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Ligand crotonoyl-CoA

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

butanoate fermentation, CO2 fixation in Crenarchaeota, ethylmalonyl-CoA pathway, glutamate and glutamine metabolism, tryptophan metabolism

KEGG

Aminobenzoate degradation, Benzoate degradation, Biosynthesis of secondary metabolites, Butanoate metabolism, Carbon fixation pathways in prokaryotes, Carbon metabolism, Fatty acid degradation, Fatty acid metabolism, Glyoxylate and dicarboxylate metabolism, Lysine degradation, Microbial metabolism in diverse environments, Tryptophan metabolism more

MetaCyc

3-hydroxypropanoate/4-hydroxybutanate cycle, 4-aminobutanoate degradation V, acetyl-CoA fermentation to butanoate, crotonate fermentation (to acetate and cyclohexane carboxylate), crotonyl-CoA/ethylmalonyl-CoA/hydroxybutyryl-CoA cycle (engineered), ethylmalonyl-CoA pathway, gallate degradation III (anaerobic), gamma-butyrobetaine degradation I, glutaryl-CoA degradation, L-glutamate degradation V (via hydroxyglutarate), L-glutamate degradation VII (to butanoate), L-glutamate degradation XI (reductive Stickland reaction), L-lysine fermentation to acetate and butanoate, oleate beta-oxidation, pyruvate fermentation to butanoate, pyruvate fermentation to butanol I, pyruvate fermentation to butanol II (engineered), pyruvate fermentation to hexanol (engineered), succinate fermentation to butanoate, superpathway of Clostridium acetobutylicum solventogenic fermentation more

Show all BRENDA pathways known for crotonoyl-CoA

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (21 results)

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Show Natural Substrate (21 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.109

(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster = butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster

687430, 725287

-

1.3.1.109

(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster = butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster

732165

-

1.3.1.109

(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster = butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster

731998, 733386, 734071

-

1.3.1.109

3 entries

1.3.1.38

crotonyl-CoA + NADPH = butanoyl-CoA + NADP+

390756

-

1.3.1.44

crotonyl-CoA + NADH = butanoyl-CoA + NAD+

724240

-

1.3.1.8

crotonyl-CoA + reduced acceptor = butyryl-CoA + oxidized acceptor

656737

-

1.3.1.85

(E)-crotonyl-CoA + CO2 + NADPH + H+ = (2S)-ethylmalonyl-CoA + NADP+

713409

-

1.3.1.85

crotonyl-CoA + CO2 + NADPH + H+ = (2S)-ethylmalonyl-CoA + NADP+

739814, 741243, 740962

-

1.3.1.85

crotonyl-CoA + CO2 + NADPH + H+ = ?

741053

-

1.3.8.1

2-butenoyl-CoA + reduced acceptor = butanoyl-CoA + acceptor

654353

-

1.3.8.1

2-butenoyl-CoA + reduced electron transfer flavoprotein = butanoyl-CoA + electron transfer protein

391284

-

1.3.8.1

crotonyl-CoA + 2 NADH + 2 Fd- = butyryl-CoA + 2 NAD+ + 2 Fd2-

742866

-

1.3.1.85

3 entries

1.3.8.1

3 entries

4.2.1.149

crotonyl-CoA + H2O = ?

726932

-

4.2.1.150

crotonyl-CoA + H2O = (S)-3-hydroxybutanoyl-CoA

727751, 726748

-

4.2.1.150

crotonyl-CoA + H2O = 3-hydroxybutyryl-CoA

33715, 748646, 748405

-

4.2.1.17

crotonoyl-CoA + H2O = (S)-3-hydroxybutyryl-CoA

726748

-

4.2.1.17

crotonyl-CoA + H2O = (3S)-3-hydroxybutanoyl-CoA

651567, 5792

-

4.2.1.17

crotonyl-CoA + H2O = (3S)-hydroxybutyryl-CoA

746582, 748661

-

4.2.1.17

crotonyl-CoA + H2O = 3-hydroxybutyryl-CoA

746611

-

4.2.1.55

crotonoyl-CoA + H2O = (3R)-3-hydroxybutanoyl-CoA

729651

-

4.2.1.55

crotonyl-CoA = ?

