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Ligand hexanoyl-CoA

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for hexanoyl-CoA

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.8.1

hexanoyl-CoA + acceptor = hex-2-enoyl-CoA + reduced acceptor

712126

-

2.3.1.206

3 malonyl-CoA + hexanoyl-CoA = 3 CoA + 3,5,7-trioxododecanoyl-CoA + 3 CO2

719492, 756711, 720760, 706171, 720934

-

2.3.1.295

a medium-chain acyl-CoA + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = a mycoketide-CoA + 10 CO2 + 10 CoA + 22 NADP+ + 11 H2O

754298, 755058

-

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.38

trans-2-hexenoyl-CoA + NADPH + H+ = hexanoyl-CoA + NADP+

0

-

1.3.8.1

2-hexenoyl-CoA + reduced electron transfer flavoprotein = hexanoyl-CoA + electron transfer protein

391284

-

Substrate in Enzyme-catalyzed Reactions (82 results)

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Show Substrate (82 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.11.18

hexanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyhexanoyl-CoA + succinate + CO2

658428

-

1.2.1.76

n-hexanoyl-CoA + NADPH + H+ = caproaldehyde + coenzyme A + NADP+

697694

-

1.3.1.10

hexanoyl-CoA + NADH + H+ = ?

740013

-

1.3.1.85

hexanoyl-CoA + NADPH + H+ = ?

724588

-

1.3.3.6

hexanoyl-CoA + O2 = (2E)-hex-2-enoyl-CoA + H2O2

685352, 391069, 391060, 391066, 391065

-

1.3.8.1

hexanoyl-CoA + acceptor = 2-hexenoyl-CoA + reduced acceptor

654618

-

1.3.8.1

hexanoyl-CoA + acceptor = hex-2-enoyl-CoA + reduced acceptor

712126

-

1.3.8.1

hexanoyl-CoA + electron acceptor = 2-hexenoyl-CoA + reduced acceptor

686920, 673718

-

1.3.8.1

hexanoyl-CoA + electron transfer flavoprotein = 2-hexenoyl-CoA + reduced acceptor

391201, 672004, 391282

-

1.3.8.1

hexanoyl-CoA + FAD = hex-2-enoyl-CoA + FADH2

712126

-

1.3.8.1

hexanoyl-CoA + phenazine methosulfate + dichloroindophenol = 2-hexenoyl-CoA + reduced acceptor

391201, 391272, 391269, 391283, 391203, 391274, 391275, 391300

-

1.3.8.4

hexanoyl-CoA + acceptor = hex-2-enoyl-CoA + reduced acceptor

391219, 656288, 391218, 391201, 391209

-

1.3.8.4

hexanoyl-CoA + electron-transfer flavoprotein = hex-2-enoyl-CoA + reduced electron-transfer flavoprotein

724512

-

1.3.8.1

6 entries

1.3.8.4

2 entries

1.3.8.5

hexanoyl-CoA + electron-transfer flavoprotein = hex-2-enoyl-CoA + reduced electron-transfer flavoprotein

656288, 656162

-

1.3.8.6

hexanoyl-CoA + acceptor = ? + reduced acceptor

391408, 391418, 391419

-

1.3.8.7

hexanoyl-CoA + 2,6-dichloroindophenol = 2-hexenoyl-CoA + reduced 2,6-dichloroindophenol

685352

-

1.3.8.7

hexanoyl-CoA + 2,6-dichlorophenolindophenol = trans-hex-2-enoyl-CoA + reduced 2,6-dichlorophenolindophenol

391283

-

1.3.8.7

hexanoyl-CoA + acceptor = 2-hexenoyl-CoA + reduced acceptor

391343, 688185, 391282, 391203, 391201, 687009

-

1.3.8.7

hexanoyl-CoA + electron transfer flavoprotein = (2E)-2-hexenoyl-CoA + reduced electron transfer flavoprotein

674476

-

1.3.8.7

hexanoyl-CoA + ferricenium = trans-hex-2-enoyl-CoA + ferrocenium

391370

-

1.3.8.7

hexanoyl-CoA + ferricenium hexafluorophosphate = trans-hex-2-enoyl-CoA + ferrocenium hexafluorophosphate

391367

-

1.3.8.7

hexanoyl-CoA + ferrocenium hexafluorophosphate = trans-hex-2-enoyl-CoA + reduced ferrocenium hexafluorophosphate

391367

-

1.3.8.7

hexanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol = 2-trans-hexenoyl-CoA + reduced acceptor

391203

-

1.3.8.7

hexanoyl-CoA + tetrazolium salt = trans-hex-2-enoyl-CoA + reduced tetrazolium salt

391275

-

1.3.8.8

hexanoyl-CoA + electron-transfer flavoprotein = 2-hexenoyl-CoA + reduced electron-transfer flavoprotein

391371, 391282, 394650

-

1.3.8.8

hexanoyl-CoA + Meldola's Blue = (2E)-2-hexenoyl-CoA + reduced meldola blue

391275

-

1.3.8.8

hexanoyl-CoA + phenazine methosulfate = 2-hexenoyl-CoA + reduced phenazine methosulfate

391282, 394667, 391268

-

1.3.8.7

9 entries

1.3.8.8

3 entries

2.3.1.111

hexanoyl-CoA + methylmalonyl-CoA + NADPH = ?

