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Ligand trans-hex-2-enoyl-CoA

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for trans-hex-2-enoyl-CoA

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Roles as Enzyme Ligand

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

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Show Natural Substrate (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+

390748, 390749

-

1.3.8.1

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

391284

-

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

1.3.8.1

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

0

-

Substrate in Enzyme-catalyzed Reactions (22 results)

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Show Substrate (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.10

2-trans-hexenoyl-CoA + NADPH = ?

703756

-

1.3.1.10

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

656515

-

1.3.1.38

2-trans-hexenoyl-CoA + NADPH = ?

706445

-

1.3.1.38

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

390748, 390749

-

1.3.1.38

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

390748, 390749, 390755, 390756, 390760

-

1.3.1.44

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

724351

-

1.3.1.44

hexenoyl-CoA + NADH = ? + NAD+

724240

-

1.3.1.44

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

656287, 390810

-

1.3.1.44

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

724351

-

1.3.1.10

2 entries

1.3.1.38

3 entries

1.3.1.44

4 entries

1.3.1.8

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

390753, 390754, 390755, 390756, 390870, 390810, 390851

-

1.3.1.85

(2E)-hex-2-enoyl-CoA + NADPH + CO2 + H+ = (S)-2-butylpropanedioyl-CoA + NADP+

739814

-

1.3.8.1

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

391284

-

4.2.1.119

(2E)-hexenoyl-CoA + H2O = (3R)-3-hydroxyhexanoyl-CoA

714098, 684952, 680715

-

4.2.1.119

hex-2-enoyl-CoA + H2O = (R)-3-hydroxyhexanoyl-CoA

33737, 33736

-

4.2.1.119

hexenoyl-CoA + H2O = 3-hydroxyhexanoyl-CoA

649389

-

4.2.1.119

3 entries

4.2.1.150

hexenoyl-CoA + H2O = ?

33715, 33729

-

4.2.1.17

hex-2-enoyl-CoA + H2O = ?

5866

3zwb, 3D-view

4.2.1.17

hexenoyl-CoA + H2O = ?

33729, 33730

3zwb, 3D-view

4.2.1.17

trans-2-hexenoyl-CoA + H2O = (3S)-3-hydroxyhexanoyl-CoA

649889, 649739

3zwb, 3D-view

4.2.1.17

3 entries

4.2.1.55

trans-2-Hexenoyl-CoA + H2O = ?

5792

-

4.2.1.74

trans-2-hexenoyl-CoA + H2O = (3S)-3-hydroxyhexanoyl-CoA

5869, 5868, 698680

-

5.3.3.8

trans-2-hexenoyl-CoA + H2O = 3-hydroxyhexanoyl-CoA

678385

3zwb, 3D-view

Product in Enzyme-catalyzed Reactions (25 results)

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Show Product (25 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.3.6

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

0

-

1.3.8.1

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

0

-

1.3.8.1

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

0

-

1.3.8.1

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

391201, 0, 391282

-

1.3.8.1

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

391201, 391272, 0, 391283, 391203, 391274, 391275, 391300

-

1.3.8.1

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

0

-

1.3.8.1

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

0

-

1.3.8.4

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

391219, 0, 391218, 391201, 391209

-

1.3.8.4

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

0

-

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

0

-

1.3.8.7

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

0

-

1.3.8.7

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

0

-

1.3.8.7

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

391343, 0, 391201

-

1.3.8.7

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

391203

-

1.3.8.7

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

0

-

1.3.8.7

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

0

-

1.3.8.7

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

0

-

1.3.8.7

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

0

-

1.3.8.7

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

0

-

1.3.8.8

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

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

391282, 394667, 391268

-

5.3.3.8

3-cis-hexenoyl-CoA = 2-trans-hexenoyl-CoA

652357

3zwb, 3D-view

5.3.3.8

3-trans-Hexenoyl-CoA = 2-trans-Hexenoyl-CoA

0, 3014, 3015, 652357, 653752, 2999, 649676, 651339

3zwb, 3D-view

5.3.3.8

trans-3-hexenoyl-CoA = trans-2-hexenoyl-CoA

0

3zwb, 3D-view

1.3.8.7

9 entries

1.3.8.8

3 entries

5.3.3.8

3 entries

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.8

competitive inhibition of crotonoyl-CoA reduction, but not of 2-trans-hexadecenoyl-CoA and 2-trans-decenoyl-CoA reduction

390753

-

4.2.1.17

-

33730

3zwb, 3D-view

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

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

EC NUMBER

ENZYME 3D STRUCTURE

1.1.1.35

3zwb, 3D-view

4.2.1.17

3zwb, 3D-view

5.3.3.8

3zwb, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (20 results)

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Show Turnover Number (20 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.1.44

15.3

-

mutant I287A, pH not specified in the publication, temperature not specified in the publication