5792

-

4.2.1.150

2 entries

4.2.1.17

4 entries

4.2.1.55

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (19 results)

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Show Natural Product (19 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.36

(R)-3-hydroxybutyryl-CoA = trans-2-butenoyl-CoA + H2O

0

-

1.3.1.109

butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster = (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster

0

-

1.3.8.1

butanoyl-CoA + acceptor = but-2-enoyl-CoA + reduced acceptor

0

-

1.3.8.1

butanoyl-CoA + oxidized acceptor = crotonyl-CoA + reduced acceptor

0

-

1.3.8.6

glutaryl-CoA + electron transfer flavoprotein = (E)-but-2-enoyl-CoA + CO2 + reduced electron transfer flavoprotein

0

-

1.3.8.6

glutaryl-CoA + FAD = (E)-but-2-enoyl-CoA + CO2 + FADH2

0

-

1.3.8.6

glutaryl-CoA + acceptor = crotonoyl-CoA + CO2 + reduced acceptor

0

-

1.3.8.6

glutaryl-CoA + electron transfer flavoprotein = crotonoyl-CoA + CO2 + reduced electron transfer flavoprotein

0

-

1.3.8.6

glutaryl-CoA + electron transfer protein = crotonoyl-CoA + CO2 + reduced electron transfer protein

0

-

1.3.8.6

glutaryl-CoA + FAD = crotonoyl-CoA + CO2 + FADH2

0

-

1.3.8.6

glutaryl-CoA + acceptor = crotonyl-CoA + CO2 + reduced acceptor

0, 391413

-

1.3.8.6

glutaryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + CO2 + reduced electron-transfer flavoprotein

0

-

4.2.1.120

4-hydroxybutanoyl-CoA = (E)-but-2-enoyl-CoA + H2O

0

-

4.2.1.120

4-hydroxybutanoyl-CoA = crotonyl-CoA + H2O

0

-

1.3.8.1

2 entries

1.3.8.6

8 entries

4.2.1.120

2 entries

4.2.1.150

3-hydroxybutyryl-CoA = crotonyl-CoA + H2O

0

-

4.2.1.17

(S)-3-hydroxybutyryl-CoA = crotonoyl-CoA + H2O

0

-

4.2.1.55

(3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H2O

0

-

7.2.4.5

glutaconyl-CoA + Na+[side 1] = but-2-enoyl-CoA + CO2 + Na+[side 2]

0, 648362

-

7.2.4.5

glutaconyal-CoA + Na+[side 1] = crotonyl-CoA + CO2 + Na+[side 2]

0

-

7.2.4.5

2 entries

Substrate in Enzyme-catalyzed Reactions (95 results)

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Show Substrate (95 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.10

crotonyl-CoA + NADPH + H+ = ?

740716

-

1.3.1.10

crotonyl-CoA + NADPH + H+ = butanoyl-CoA + NADP+

762612

-

1.3.1.104

crotonyl-CoA + NADPH + H+ = butanoyl-CoA + NADP+

763551, 743859

-

1.3.1.104

crotonyl-CoA + NADPH + H+ = butyryl-CoA + NADP+

763903

-

1.3.1.109

(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster = butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster

687430, 725287, 732165

-

1.3.1.109

(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster = butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster

732165

-

1.3.1.109

(E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster = butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster

725287

-

1.3.1.109

(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster = butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster

731998, 733386, 734071

-

1.3.1.10

2 entries

1.3.1.104

2 entries

1.3.1.109

4 entries

1.3.1.38

crotonyl-CoA + NADPH = butanoyl-CoA + NADP+

390748, 390755, 390756, 390761

-

1.3.1.39

crotonyl-CoA + NADPH + H+ = butyryl-CoA + NADP+

726431

-

1.3.1.44

crotonyl-CoA + NAD(P)H = butyryl-CoA + NAD(P)+

656287

-

1.3.1.44

crotonyl-CoA + NADH + H+ = butyryl-CoA + NAD+

686722, 656287, 724351, 286051

-

1.3.1.44

crotonyl-CoA + NADH = butanoyl-CoA + NAD+

724240

-

1.3.1.44

crotonyl-CoA + NADH = butyryl-CoA + NAD+

390806, 390810

-

1.3.1.44

crotonyl-CoA + NADPH + H+ = butyryl-CoA + NADP+

724351

-

1.3.1.44

crotonyl-CoA + NADPH = butanoyl-CoA + NADP+

724240, 724351

-

1.3.1.8

crotonyl-CoA + NAD(P)H = butanoyl-CoA + NADP+

390753, 390755, 390756, 390850, 390852, 390849, 390810, 390851

-

1.3.1.8

crotonyl-CoA + NADPH = butanoyl-CoA + NADP+

689745

-

1.3.1.8

crotonyl-CoA + NADPH = butyryl-CoA + NADP+

685980

-

1.3.1.8

crotonyl-CoA + reduced acceptor = butyryl-CoA + oxidized acceptor

656737

-

1.3.1.85

(E)-crotonyl-CoA + CO2 + NADPH + H+ = (2S)-ethylmalonyl-CoA + NADP+

713409

-

1.3.1.85

(E)-crotonyl-CoA + NADPH + H+ = butyryl-CoA + NADP+

713409

-

1.3.1.85

crotonyl-CoA + CO2 + NADPH + H+ = (2S)-ethylmalonyl-CoA + NADP+

710982, 739814, 741243, 740962, 760072, 689745

-

1.3.1.85

crotonyl-CoA + CO2 + NADPH + H+ = ?

741053

-

1.3.1.85

crotonyl-CoA + NADPH + CO2 + H+ = (2S)-ethylmalonyl-CoA + NADP+

739852

-

1.3.1.85

crotonyl-CoA + NADPH + H+ = ?

724588

-

1.3.1.85

crotonyl-CoA + NADPH + H+ = butyryl-CoA + NADP+

689745

-

1.3.1.86

(E)-but-2-enoyl-CoA + NADPH + H+ = butanoyl-CoA + NADP+

711366, 712641

-

1.3.1.86

crotonyl-CoA + NADH + ferredoxin = butyryl-CoA + ?

725287

-

1.3.1.86

crotonyl-CoA + NADPH + H+ = butanoyl-CoA + NADP+

711884

-

1.3.1.86

crotonyl-CoA + NADPH + H+ = butyryl-CoA + NADP+

656737, 712939, 712270, 713435, 712617, 712233

-

1.3.1.86

trans-crotonyl-CoA + NADPH + H+ = butyryl-CoA + NADP+

390852

-

1.3.1.9

crotonoyl-CoA + NADH + H+ = butanoyl-CoA + NAD+

763733, 763022, 763271

-

1.3.1.9

crotonoyl-CoA + NADH + H+ = butyryl-CoA + NAD+

390505

-

1.3.1.9

crotonoyl-CoA + NADH = butyryl-CoA + NAD+

684850

-

1.3.1.9

crotonyl-CoA + NAD+ = ?