486135

-

2.3.1.118

hexanoyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole = CoA + N-hexanoyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole

486156

-

2.3.1.13

hexanoyl-CoA + glycine = CoA + N-hexanoylglycine

737197

-

2.3.1.137

hexanoyl-CoA + L-carnitine = CoA + L-hexanoylcarnitine

486290, 486291, 486295, 486292, 486305, 659372

-

2.3.1.150

n-Hexanoyl-CoA + salutaridinol = ?

16324

-

2.3.1.151

3 malonyl-CoA + hexanoyl-CoA = 4 CoA + 4-hydroxy-6-pentyl-2H-pyran-2-one + 5-hexanoyl-4-hydroxy-6-methyl-2H-pyran-2-one + 3 CO2

720639

-

2.3.1.159

3 malonyl-CoA + hexanoyl-CoA = 4 CoA + phloroglucinol + 3 CO2

736426

-

2.3.1.159

hexanoyl-CoA + malonyl-CoA = ? + CoA + CO2

673581

-

2.3.1.159

2 entries

2.3.1.16

hexanoyl-CoA + H2O = hexanoate + CoA

664215

-

2.3.1.165

hexanoyl-CoA + malonyl-CoA = 6-pentyl triacetic acid lactone + CoA

486451

-

2.3.1.180

hexanoyl-CoA + malonyl-[acyl-carrier protein] = 3-oxo-octanoyl-[acyl-carrier protein] + CoA + CO2

486937, 761373, 660466

-

2.3.1.19

hexanoyl-CoA + phosphate = CoA + hexanoyl phosphate

756087

-

2.3.1.19

hexanoyl-CoA + phosphate = hexanoyl phosphate + CoA

756087

-

2.3.1.19

2 entries

2.3.1.20

hexanoyl-CoA + 1,2-dipalmitoyl glycerol = coenzyme A + 1,2-dipalmitoyl-3-hexanoyl glycerol

486487

-

2.3.1.206

3 malonyl-CoA + hexanoyl-CoA = 3 CoA + 3,5,7-trioxododecanoyl-CoA + 3 CO2

719492, 756711, 720760, 706171, 720934

-

2.3.1.206

3 malonyl-CoA + hexanoyl-CoA = ?

720721

-

2.3.1.206

2 entries

2.3.1.21

hexanoyl-CoA + L-carnitine = CoA + L-hexanoylcarnitine

486565, 486528, 486526

-

2.3.1.220

3 malonyl-CoA + hexanoyl-CoA = 4 CoA + 4-hydroxy-6-pentyl-2H-pyran-2-one + 4-hydroxy-6-(2-oxoheptyl)-2H-pyran-2-one + 3 CO2

487479

-

2.3.1.233

hexanoyl-CoA + 2 malonyl-CoA = 4-hydroxy-6-pentyl-2H-pyran-2-one + CoA + CO2 + H2O

729966

-

2.3.1.233

hexanoyl-CoA = 4-hydroxy-6-pentyl-2-pyrone + 4-hydroxy-6-(2'-oxoheptyl)-2-pyrone + CoA + CO2 + H2O

729157, 729961

-

2.3.1.233

hexanoyl-CoA = ? + CoA + CO2 + H2O

729966

-

2.3.1.24

hexanoyl-CoA + sphingosine = CoA + N-hexanoylsphingosine

486668

-

2.3.1.24

sphingosine + hexanoyl-CoA = N-hexanoylsphingosine + CoA

754575

-

2.3.1.233

3 entries

2.3.1.24

2 entries

2.3.1.250

hexanoyl-CoA + [Wnt]-L-serine = CoA + [Wnt]-O-hexanoyl-L-serine

757228

-

2.3.1.253

hexanoyl-CoA = 4-hydroxy-6-pentyl-2H-pyran-2-one + 4-hydroxy-6-(2-oxoheptyl)-2H-pyran-2-one + CO2 + CoA

740681

-

2.3.1.273

hexanoyl-CoA + 2-O-[alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-D-glycerate = 2-O-[6-O-hexanoyl-alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-D-glycerate + CoA

749305

-

2.3.1.295

a medium-chain acyl-CoA + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = a mycoketide-CoA + 10 CO2 + 10 CoA + 22 NADP+ + 11 H2O

754298, 755058

-

2.3.1.301

hexanoyl-CoA + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CoA + CO2

761437

-

2.3.1.38

hexanoyl-CoA + [acyl-carrier protein] = CoA + hexanoyl-[acyl-carrier protein]

486864, 285675, 486863, 486865, 486866

-

2.3.1.47

hexanoyl-CoA + L-arginine = N-[(4S)-4-amino-5-oxodecyl]guanidine + CO2 + CoA

758497

-

2.3.1.67

hexanoyl-CoA + 1-alkyl-2-lyso-sn-glycero-3-phosphocholine = 2-hexanoyl-1-alkyl-sn-glycero-3-phosphocholine

487377

-

2.3.1.7

hexanoyl-CoA + carnitine = CoA + O-hexanoylcarnitine

659372, 672172

-

2.3.1.7

hexanoyl-CoA + carnitine = hexanoylcarnitine + CoASH

486295, 487406, 487408, 674651

-

2.3.1.7

hexanoyl-CoA + L-carnitine = CoA + O-hexanoyl-L-carnitine

487416

-

2.3.1.74

3 malonyl-CoA + hexanoyl-CoA = 4 CoA + ? + 3 CO2

719618

1chw, 3D-view

2.3.1.74

hexanoyl-CoA + malonyl-CoA = phlorocaprophenone + CoA + CO2

663042

1chw, 3D-view

2.3.1.74

hexanoyl-CoA + methylmalonyl-CoA = 4-hydroxy-3,5-dimethyl-6-pentyl-pyran-2-one + CoA + CO2

663006

1chw, 3D-view

2.3.1.74

malonyl-CoA + hexanoyl-CoA = 4-hydroxy-6-pentyl-2H-pyran-2-one + CoA + CO2

757938

1chw, 3D-view

2.3.1.74

malonyl-CoA + hexanoyl-CoA = ?