724351

1.3.1.44

19

-

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

724351

1.3.1.44

22.4

-

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

724351

1.3.1.44

48

-

mutant Y370A, pH not specified in the publication, temperature not specified in the publication

724351

1.3.1.44

50

-

mutant L291A, pH not specified in the publication, temperature not specified in the publication

724351

1.3.1.44

64

-

mutant F295A, pH not specified in the publication, temperature not specified in the publication

724351

1.3.1.44

112

-

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

724351

4.2.1.119

22.8

-

-

684952

4.2.1.119

210

-

pH 7.5, 22°C, recombinant full-length enzyme

714098

4.2.1.17

0.06

-

pH 8.0, 22°C, mutant enzyme E144A/Q162L

649889

4.2.1.17

0.43

-

pH 8.0, 22°C, mutant enzyme E144A

649889

4.2.1.17

0.44

-

pH 8.0, 22°C, mutant enzyme E164A

649889

4.2.1.17

180

-

pH 8

678385

4.2.1.17

561

-

pH 8.0, 22°C, mutant enzyme Q162L

649889

4.2.1.17

601

-

pH 8.0, 22°C, mutant enzyme Q162M

649889

4.2.1.17

607

-

pH 8.0, 22°C, mutant enzyme Q162A

649889

4.2.1.17

745

-

pH 8.0, 22°C, wild-type enzyme

649889

5.3.3.8

0.013

-

pH 8, hydratase activity, mutant enzyme K242D

678385

5.3.3.8

0.021

-

pH 8, hydratase activity, mutant enzyme K242T

678385

5.3.3.8

1

-

pH 8, hydratase activity, mutant enzyme K242C

678385

1.3.1.44

7 entries

4.2.1.119

2 entries

4.2.1.17

8 entries

5.3.3.8

3 entries

K_M Value (35 results)

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Show KM Value (35 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.38

0.048

-

-

390748

1.3.1.44

0.0034

-

mutant I287A, pH not specified in the publication, temperature not specified in the publication

724351

1.3.1.44

0.007

-

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

724351

1.3.1.44

0.012

-

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

724351

1.3.1.44

0.015

-

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

724351

1.3.1.44

0.018

-

mutant Y370A, pH not specified in the publication, temperature not specified in the publication

724351

1.3.1.44

0.019

-

mutant F295A, pH not specified in the publication, temperature not specified in the publication

724351

1.3.1.44

0.038

-

mutant L291A, pH not specified in the publication, temperature not specified in the publication

724351

1.3.1.44

0.091

-

pH 6.2, 30°C

656287

1.3.1.44

0.091

-

recombinant enzyme, pH 6.2, 30°C, with NADH as cofactor

656287

1.3.1.44

9 entries

1.3.1.8

0.0005

-

-

390753

4.2.1.119

0.015

-

-

33737

4.2.1.119

0.018

-

pH 8, 30°C, L65A mutant

649389

4.2.1.119

0.034

-

pH 8.0, 30°C

33736

4.2.1.119

0.04

-

pH 8, 30°C, wild-type

649389

4.2.1.119

0.0667

-

pH 7.5, 22°C, recombinant full-length enzyme

714098

4.2.1.119

0.102

-

pH 8, 30°C, V130G mutant

649389

4.2.1.119

8.7

-

-

684952

4.2.1.150

0.13

-

25°C, pH 7.5

33729

4.2.1.150

0.13

-

at pH 8.0 and 25°C

33715

4.2.1.17

0.0143

-

pH 8.0, 22°C, mutant enzyme Q162A

649889

4.2.1.17

0.0152

-

pH 8.0, 22°C, mutant enzyme E144A

649889

4.2.1.17

0.021

-

pH 8.0, 22°C, mutant enzyme E144A/Q162L

649889

4.2.1.17

0.0229

-

pH 8.0, 22°C, mutant enzyme Q162M

649889

4.2.1.17

0.024

-

pH 8.0, 22°C, mutant enzyme E164A

649889

4.2.1.17

0.025

-

pH 8.0, 22°C, wild-type enzyme

649889

4.2.1.17

0.027

-

pH 8.0, 22°C, mutant enzyme Q162L

649889

4.2.1.17

0.029

-

pH 9.0

5866

4.2.1.17

0.13

-

25°C

33729

4.2.1.119

7 entries

4.2.1.150

2 entries

4.2.1.17

9 entries

4.2.1.55

0.0263

-

-

5792

4.2.1.74

0.045

-

-

5868

4.2.1.74

0.045

-

25°C

698680

5.3.3.8

0.00062

-

pH 8, hydratase activity, mutant enzyme K242T

678385

5.3.3.8

0.0026

-

pH 8, hydratase activity, mutant enzyme K242D

678385

5.3.3.8

0.31

-

pH 8, hydratase activity, mutant enzyme K242C

678385

4.2.1.74

2 entries

5.3.3.8

3 entries

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.2.1.17

0.00024

-

pH 7.5, 25°C

33730

References & Links

Literature References (58)

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Show Reference (58 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

2999

376522

Purification of hog liver isomerase. Mechanism of isomerization of 3-alkenyl and 3-alkynyl thioesters

1979

Miscowicz, F.M.; Bloch, K.