689919

-

1.3.1.9

crotonyl-CoA + NAD+ = butyryl-CoA + NADH + H+

696691, 696692, 696013, 697336

-

1.3.1.9

crotonyl-CoA + NADH + H+ = butyryl-CoA + NAD+

687327, 689435, 739906, 689612, 740323, 687598, 688247, 724889, 725169, 689328, 687702, 739819, 689919, 686787, 726284, 725221, 741373, 742918, 740250, 743553, 673193, 672556, 672553, 675299, 676367

-

1.3.1.9

crotonyl-CoA + NADH = butyryl-CoA + NAD+

390897, 661991, 390875, 390876, 390877, 390887, 390898, 285669

-

1.3.1.9

crotonyl-CoA + NADPH + H+ = butyryl-CoA + NADP+

285669, 687702

-

1.3.1.9

trans-but-2-enoyl-CoA + NADH = butanoyl-CoA + NAD+

654543

-

1.3.1.44

6 entries

1.3.1.8

4 entries

1.3.1.85

7 entries

1.3.1.86

5 entries

1.3.1.9

9 entries

1.3.1.95

(E)-2-butenoyl-CoA + methyl viologen = ?

696519

-

1.3.1.B14

crotonyl-CoA + NADPH + H+ = butanoyl-CoA + NADP+

743859

-

1.3.8.1

(E)-2-butenoyl-CoA + reduced methylviologen = ? + oxidized methylviologen

696519

-

1.3.8.1

2-butenoyl-CoA + reduced acceptor = butanoyl-CoA + acceptor

654353

-

1.3.8.1

2-butenoyl-CoA + reduced acceptor = butyryl-CoA + acceptor

391291

-

1.3.8.1

2-butenoyl-CoA + reduced electron transfer flavoprotein = butanoyl-CoA + electron transfer protein

391284

-

1.3.8.1

crotonyl-CoA + 2 NADH + 2 Fd- = butyryl-CoA + 2 NAD+ + 2 Fd2-

742866

-

1.3.8.1

crotonyl-CoA + electron acceptor = butyryl-CoA + reduced acceptor

672003

-

1.3.8.1

crotonyl-CoA + electron transfer flavoprotein = butyryl-CoA + ?

725287

-

1.3.8.1

crotonyl-CoA + O2 + 2 NADH + 2 H+ = butanoyl-CoA + H2O2 + 2 NAD+

725287

-

1.3.8.1

crotonyl-CoA + reduced acceptor = butyryl-CoA + oxidized acceptor

676021

-

1.3.8.1

crotonyl-CoA + reduced ferredoxin = butanoyl-CoA + oxidized ferredoxin

725287, 742866

-

1.3.8.1

10 entries

1.3.8.7

crotonyl-CoA + H2O = L-3-hydroxy-butyryl-CoA

391329

-

2.3.1.165

crotonyl-CoA + malonyl-CoA = 6-(2-propene) triacetic acid lactone + CoA

486451

-

2.3.1.31

crotonyl-CoA + L-homoserine = CoA + O-crotonyl-L-homoserine

486788

-

2.3.1.39

2-butenoyl-CoA + an [acyl-carrier protein] = CoA + 2-butenoyl-[acyl carrier protein]

755871

-

2.3.1.85

crotonyl-CoA + an [acyl-carrier protein] = CoA + crotonyl-[acyl-carrier protein]

755686

-

2.3.3.13

crotonyl-CoA + H2O = crotonate + CoA

672203

-

2.7.8.7

crotonyl-CoA + apo-[acyl-carrier protein] = ? + holo-[acyl-carrier protein]

674285

-

2.7.8.7

crotonyl-CoA + apo-[acyl-carrier protein] = CoA + crotonyl-[acyl-carrier protein]

760467

-

2.7.8.7

2 entries

2.8.3.1

crotonyl-CoA + propanoate = ?