676378, 758097, 758151

1chw, 3D-view

2.3.1.74

malonyl-CoA + hexanoyl-CoA = phlorocaprophenone + CO2 + CoA

487467, 487480

1chw, 3D-view

2.3.1.74

(2RS)-methylmalonyl-CoA + n-hexanoyl-CoA = triketide lactone + 6-ethyl-4-hydroxy-3,5-dimethyl-2-pyrone

758097

1chw, 3D-view

2.3.1.74

n-hexanoyl-CoA + butyryl-CoA = phlorobutyrophenone + phlorocaprophenone

758097

1chw, 3D-view

2.3.1.84

hexanoyl-CoA + butanol = CoA + butyl hexanoate

719627

-

2.3.1.84

hexanoyl-CoA + cinnamyl alcohol = CoA + cinnamyl hexanoate

720138

-

2.3.1.84

hexanoyl-CoA + ethanol = CoA + ethyl hexanoate

719627

-

2.3.1.84

hexanoyl-CoA + methanol = CoA + methyl hexanoate

719627

-

2.3.1.7

3 entries

2.3.1.74

8 entries

2.3.1.84

4 entries

2.3.1.87

hexanoyl-CoA + histamine = CoA + N-hexanoylhistamine

735681

-

2.3.1.95

n-hexanoyl-CoA + malonyl-CoA = bisnoryangonin-type and p-coumaroyltriacetic acid lactone-type pyrones + CoA + CO2

487730

-

3.1.2.1

hexanoyl-CoA + H2O = CoA + hexanoate

651098

-

3.1.2.1

hexanoyl-CoA = hexanoate + CoA

94471

-

3.1.2.2

hexanoyl-CoA + H2O = CoA + hexanoate

646120, 646158, 646124, 646156, 646200, 679171, 646179, 646176

-

3.1.2.2

hexanoyl-CoA + H2O = CoA + n-hexanoate

646200

-

3.1.2.20

hexanoyl-CoA + H2O = CoA + hexanoate

707430, 646120, 646158, 646124, 646156, 646200, 690932, 698975, 646179, 646176, 731658

-

3.1.2.20

n-hexanoyl-CoA + H2O = CoA + n-hexanoate

707486

-

3.1.2.1

2 entries

3.1.2.2

2 entries

3.1.2.20

2 entries

3.1.2.25

hexanoyl-CoA + H2O = hexanoate + CoA

751066

-

Product in Enzyme-catalyzed Reactions (22 results)

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Show Product (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.10

hexylaldehyde + CoA + NAD+ = hexanoyl-CoA + NADH

0

-

1.2.1.57

hexanal + CoA + NAD+ = hexanoyl-CoA + NADH

0

-

1.2.1.76

caproaldehyde + coenzyme A + NADP+ = n-hexanoyl-CoA + NADPH + H+

0

-

1.3.1.10

trans-2-hexenoyl-CoA + NADPH = hexanoyl-CoA + NADP+

0

-

1.3.1.38

trans-2-hexenoyl-CoA + NADPH + H+ = hexanoyl-CoA + NADP+

0

-

1.3.1.38

trans-2-hexenoyl-CoA + NADPH = hexanoyl-CoA + NADP+

390748, 0, 390755, 390760

-

1.3.1.44

(E)-2-hexanoyl-CoA + NADPH = hexanoyl-CoA + NADP+

0

-

1.3.1.44

trans-2-hexenoyl-CoA + NAD(P)H = hexanoyl-CoA + NAD(P)+

0

-

1.3.1.44

trans-2-hexenoyl-CoA + NADH + H+ = hexanoyl-CoA + NAD+

0

-

1.3.1.38

2 entries

1.3.1.44

3 entries

1.3.1.8

2-trans-hexenoyl-CoA + NAD(P)H = hexanoyl-CoA + NADP+

0, 390755, 390756

-

1.3.8.1

2-hexenoyl-CoA + reduced electron transfer flavoprotein = hexanoyl-CoA + electron transfer protein

391284

-

2.3.1.137

L-hexanoylcarnitine + CoA = hexanoyl-CoA + L-carnitine

0

-

2.3.1.155

3-oxooctanoyl-CoA + CoA = acetyl-CoA + hexanoyl-CoA

0

-

2.3.1.16

CoA + 3-oxooctanoyl-CoA = acetyl-CoA + hexanoyl-CoA

0

-

2.3.1.7

hexanoylcarnitine + CoASH = hexanoyl-CoA + carnitine

0

-

2.8.3.1

acetyl-CoA + hexanoate = acetate + hexanoyl-CoA

0

-

6.2.1.1

ATP + hexanoate + CoA = AMP + diphosphate + hexanoyl-CoA

0

-

6.2.1.12

ATP + hexanoate + CoA = AMP + diphosphate + hexanoyl-CoA

0

-

6.2.1.13

ATP + hexanoate + CoA = ADP + phosphate + hexanoyl-CoA

0

-

6.2.1.2

ATP + hexanoate + CoA = AMP + diphosphate + hexanoyl-CoA

650831, 0, 649783, 649791, 650950, 650334

-

6.2.1.3

ATP + hexanoate + CoA = AMP + diphosphate + hexanoyl-CoA

0, 649789

-

6.2.1.44

ATP + hexanoate + CoA = AMP + diphosphate + hexanoyl-CoA

0

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

4.1.1.31

activates

4337

-

Inhibitor in Enzyme-catalyzed Reactions (10 results)

