1.2.1.46

-

288245, 288250

-

1.2.3.1

1 mM, 20% residual activity

740776

-

1.2.3.4

0.1 mM concentration 41% inhibition

288392

-

1.2.3.4

0.5 mM concentration 56% activity retained

288389, 288390

-

1.2.3.4

2 entries

1.3.1.119

1 mM, 54% inhibition

746932

-

1.3.1.29

16.7 mM, 25% inhibition

390641

-

1.3.1.57

enzyme preincubated with the inhibitor, 0.00166 mM, for 60 min at room temperature before the addition of the substrate, 83% inhibition

288478

-

1.3.99.5

1 mM, 10% inhibition

391383

-

1.4.3.2

2% residual activity at 1 mM

742930

-

1.4.3.2

70.07% inhibition at 10 mM

743071

-

1.4.3.2

76% residual activity at 1 mM (pH 5.5)

725575

-

1.4.3.21

0.0075 mM, 27% inhibition

391908

-

1.4.3.21

non-competitive inhibitor; non-competitive inhibitor; non-competitive inhibitor

724675

-

1.4.3.21

strong inhibition at 1 mM

742933

-

1.4.3.22

1 mM, 49.3% inhibition

391947

-

1.4.3.22

10 mM, 24% inhibition

656323

-

1.4.3.22

-

391959

-

1.4.3.2

3 entries

1.4.3.21

3 entries

1.4.3.22

3 entries

1.4.3.4

reversible by the addition of Zn2+, Ni2+, Co2+

394548

-

1.4.9.1

slight

396576

-

1.4.9.2

33% inhibition at 1 mM

655062

-

1.5.1.48

1 mM, 94% inhibition

724593

-

1.5.3.15

1 mM, slight inhibition

694075

-

1.5.99.4

77% inhibition at 5 mM

392542

-

1.6.5.10

0.3 mM, 80% inhibition

394367

-

1.6.5.2

1 mM, 50% inhibition

394350

-

1.6.5.4

10 mM, 15% inhibition

392751

-

1.6.5.6

0.1 mM

288624

-

1.7.1.10

-

394440

-

1.7.1.10

0.1 mM, 50% inhibition of hydroxylamine reductase activity

392937

-

1.7.1.10

1 mM, complete inhibition

394439

-

1.7.1.3

-

395975

-

1.7.1.3

94% inhibition at 10 mM

395970

-

1.7.1.3

pH 7.5, 20% inhibition at 0.1 mM

395968

-

1.7.1.4

-

392931, 392935

-

1.7.1.4

1 mM, 96% inhibition

392937

-

1.7.1.10

3 entries

1.7.1.3

3 entries

1.7.1.4

2 entries

1.7.2.6

50% inhibition at 0.2 mM

394330

-

1.7.3.2

-

395021

-

1.7.7.1

7% inhibition at 5 mM

394413

-

1.8.1.2

-

392973

-

2.1.1.11

-

485101

-

2.3.1.150

0.1 mM, 85% inhibition

16324

-

2.3.2.5

time-dependent inactivation

671982

-

2.4.1.34

-

489074

-

2.5.1.34

-

637461, 637463

-

2.7.7.12

inactivation of the enzyme by chelation of Zn2+ and Fe2+ ions

642853

-

3.1.1.1

-

651369

-

3.1.1.20

47.2% residual activity at 1 mM

691358

-

3.1.1.25

at 2 mM, 50% residual activity

650606

-

3.1.2.7

-

81019

-

3.1.21.2

inhibits cleavage of alkylated dsDNA

665452

-

3.1.3.1

-

94596

-

3.1.3.11

-

170771

-

3.1.3.15

-

170822

-

3.1.3.6

-

95076

-

3.1.4.17

2 mM, 28% residual activity

728995

-

3.2.2.1

1 mM, 93% inhibition

654255

-

3.4.11.10

-

732189

3vh9, 3D-view

3.4.11.14

2.0 mM, 84% inhibition

647035

-

3.4.11.18

-

717326

-

3.4.11.2

-

666240

-

3.4.11.2

91% inhibition at 3 mM

35876

-

3.4.11.2

2 entries

3.4.11.3

-

35900, 35908

-

3.4.11.6

-

35984

-

3.4.11.9

-

36047

-

3.4.15.1

-

81242

-

3.4.17.1

-

706874

-

3.4.17.6

100% inhibition at 1 mM

81313

-

3.4.19.3

-

95281, 95282, 95299

-

3.4.19.6

10 mM, 68% inhibition

95299

-

3.4.24.27

-

699468

-

3.4.24.3

-

37105

-

3.4.24.36

Zn2+ reverses, bovine serum albumin as substrate

31226

-

3.4.24.40

0.1 mM at pH 10, 5 mM at pH 7

31243

-

3.5.1.11

complexed with zinc, reactivation by addition of ZnSO4, MnSO4, MgSO4, CoSO4, FeSO4