737535

-

2.8.3.9

crotonyl-CoA + acetate = crotonate + acetyl-CoA

643837

-

3.1.2.1

crotonyl-CoA = trans-2-butenoate + CoA

94488

-

3.1.2.2

crotonyl-CoA + H2O = CoA + crotonate

679171, 646180

-

3.1.2.20

2-butenoyl-CoA + H2O = CoA + 2-butenoate

732296, 707486

-

3.1.2.20

crotonyl-CoA + H2O = CoA + crotonate

690932, 707486, 646180

-

3.1.2.20

2 entries

3.3.2.12

crotonyl-CoA + H2O = (R)-3-hydroxybutyryl-CoA

715582

-

4.2.1.119

(2E)-butenoyl-CoA + H2O = (3R)-hydroxybutanoyl-CoA

714098

-

4.2.1.119

2-trans-butenoyl-CoA + H2O = (3R)-hydroxybutanoyl-CoA

697692

-

4.2.1.119

Crotonyl-CoA + H2O = (3R)-3-Hydroxybutanoyl-CoA

684952, 687485

-

4.2.1.119

crotonyl-CoA + H2O = (R)-3-hydroxybutanoyl-CoA

33736, 33737

-

4.2.1.119

crotonyl-CoA + H2O = 3-hydroxybutanoyl-CoA

649389

-

4.2.1.119

crotonyl-CoA + H2O = ?

696077, 651723

-

4.2.1.119

6 entries

4.2.1.149

crotonyl-CoA + H2O = ?

726932, 724139

-

4.2.1.150

a short-chain trans-2-enoyl-CoA + H2O = short-chain (3S)-3-hydroxyacyl-CoA

33729

-

4.2.1.150

crotonyl-CoA + H2O = (S)-3-hydroxybutanoyl-CoA

726748, 727751

-

4.2.1.150

crotonyl-CoA + H2O = 3-hydroxybutyryl-CoA

2966, 33715, 286058, 748646, 748405

-

4.2.1.150

crotonyl-CoA + H2O = ?

33729

-

4.2.1.17

crotonoyl-CoA + H2O = (S)-3-hydroxybutyryl-CoA

726748, 746710

-

4.2.1.17

crotonyl-CoA + H2O = (3S)-3-hydroxybutanoyl-CoA

649889, 33718, 696477, 651567, 5792, 696077, 650113, 687485, 697212

-

4.2.1.17

crotonyl-CoA + H2O = (3S)-hydroxybutyryl-CoA

746582, 748661

-

4.2.1.17

crotonyl-CoA + H2O = 3-hydroxybutyryl-CoA

746611

-

4.2.1.17

crotonyl-CoA + H2O = ?

5866, 33730, 2207, 700005, 33729, 33713

-

4.2.1.17

trans-crotonyl-CoA + H2O = (S)-3-hydroxybutanoyl-CoA

752454

-

4.2.1.150

4 entries

4.2.1.17

6 entries

4.2.1.18

crotonyl-CoA = ?

679737

-

4.2.1.54

crotonoyl-CoA + H2O = 2-hydroxybutyryl-CoA

33926, 33929

-

4.2.1.55

crotonoyl-CoA + H2O = (3R)-3-hydroxybutanoyl-CoA

729651

-

4.2.1.55

Crotonyl-CoA + H2O = (3R)-3-Hydroxybutanoyl-CoA

5792

-

4.2.1.55

crotonyl-CoA = ?

5792

-

4.3.1.14

crotonoyl-CoA + NH3 = L-3-aminobutyryl-CoA

6045

-

4.3.1.14

Crotonyl-CoA + hydroxylamine = CoA + 3-methyl-5-isoxazolidinone

6045

-

4.2.1.55

3 entries

4.3.1.14

2 entries

6.4.1.3

ATP + crotonyl-CoA + HCO3- = ADP + phosphate + ?

1873

-

6.4.1.4

ATP + crotonoyl-CoA + HCO3- = ?