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Show Inhibitors (10 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.44

-

724351

-

1.3.8.5

-

12302

-

1.3.8.5

19% inhibition

391254

-

1.3.8.5

2 entries

2.3.1.273

0.12 mM, about 50% inhibition

749305

-

2.3.1.5

0.1 mM, 24% inhibition

657884

-

2.3.3.10

-

488091

-

2.7.11.2

-

642139

-

3.1.2.17

competitive inhibition

643853

-

4.2.1.149

0.1 mM, 43% inhibition

724139

-

6.4.1.4

weak

1896

-

3D Structure of Enzyme-Ligand-Complex (PDB) (9 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (9 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.1.1.100

3v1u, 3D-view

1.3.1.34

1w6u, 3D-view

1.3.1.34

4fc6, 3D-view

1.3.1.34

1w6u, 3D-view

1.3.1.34

4fc6, 3D-view

1.3.1.34

1w6u, 3D-view

1.3.1.34

4fc6, 3D-view

1.3.1.34

6 entries

2.3.1.74

1chw, 3D-view

4.2.1.17

1mj3, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (54 results)

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Show Turnover Number (54 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.1.44

15.3

-

pH and temperature not specified in the publication, mutant I287A

724351

1.3.1.44

19

-

pH and temperature not specified in the publication, mutant L276A/V277A

724351

1.3.1.44

22.4

-

pH and temperature not specified in the publication, mutant L276A/V277A/F295A

724351

1.3.1.44

48

-

pH and temperature not specified in the publication, mutant Y370A

724351

1.3.1.44

50

-

pH and temperature not specified in the publication, mutant L291A

724351

1.3.1.44

64

-

pH and temperature not specified in the publication, mutant F295A

724351

1.3.1.44

112

-

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

724351

1.3.3.6

0.089

-

in 50 mM phosphate buffer, pH 7.4, at 30°C

685352

1.3.3.6

0.203

-

-

391060

1.3.3.6

8.59

-

recombinant enzyme

391066

1.3.8.1

0.2992

-

-

673718

1.3.8.1

1.35

-

-

391269

1.3.8.1

10

-

32°C, pH 7.0

654618

1.3.8.1

16.5

-

-

391201

1.3.1.44

7 entries

1.3.3.6

3 entries

1.3.8.1

4 entries

1.3.8.4

0.533

-

using recombinant enzyme, electron acceptor: electron-transferring flavoprotein

391218

1.3.8.5

1200

-

mutant L222I/A383T, 32°C

656162

1.3.8.5

1800

-

wild-type enzyme, 32°C

656162

1.3.8.5

2000

-

mutant V104L/F105L, 32°C

656162

1.3.8.5

2500

-

mutant F105L, 32°C

656162

1.3.8.5

5800

-

mutant L220M/A383T, 32°C

656162

1.3.8.5

7400

-

deletion mutant M10, 32°C

656162

1.3.8.5

7600

-

wild-type enzyme, 32°C

656162

1.3.8.7

2.83

-

T255E mutant enzyme

391369

1.3.8.7

12.7

-

K304E mutant enzyme, ferricenium assay

391370

1.3.8.7

14.2

-

-

391367

1.3.8.7

16.8

-

-

391369

1.3.8.7

20.6

-

-

391367

1.3.8.7

20.8

-

ferricenium assay

391370

1.3.8.7

31.2

-

medium-chain acyl-CoA dehydrogenase

391272

2.3.1.13

4.6

-

apparent value, at pH 8.0, temperature not specified in the publication

737197

2.3.1.13

4.6

-

pH 8.0, temperature not specified in the publication

737197

2.3.1.180

8.1

-

pH 7.0, 30°C, recombinant enzyme

660466

2.3.1.180

25.5

41.7

pH 7.0, 30°C, recombinant enzyme

660466

2.3.1.19

47

-

pH 7.5, 23°C

756087

2.3.1.19

47

-

pH 7.5, 25°C

756087

1.3.8.5

7 entries

1.3.8.7

7 entries

2.3.1.13

2 entries

2.3.1.180

2 entries

2.3.1.19

2 entries

2.3.1.206

0.018

0.058

pH 5.5, 30°C, dependent on product formed

719492

2.3.1.233

0.6

-

wild type enzyme, at pH 7.5 and 30°C

729157

2.3.1.233

0.65

-

mutant enzyme Y224G, at pH 7.5 and 30°C

729157

2.3.1.233

1.45

-

mutant enzyme Y224L, at pH 7.5 and 30°C

729157

2.3.1.233

2.07

-

mutant enzyme A350I, at pH 7.5 and 30°C

729157

2.3.1.233

9

-

mutant enzyme A350S, at pH 7.5 and 30°C

729157

2.3.1.273

0.00017

-

37°C, pH 8.0, cosubstrate: 20 mM 2-O-(alpha-D-glucopyranosyl)-D-glycerate

749305

2.3.1.273

0.00067

-

37°C, pH 8.0, cosubstrate: 20 mM 2-O-[alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-D-glycerate