J. Biol. Chem.

254

5868-5877

3014

2154476

DELTA3,DELTA2-Enoyl-CoA isomerases. Characterization of the mitochondrial isoenzyme in the rat

1990

Palossari, P.M.; Kilponen, J.M.; Sormunen, R.T.; Hassinen, I.E.; Hiltunen, J.K.

J. Biol. Chem.

265

3347-3353

3015

2303409

Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and DELTA3,DELTA2-enoyl-CoA isomerase activities

1990

Palossari, P.M.; Hiltunen, J.K.

J. Biol. Chem.

265

2446-2449

5792

5808333

Metabolism of poly-beta-hydroxybutyrate. II. Enzymatic synthesis of D(-)-beta-hydroxybutyryl coenzyme A by an enoyl hydrase from Rhodospirillum rubrum

1969

Moskowitz, G.J.; Merrick, J.M.

Biochemistry

8

2748-2755

5866

833142

Purification and properties of pig heart crotonase and the presence of short chain and long chain enoyl coenzyme A hydratases in pig and guinea pig tissues

1977

Fong, J.C.; Schulz, H.

J. Biol. Chem.

252

542-547

5868

7278662

Short-chain and long-chain enoyl-CoA hydratases from pig heart muscle

1981

Fong, J.C.; Schulz, H.

Methods Enzymol.

71

390-398

5869

8323290

Purification and characterization of the trifunctional beta-oxidation complex from pig heart mitochondria

1993

Luo, M.J.; He, X.Y.; Sprecher, H.; Schulz, H.

Arch. Biochem. Biophys.

304

266-271

33715

7024731

Enoyl-CoA hydratases from Clostridium acetobutylicum and Escherichia coli

1981

Waterson, R.M.; Conway, R.S.

Methods Enzymol.

71

421-430

33729

5057466

Purification and characterization of cortonase from Clostridium acetobutylicum

1972

Waterson, R.M.; Castellino, F.J.; Hass, G.M.; Hill, R.L.

J. Biol. Chem.

247

5266-5271

33730

5057465

Enoyl coenzyme A hydratase (crotonase). Catalytic properties of crotonase and its possible regulatory role in fatty acid oxidation

1972

Waterson, R.M.; Hill, R.L.

J. Biol. Chem.

247

5258-5265

33736

9457873

Expression and characterization of (R)-specific enoyl coenzyme A hydratase involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae

1998

Fukui, T.; Shiomi, N.; Doi, Y.

J. Bacteriol.

180

667-673

33737

8902629

Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase

1996

Jiang, L.L.; Kobayashi, A.; Matsuura, H.; Fukushima, H.; Hashimoto, T.

J. Biochem.

120

624-632

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

390749

6754111

Studies on the metabolism of unsaturated fatty acids. VII. Separation and general properties of reduced nicotinamide adenine dinucleotide phosphate-dependent trans-2-enoyl-coenzyme A reductase from Escherichia coli K-12

1982

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

Chem. Pharm. Bull.

30

2503-2511

390753

3977322

Solubilization and purification of hepatic microsomal trans-2-enoyl-CoA reductase: evidence for the existence of a second long-chain enoyl-CoA reductase

1985

Prasad, M.R.; Chiang, C.F.; Cook, L.; Cinti, D.L.

Arch. Biochem. Biophys.

237

535-544

390754

6416174

Biochemical properties of short- and long-chain rat liver microsomal trans-2-enoyl coenzyme A reductase

1983

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

Arch. Biochem. Biophys.

226

50-64

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

390810

6146525

Fatty acid synthesis in mitochondria of Euglena gracilis

1984

Inui, H.; Miyatake, K.; Nakano, Y.; Kitaoka, S.

Eur. J. Biochem.

142

121-126

390851

468815

Enoyl coenzyme A reduction by bovine mammary fatty acid synthetase. Specificity and other characteristics

1979

Strom, K.A.; Galeos, W.L.; Davidson, L.A.; Kumar, S.

J. Biol. Chem.

254

8153-8158

390870

3994691

Purification and characterization of 2-enoyl-CoA-reductase from bovine liver

1985

Cvetanovic, M.; Moreno de la Garza, M.; Dommes, V.; Kunau, W.H.

Biochem. J.

227

49-56

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

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

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

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Links to other databases for trans-hex-2-enoyl-CoA

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