1896, 1884, 1886

-

6.4.1.4

ATP + crotonyl-CoA + HCO3- = ADP + phosphate + glutaconyl-CoA

653128

-

6.4.1.4

2 entries

Product in Enzyme-catalyzed Reactions (70 results)

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Show Product (70 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.36

(R)-3-hydroxybutyryl-CoA = trans-2-butenoyl-CoA + H2O

0

-

1.3.1.109

butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster = (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster

0

-

1.3.1.109

butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster = (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster

0

-

1.3.1.109

2 entries

1.3.3.6

butyryl-CoA + O2 = trans-2-butenoyl-CoA + H2O2

0

-

1.3.8.1

butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor

0

-

1.3.8.1

butanoyl-CoA + FAD = 2-butenoyl-CoA + FADH2

0

-

1.3.8.1

butyryl-CoA + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = 2-butenoyl-CoA + reduced acceptor

391308

-

1.3.8.1

butyryl-CoA + electron acceptor = 2-butenoyl-CoA + reduced acceptor

0, 391199, 391256, 391287, 391261, 391283, 391300, 391264, 391266, 391291, 391303, 391259, 391201, 391272, 391282, 391276, 391274, 391275, 391047, 391203, 391268, 391284, 391297

-

1.3.8.1

butyryl-CoA + electron transfer flavoprotein = 2-butenoyl-CoA + reduced electron transfer flavoprotein

0

-

1.3.8.1

butyryl-CoA + electron-transferring flavoprotein = 2-butenoyl-CoA + reduced electron-transferring flavoprotein

0

-

1.3.8.1

butyryl-CoA + ferricenium = 2-butenoyl-CoA + ferrocene

0

-

1.3.8.1

butyryl-CoA + ferrocenium = 2-butenoyl-CoA + ferrocene

0

-

1.3.8.1

butyryl-CoA + O2 = 2-butenoyl-CoA + H2O2

391297, 391310

-

1.3.8.1

butyryl-CoA + pyocyanine + triphenyltetrazolium chloride = 2-butenoyl-CoA + reduced acceptor

391300

-

1.3.8.1

butanoyl-CoA + acceptor = but-2-enoyl-CoA + reduced acceptor

0

-

1.3.8.1

butanoyl-CoA + FAD = but-2-enoyl-CoA + FADH2

0

-

1.3.8.1

butyryl-CoA + 2,6-dichloro-phenolindophenol = but-2-enoyl-CoA + reduced 2,6-dichloro-phenolindophenol

0

-

1.3.8.1

butanoyl-CoA + oxidized acceptor = crotonyl-CoA + reduced acceptor

0

-

1.3.8.1

butyryl-CoA + electron transfer flavoprotein = crotonyl-CoA + reduced electron transfer flavoprotein

0

-

1.3.8.1

butyryl-CoA + oxidized acceptor = crotonyl-CoA + reduced acceptor

0

-

1.3.8.1

butanoyl-CoA + FAD = trans-2,3-dehydrobutanoyl-CoA + FADH2

0

-

1.3.8.4

butyryl-CoA + acceptor = but-2-enoyl-CoA + reduced acceptor

0, 391218, 391201, 391202, 391209

-

1.3.8.4

butyryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + reduced electron-transfer flavoprotein

0

-

1.3.8.5

butyryl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor

0

-

1.3.8.5

butyryl-CoA + electron-transfer flavoprotein = but-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+

0

-

1.3.8.6

glutaryl-CoA + electron transfer flavoprotein = (E)-but-2-enoyl-CoA + CO2 + reduced electron transfer flavoprotein

0

-

1.3.8.6

glutaryl-CoA + FAD = (E)-but-2-enoyl-CoA + CO2 + FADH2

0

-

1.3.8.6

glutaryl-CoA + 2,6-dichlorophenol indophenol = crotonoyl-CoA + CO2 + reduced 2,6-dichlorophenol indophenol

0

-

1.3.8.6

glutaryl-CoA + acceptor = crotonoyl-CoA + CO2 + reduced acceptor

0

-

1.3.8.6

glutaryl-CoA + electron transfer flavoprotein = crotonoyl-CoA + CO2 + reduced electron transfer flavoprotein

0

-

1.3.8.6

glutaryl-CoA + electron transfer protein = crotonoyl-CoA + CO2 + reduced electron transfer protein