749305

2.3.1.7

1.42

-

21°C, pH 7.8, mutant enzyme S554A

674651

2.3.1.7

8.2

-

21°C, pH 7.8, mutant enzyme S554A/M564G

674651

2.3.1.7

30.4

-

21°C, pH 7.8, wild-type enzyme

674651

2.3.1.7

89

-

21°C, pH 7.8, mutant enzyme M564G

674651

2.3.1.7

104.7

-

21°C, pH 7.8, mutant enzyme M564G

674651

2.3.1.233

5 entries

2.3.1.273

2 entries

2.3.1.7

5 entries

2.3.1.74

0.147

-

pH 8.0, 30°C

663042

2.3.1.87

0.093

-

wild-type, pH 8.0, 22°C

735681

3.1.2.2

0.012

-

pH 7.5

679171

3.1.2.20

0.022

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

0.03

-

-

707430

3.1.2.20

15

-

pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay

690932

3.1.2.20

3 entries

K_M Value (88 results)

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Show KM Value (88 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.44

0.0034

-

pH and temperature not specified in the publication, mutant I287A

724351

1.3.1.44

0.007

-

pH and temperature not specified in the publication, mutant L276A/V277A

724351

1.3.1.44

0.012

-

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

724351

1.3.1.44

0.015

-

pH and temperature not specified in the publication, mutant L276A/V277A/F295A

724351

1.3.1.44

0.018

-

pH and temperature not specified in the publication, mutant Y370A

724351

1.3.1.44

0.019

-

pH and temperature not specified in the publication, mutant F295A

724351

1.3.1.44

0.038

-

pH and temperature not specified in the publication, mutant L291A

724351

1.3.3.6

0.006

-

isozyme SCOX

391069

1.3.3.6

0.02

-

isozyme AtSACX

391065

1.3.3.6

0.03

-

in 50 mM phosphate buffer, pH 7.4, at 30°C

685352

1.3.3.6

0.067

-

recombinant enzyme

391066

1.3.3.6

0.092

-

-

391060

1.3.8.1

0.0017

-

E368G/G247E double mutant enzyme

391307

1.3.8.1

0.0038

-

wild-type enzyme

391307

1.3.8.1

0.004

-

32°C, pH 7.0

654618

1.3.8.1

0.005

-

E368D mutant enzyme

391307

1.3.8.1

0.012

-

-

391283

1.3.8.1

0.02

-

-

391275

1.3.8.1

0.0339

-

-

391201

1.3.8.1

0.034

-

-

391047

1.3.8.1

0.053

-

-

391274

1.3.8.1

0.09303

-

-

673718

1.3.8.1

0.285

-

-

391272

1.3.8.4

0.02

-

-

391201

1.3.8.4

0.0338

-

-

391218

1.3.8.5

0.0053

-

mutant L220M/A383T, 32°C

656162

1.3.8.5

0.0055

-

mutant L222I/A383T, 32°C

656162

1.3.8.5

0.035

-

mutant F105L, 32°C

656162

1.3.8.5

0.036

-

wild-type enzyme, 32°C

656162

1.3.8.5

0.044

-

wild-type enzyme, 32°C

656162

1.3.8.5

0.057

-

deletion mutant M10, 32°C

656162

1.3.8.5

0.15

-

mutant V104L/F105L, 32°C

656162

1.3.1.44

7 entries

1.3.3.6

5 entries

1.3.8.1

11 entries

1.3.8.4

2 entries

1.3.8.5

7 entries

1.3.8.6

0.085

-

-

391419

1.3.8.7

0.0014

-

T255E mutant enzyme

391369

1.3.8.7

0.0035

-

-

391283

1.3.8.7

0.0036

-

-

391367

1.3.8.7

0.004

-

-

391275

1.3.8.7

0.005

-

-

391275

1.3.8.7

0.0068

-

-

391367

1.3.8.7

0.0075

-

K304E mutant enzyme, ferricenium assay

391370

1.3.8.7

0.008

-

-

391201

1.3.8.7

0.009

-

-

391370

1.3.8.7

0.0094

-

-

391272

1.3.8.7

0.015

-

-

391369

1.3.8.7

0.0216

-

-

391201

1.3.8.8

0.0063

-

-

391371

1.3.8.8

0.029

-

-

391371

1.3.8.8

0.55

-

-

391275

2.3.1.13

0.045

-

pH 8.0, temperature not specified in the publication

737197

2.3.1.13

450

-

apparent value, at pH 8.0, temperature not specified in the publication

737197

1.3.8.7

12 entries

1.3.8.8

3 entries

2.3.1.13

2 entries

2.3.1.150

0.093

-

-

16324

2.3.1.180

0.013

0.021

pH 7.0, 30°C, recombinant enzyme

660466

2.3.1.19

0.0315

-

pH 7.5, 23°C

756087

2.3.1.19

0.0315

-

pH 7.5, 25°C

756087

2.3.1.19

2 entries

2.3.1.20

0.0057

0.0068

-

486487

2.3.1.206

0.0569

0.0631

pH 5.5, 30°C, dependent on product formed

719492

2.3.1.21

0.0018

-

-

486528

2.3.1.21

0.152

-

-

486565

2.3.1.233

0.0087

-

mutant enzyme A350I, at pH 7.5 and 30°C

729157

2.3.1.233

0.0132

-

wild type enzyme, at pH 7.5 and 30°C

729157

2.3.1.233

0.0143

-

mutant enzyme Y224L, at pH 7.5 and 30°C

729157

2.3.1.233

0.0157

-

mutant enzyme A350S, at pH 7.5 and 30°C

729157

2.3.1.233

0.0508

-

mutant enzyme Y224G, at pH 7.5 and 30°C

729157

2.3.1.24

0.522

-

-

486668

2.3.1.24

0.522

-

pH 7.5, 37°C

754575

2.3.1.273

0.01

-

37°C, pH 8.0, cosubstrate: 20 mM 2-O-(alpha-D-glucopyranosyl)-D-glycerate

749305

2.3.1.273

0.02

-

37°C, pH 8.0, cosubstrate: 20 mM 2-O-[alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-D-glycerate