171888

-

3.5.1.13

-

208980

-

3.5.1.19

-

246567

-

3.5.1.32

60% inhibition at 3.3 mM

172036

-

3.5.1.48

slight inhibition at 1 mM

172046

-

3.5.1.56

-

209201

-

3.5.1.6

1 mM, 29% inhibition

657030

-

3.5.1.6

2 mM 100% inhibition

172065

-

3.5.1.6

2 entries

3.5.1.62

very slight inhibition, 1 mM: 2% inhibition

172070

-

3.5.1.87

2 mM, 65% inhibition

288945

-

3.5.1.88

50% inhibition at 2 mM

393806

-

3.5.1.91

54% inhibition

660362

-

3.5.1.91

84% inhibition at 1 mM

733172

-

3.5.1.91

2 entries

3.5.1.98

85% residual activity at 0.5 mM

711439

-

3.5.2.1

2 mM, 60% inhibition

652350

-

3.5.2.14

1 mM

246616

-

3.5.2.16

5 mM, 9.4% residual activity

711007

-

3.5.2.2

-

209273, 209283

-

3.5.2.3

-

246629

-

3.5.3.2

-

209441

-

3.5.5.1

36% inhibition at 1 mM

209746

-

3.5.5.5

weak

32503

-

3.6.1.18

-

209916

-

4.1.1.34

Mn2+ or Mg2+ restore activity

4390

-

4.1.1.5

-

4651

-

4.1.1.92

1 mM, 49% inhibition

711507

-

4.1.2.13

-

692126

-

4.1.2.13

aldolase class II

4924

-

4.1.2.13

2 entries

4.1.99.5

strong

648392, 648393

-

4.2.1.103

26.1% inhibition at 1 mM

715552

-

4.2.1.24

-

210714

-

4.2.1.84

-

648440

-

4.3.1.2

5 mM, 44% loss of activity

6060

-

4.3.1.2

5 mM, 88% loss of activity

6060

-

4.3.1.2

58% loss of activity in the deamination reaction of L-threo-3-methylaspartate

6059

-

4.3.1.2

3 entries

4.3.1.24

-

34360

-

4.8.1.3

inhibition is partly reversed by ferric citrate, ascorbic acid and dehydroascorbic acid

648796

-

5.1.1.15

59% inhibition at 1 mM

748352

-

5.1.2.1

-

2174

-

5.3.1.5

above 5 mM

2751

-

5.3.1.8

-

2806

-

3D Structure of Enzyme-Ligand-Complex (PDB) (2 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (2 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.14.11.16

3kcy, 3D-view

3.4.11.10

3vh9, 3D-view

Enzyme Kinetic Parameters

K_M Value (5 results)

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Show KM Value (5 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.4.1.17

0.00048

-

isozyme UGT1A9, pH 7.4, 37°C

657537

2.4.1.17

0.0065

-

isozyme UGT1A6, pH 7.4, 37°C

657537

2.4.1.17

0.016

-

isozyme UGT2B15, pH 7.4, 37°C

657537

2.4.1.17

0.301

-

isozyme UGT2B7, pH 7.4, 37°C

657537

2.4.1.17

0.494

-

isozyme UGT1A3, pH 7.4, 37°C

657537

2.4.1.17

5 entries

K_i Value (6 results)

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Show KI Value (6 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.24

0.034

-

-

439531

1.4.3.22

20

-

-

391959

1.4.3.22

35

-

-

391959

1.4.3.22

2 entries

1.4.3.4

0.65

-

-

394548

3.4.11.10

0.00058

-

pH 8, 25°C

732189

3.4.24.27

0.214

-

25°C, pH 7.5

699468

IC₅₀ Value (7 results)

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Show IC50 Value (7 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.13.11.52

0.75

-

in potassium phosphate buffer (100 mM, pH 6.5) ascorbic acid (20 mM), catalase (200 units/ml), methylene blue (0.01 mM), at 37°C

712694

3.4.11.18

0.00077

-

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

717326

3.4.11.18

0.0056

-

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

717326

3.4.11.18

0.0183

-

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

717326

3.4.11.18

0.0215

-

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

717326

4.1.2.13

0.496

-

NADH-linked enzymatic assay

692126

4.1.2.13

0.5

-

determined by the colorimetric assay

692126

3.4.11.18

4 entries

4.1.2.13

2 entries

References & Links

Literature References (237)

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Show Reference (237 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

805

5166363

Porphyrin biosynthesis in soybean callus tissue system. VIII. Isolation, purification and general properties of succinyl CoA synthetase

1971

Wider, E.A.; Tigier, H.A.

Enzymologia

41

217-231

2174

5707819

Purification and properties of lactate racemase from Lactobacillus sake

1968

Hiyama, T.; Fukui, S.; Kitahara, K.

J. Biochem.

64

99-107

2751

-

Characterization of the purified extracellular D-xylose isomerase devoid of D-glucose isomerase from Chainia sp.

1990

Khire, J.M.; Lachke, A.H.; Srinivasan, M.C.; Vartak, H.G.

Appl. Biochem. Biotechnol.

23

41-52

2806

4969968

Studies on phosphomannose isomerase. II. Characterization as a zinc metalloenzyme

1968

Gracy, R.W.; Noltmann, E.A.

J. Biol. Chem.

243

4109-4116

3300

4996162

Purification and properties of phosphoglucosamine mutase

1971

Fernandez-Sorensen, A.; Carlson, D.M.

J. Biol. Chem.

246

3485-3493

4390

-

Catabolism of L-ascorbate in animal tissues

1970

Kagawa, Y.; Shimazono, N.

Methods Enzymol.

18

46-50

4651

-

Purification and characterization of alpha-acetolactate decarboxylase from Brevibacterium acetylicum

1989

Oshiro, T.; Aisaka, K.; Uwajima, T.

Agric. Biol. Chem.

53

1913-1918

4924

6818421

Fructose-bisphosphate aldolases from Mycobacteria

1982

Jayanthi Bai, N.; Ramachandra Pai, M.; Suryanarayana Murthy, P.; Venkitasubramanian, T.A.

Methods Enzymol.

90

241-250

6059

7576557

3-Methylaspartate ammonia-lyase from a facultative anaerobe, strain YG-1002

1995

Kato, Y.; Asano, Y.

Appl. Microbiol. Biotechnol.

43

901-907

6060

7765982

Purification and properties of crystalline 3-methylaspartase from two facultative anaerobes, Citrobacter sp. strain YG-0504 and Morganella morganii strain YG-0601

1995

Kato, Y.; Asano, Y.

Biosci. Biotechnol. Biochem.

59

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