749305

2.3.1.21

2 entries

2.3.1.233

5 entries

2.3.1.24

2 entries

2.3.1.273

2 entries

2.3.1.38

0.0086

-

-

285675, 486866

2.3.1.67

0.02

-

-

487377

2.3.1.7

0.02

-

-

486295

2.3.1.7

0.022

-

M564G mutant enzyme from yeast, pH 7.8, 30°C

659372

2.3.1.7

0.0224

-

21°C, pH 7.8, mutant enzyme M564G

674651

2.3.1.7

0.033

-

recombinant enzyme from yeast, pH 7.8, 30°C

659372

2.3.1.7

0.0415

-

21°C, pH 7.8, mutant enzyme S554A

674651

2.3.1.7

0.0549

-

-

487416

2.3.1.7

0.1034

-

21°C, pH 7.8, wild-type enzyme

674651

2.3.1.7

0.112

-

21°C, pH 7.8, mutant enzyme S554A/M564G

674651

2.3.1.74

0.0007

-

-

487467

2.3.1.74

0.0245

-

pH 8.0, 30°C

663042

2.3.1.7

8 entries

2.3.1.74

2 entries

2.3.1.87

0.04

-

wild-type, pH 8.0, 22°C

735681

3.1.2.2

0.0055

-

pH 7.8, 22°C

646176

3.1.2.2

0.06318

-

pH 7.5

679171

3.1.2.2

0.077

-

pH 7.0, 30°C

646179

3.1.2.20

0.0041

-

pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay

690932

3.1.2.20

0.0055

-

pH 7.8, 22°C

646176

3.1.2.20

0.07

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

0.077

-

pH 7.0, 30°C

646179

3.1.2.20

0.1382

-

-

707430

3.1.2.2

3 entries

3.1.2.20

5 entries

K_i Value (5 results)

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Show KI Value (5 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.44

0.05

-

pH and temperature not specified in the publication, 0.05 mM inhibitor, wild-type

724351

1.3.1.44

0.05

-

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

724351

1.3.1.44

0.08

-

pH and temperature not specified in the publication, 0.25 mM inhibitor, wild-type

724351

1.3.1.44

3 entries

2.3.3.10

0.022

-

pH 8.0

488091

3.1.2.17

1.7

-

pH 6.0, 30°C

643853

References & Links

Literature References (148)

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Show Reference (148 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1896

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Purification and characterization of 3-methylcrotonyl-coenzyme-A carboxylase from leaves of Zea mays

1994

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Arch. Biochem. Biophys.

310

64-75

4337

1416912

Purification and characterization of the phosphoenolpyruvate carboxylase from the facultative chemolithotroph Thiobacillus novellus (ATCC 8093)

1992

Charles, A.M.; Sykora, Y.

Antonie van Leeuwenhoek

62

155-165

12302

3988734

Purification and characterization of the 2-methyl branched-chain acyl-CoA dehydrogenase, an enzyme involved in NADH-dependent enoyl-CoA reduction in anaerobic mitochondria of the nematode, Ascaris suum

1985

Komuniecki, R.; Fekete, S.; Thissen-Parra, J.

J. Biol. Chem.

260

4770-4777

16324

8537369

Acetyl coenzyme A:salutaridinol-7-O-acetyltransferase from Papaver somniferum plant cell cultures

1995

Lenz, R.; Zenk, M.H.

J. Biol. Chem.

270

31091-31096

94471

34392

Acetyl-coenzyme A deacylase activity in liver is not an artifact. Subcellular distribution and substrate specificity of acetyl-coenzyme A deacylase activities in rat liver

1979

Grigat, K.P.; Koppe, K.; Seufert, C.D.; Söling, H.D.

Biochem. J.

177

71-79

285675

6833216

The purification and function of acetyl coenzyme A:acyl carrier protein transacylase

1983

Shimakata, T.; Stumpf, P.K.

J. Biol. Chem.

258

3592-3598

390748

6378898

Studies on the metabolism of unsaturated fatty acids. XIV. Purification and properties of NADPH-dependent trans-2-enoyl-CoA reductase of Escherichia coli K-12

1984

Nishimaki, T.; Yamanaka, H.; Mizugaki, M.

J. Biochem.

95

1315-1321

390755

6870879

Kinetic evidence for two separate trans-2-enoyl CoA reductases in rat hepatic microsomes: NADPH-specific short chain- and NAD(P)H-dependent long chain-reductase

1983

Prasad, M.R.; Nagi, M.N.; Cook, L.; Cinti, D.L.

Biochem. Biophys. Res. Commun.

113

659-665

390756

6815194

Evidence for a second microsomal trans-2-enoyl coenzyme A reductase in rat liver. NADPH-specific short chain reductase

1982

Cinti, D.L.; Nagi, M.N.; Cook, L.; White, R.E.

J. Biol. Chem.

257

14333-14340

390760

10811639

Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs

2000

Das, A.K.; Uhler, M.D.; Hajra, A.K.

J. Biol. Chem.

275

24333-24340

391047

2914148

Compartmentation of dicarboxylic acid beta-oxidation in rat liver: importance of peroxisomes in the metabolism of dicarboxylic acids

1989

Suzuki, H.; Yamada, J.; Watanabe, T.; Suga, T.

Biochim. Biophys. Acta

990

25-30

391060

-

Bacterial short-chain acyl-CoA oxidase: production, purification and characterization

1993

Sztajer, H.; Wagner, G.; Schmid, R.D.

Appl. Microbiol. Biotechnol.

39

708-713

391065

10859203

ACX3, a novel medium-chain acyl-coenzyme A oxidase from Arabidopsis

2000

Froman, B.E.; Edwards, P.C.; Bursch, A.G.; Dehesh, K.

Plant Physiol.

123

733-741

391066

11147819

Purification and characterization of the recombinant form of acyl CoA oxidase 3 from the yeast Yarrowia lipolytica

2000

Luo, Y.S.; Wang, H.J.; Gopalan, K.V.; Srivastava, D.K.; Nicaud, J.M.; Chardot, T.

Arch. Biochem. Biophys.

384

1-8

391069

8973574

Higher-plant medium- and short-chain acyl-CoA oxidases: identification, purification and characterization of two novel enzymes of eukaryotic peroxisomal.beta-oxidation

1996

Hooks, M.A.; Bode, K.; Couee, I.

Biochem. J.

320

607-614

391201

3597357

Purification and properties of short chain acyl-CoA, medium chain acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver

1987

Finocchiaro, G.; Ito, M.; Tanaka, K.

J. Biol. Chem.

262

7982-7989

391203

6401712

Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase

1983

Ikeda, Y.; Dabrowski, C.; Tanaka, K.

J. Biol. Chem.

258

1066-1076

391209

7640268

Identification of the active site catalytic residue in human isovaleryl-CoA dehydrogenase

1995

Mohsen, A.W.A.; Vockley, J.

Biochemistry

34

10146-10152

391218

11386848

Identification of Caenorhabditis elegans isovaleryl-CoA dehydrogenase and structural comparison with other scyl-CoA dehydrogenases

2001

Mohsen, A.W.A.; Navarette, B.; Vockley, J.

Mol. Genet. Metab.

73

126-137

391219

11402190

The mitochondrial isovaleryl-coenzyme A dehydrogenase of Arabidopsis oxidizes intermediates of leucine and valine catabolism

2001

Daschner, K.; Couee, I.; Binder, S.

Plant Physiol.

126

601-612

391254

6874697

Purification and characterization of 2-methyl-branched chain acyl coenzyme a dehydrogenase, an enzyme involved in the isoleucine and valine metabolism, from rat liver mitochondria

1983

Ikeda, Y.; Tanaka, K.

J. Biol. Chem.

258

9477-9487

391268

4084576

Spectroscopic analysis of the interaction of rat liver short-chain, medium-chain, and long-chain acyl coenzyme A dehydrogenases with acyl coenzyme A substrates

1985

Ikeda, Y.; Okamura-Ikeda, K.; Tanaka, K.

Biochemistry

24

7192-7199

391269

4062874

The suicide inactivation of ox liver short-chain acyl-CoA dehydrogenase by propionyl-CoA. Formation of an FAD adduct

1985

Shaw, L.; Engel, P.C.

Biochem. J.

230

723-731

391272

3968063

Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme

1985

Ikeda, Y.; Okamura-Ikeda, K.; Tanaka, K.

J. Biol. Chem.

260

1311-1325

391274

6712628

Butyryl-CoA dehydrogenase from Megasphaera elsdenii. Specificity of the catalytic reaction

1984

Williamson, G.; Engel, P.C.

Biochem. J.

218

521-529

391275

6546382

Purification and properties of acyl coenzyme A dehydrogenases from bovine liver. Formation of 2-trans,4-cis-decadienoyl coenzyme A

1984

Dommes, V.; Kunau, W.H.

J. Biol. Chem.

259

1789-1797

391282

7334008

Purification and properties of rat liver acyl-CoA dehydrogenases and electron transfer flavoprotein

1981

Furuta, S.; Miyazawa, S.; Hashimoto, T.

J. Biochem.

90

1739-1750

391283

7059177

Separation, properties, and regulation of acyl coenzyme A dehydrogenases from bovine heart and liver

1982

Davidson, B.; Schulz, H.

Arch. Biochem. Biophys.

213

155-162

391284

-

Butyryl-CoA dehydrogenase from Megasphaera elsdenii

1981

Engel, P.C.

Methods Enzymol.

71

359-366

391300

13130521

Studies on the fatty acid oxidization system of animal tissues. III. Butyryl coenzyme A dehydrogenase

1954

Green, D.E.; Mahler, H.R.

J. Biol. Chem.

206

1-12

391307

8952487

Functional role of the active site glutamate-368 in rat short chain Acyl-CoA dehydrogenase

1996

Battaile, K.P.; Mohsen, A.W.A.; Vockley, J.

Biochemistry

35

15356-15363

391343

6139087

Peroxisomal fatty acyl-coenzyme A oxidation in chicken liver

1983

Ishii, H.; Ishii, S.; Kazama, M.; Suga, T.

Arch. Biochem. Biophys.

226

484-491

391367

7578106

Recombinant human liver medium-chain acyl-CoA dehydrogenase: purification, characterization, and the mechanism of interactions with functionally diverse C8-CoA molecules

1995

Peterson, K.L.; Sergienko, E.E.; Wu, Y.; Kumar, N.R.; Strauss, A.W.; Oleson, A.E.; Muhonen, W.W.; Shabb, J.B.; Srivastava, D.K.

Biochemistry

34

14942-14953

391369

8823175

Medium-long-chain chimeric human acyl-CoA dehydrogenase: medium-chain enzyme with the active center base arrangement of long-chain acyl-CoA dehydrogenase

1996

Nandy, A.; Kieweg, V.; Kraeutle, F.G.; Vock, P.; Kuechler, B.; Bross, P.; Kim, J.J.P.; Rasched, I.; Ghisla, S.

Biochemistry

35

12402-12411

391370

9208949

Biochemical characterization of purified, human recombinant Lys304-->Glu medium-chain acyl-CoA dehydrogenase containing the common disease-causing mutation and comparison with the normal enzyme

1997

Kieweg, V.; Krautle, F.G.; Nandy, A.; Engst, S.; Vock, P.; Abdel-Ghany, A.G.; Bross, P.; Gregersen, N.; Rasched, I.; Strauss, A.; Ghisla, S.

Eur. J. Biochem.

246

548-556

391371

9182995

Characterization of human and pig kidney long-chain-acyl-CoA dehydrogenases and their role in beta-oxidation

1997

Eder, M.; Krautle, F.; Dong, Y.; Vock, P.; Kieweg, V.; Kim, J.J.; Strauss, A.W.; Ghisla, S.

Eur. J. Biochem.

245

600-607

391408

3081514

The purification and characterization of glutaryl-coenzyme A dehydrogenase from porcine and human liver

1986

Lenich, A.C.; Goodman, S.I.

J. Biol. Chem.

261

4090-4096

391418

11705404

Binding, hydration, and decarboxylation of the reaction intermediate glutaconyl-Coenzyme A by human Glutaryl-CoA dehydrogenase

2001

Westover, J.B.; Goodman, S.I.; Frerman, F.E.

Biochemistry

40

14106-14114

391419

11802727

Alternate substrates of human glutaryl-CoA dehydrogenase: Structure and reactivity of substrates, and identification of a novel 2-enoyl-CoA product

2002

Rao, K.S.; Vander Velde, D.; Dwyer, T.M.; Goodman, S.I.; Frerman, F.E.

Biochemistry

41

1274-1284

394650

13319294

On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A

1956

Hauge, J.G.; Crane, F.L.; Beinert, H.

J. Biol. Chem.

219

727-733

394667

10198089

Identification, separation, and characterization of acyl-coenzyme A dehydrogenases involved in mitochondrial beta-oxidation in higher plants

1999

Bode, K.; Hooks, M.A.; Couee, I.

Plant Physiol.

119

1305-1314

486135

3880746

Fatty acid biosynthesis in Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin. Purification and characterization of a novel fatty acid synthase, mycocerosic acid synthase, which elongates n-fatty acyl-CoA with methylmalonyl-CoA

1985

Rainwater, D.L.; Kolattokudy, P.E.

J. Biol. Chem.

260

616-623

486156

3890753

Metabolic activation of mutagenic N-hydroxyarylamines by O-acetyltransferase in Salmonella typhimurium TA98

1985

Saito, K.; Shinohara, A.; Kamataki, T.; Kato, R.

Arch. Biochem. Biophys.

239

286-295

486290

4629977

Different carnitine acyltransferases in calf liver

1972

Solberg, H.E.

Biochim. Biophys. Acta

280

422-433

486291

4417128

Acyl group specificity of mitochondrial pools of carnitine acyltransferases

1974

Solberg, H.E.

Biochim. Biophys. Acta

360

101-112

486292

-

Comparison of the carnitine acyltransferase activities from rat liver peroxisomes and microsomes

1976

Markwell, M.A.K.; Tolbert, N.E.; Bieber, L.L.

Arch. Biochem. Biophys.

176

479-488

486295

6436243

Properties of purified carnitine acyltransferases of mouse liver peroxisomes

1984

Farrell, S.O.; Fiol, C.J.; Reddy, J.K.; Bieber, L.L.

J. Biol. Chem.

259

13089-13095

486305

10486279

Molecular cloning and expression of human carnitine octanoyltransferase: Evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids

1999

Ferdinandusse, S.; Mulders, J.; IJlst, L.; Denis, S.; Dacremont, G.; Waterham, H.R.; Wanders, R.J.A.

Biochem. Biophys. Res. Commun.

263

213-218

486451

9766003

Incubation of 6-methylsalicylic acid synthase with alternative starter units in the absence of NADPH and the identification of the resulting triaceticacid lactones

1998

Campuzano, I.D.G.; Shoolingin-Jordan, P.M.

Biochem. Soc. Trans.

26

S284

486487

436848

Specificity of diacylglycerol acyltransferase from bovine mammary gland, liver and adipose tissue towards acyl-CoA esters

1979

Marshall, M.O.; Knudsen, J.

Eur. J. Biochem.

94

93-98

486526

7275984

Isolation and purification of mitochondrial carnitine octanoyltransferase activities from beef heart

1981

Clarke, P.R.H.; Bieber, L.L.

J. Biol. Chem.

256

9861-9868

486528

3663121

Purification and properties of the soluble carnitine palmitoyltransferase from bovine liver mitochondria

1987

Ramsay, R.R.; Derrick, J.P.; Friend, A.S.; Tubbs, P.K.

Biochem. J.

244

271-278

486565

2174799

Purification, characterization and partial amino acid sequences of carnitine palmitoyl-transferase from human liver

1990

Finocchiaro, G.; Colombo, I.; DiDonato, S.

FEBS Lett.

274

163-166

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