0

-

1.3.8.6

glutaryl-CoA + FAD = crotonoyl-CoA + CO2 + FADH2

0

-

1.3.8.6

proteo-glutaryl-CoA + acceptor = crotonoyl-CoA + CO2 + reduced acceptor

0

-

1.3.8.6

glutaconyl-CoA + acceptor = crotonyl-CoA + CO2 + reduced acceptor

391418, 0

-

1.3.8.6

glutaconyl-CoA + ferrocenium hexafluorophosphate = crotonyl-CoA + CO2 + ferricenium hexafluorophosphate

0

-

1.3.8.6

glutaryl-CoA + acceptor = crotonyl-CoA + CO2 + reduced acceptor

0, 391406, 391409, 391410, 391408, 391417, 391412, 391293, 391407, 391413

-

1.3.8.6

glutaryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + CO2 + reduced electron-transfer flavoprotein

0

-

1.3.8.6

glutaryl-CoA + ferricenium hexafluorophosphate = crotonyl-CoA + CO2 + ferrocenium hexafluorophosphate

0

-

1.3.8.6

glutaryl-CoA + human electron-transfer flavoprotein = crotonyl-CoA + CO2 + reduced human electron-transfer flavoprotein

0

-

1.3.8.6

glutaryl-CoA + phenazine methosulfate = crotonyl-CoA + CO2 + reduced phenazine methosulfate

0

-

1.3.8.7

butanoyl-CoA + electron-transfer flavoprotein = crotonoyl-CoA + reduced electron-transfer flavoprotein

0

-

1.3.8.7

butanoyl-CoA + acceptor = crotonyl-CoA + reduced acceptor

391343, 391201, 0, 391282, 391320, 391331, 391312

-

1.3.8.8

butyryl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein

391282, 391361

-

1.3.8.8

butyryl-CoA + phenazine methosulfate = 2-butenoyl-CoA + reduced phenazine methosulfate

391282

-

2.8.3.1

acetyl-CoA + crotonate = acetate + crotonoyl-CoA

0

-

2.8.3.1

crotonate + acetyl-CoA = acetate + crotonyl-CoA

0

-

1.3.8.1

17 entries

1.3.8.4

2 entries

1.3.8.5

2 entries

1.3.8.6

15 entries

1.3.8.7

2 entries

1.3.8.8

2 entries

2.8.3.1

2 entries

2.8.3.12

acetyl-CoA + crotonate = crotonyl-CoA + acetate

0

-

2.8.3.9

crotonate + acetoacetyl-CoA = crotonyl-CoA + acetoacetate

643838

-

4.2.1.116

(S)-3-hydroxybutyryl-CoA = crotonyl-CoA + H2O

0

-

4.2.1.120

4-hydroxybutanoyl-CoA = (E)-but-2-enoyl-CoA + H2O

0

-

4.2.1.120

4-hydroxybutanoyl-CoA = crotonyl-CoA + H2O

0

-

4.2.1.120

4-hydroxybutyryl-CoA = crotonyl-CoA + H2O

0

-

4.2.1.120

3 entries

4.2.1.150

3-hydroxybutyryl-CoA = crotonyl-CoA + H2O

0

-

4.2.1.17

(S)-3-hydroxybutyryl-CoA = crotonoyl-CoA + H2O

0

-

4.2.1.54

(2R)-2-hydroxybutyryl-CoA = crotonyl-CoA + H2O

33930

-

4.2.1.55

(3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H2O

0

-

4.2.1.55

(3R)-3-hydroxybutanoyl-CoA = crotonyl-CoA + H2O

5792

-

4.2.1.55

3-hydroxybutyryl-CoA = crotonyl-CoA + H2O

0

-

4.3.1.14

L-3-aminobutyryl-CoA = crotonoyl-CoA + NH3

0

-

4.3.1.14

L-3-Aminobutanoyl-CoA = Crotonyl-CoA + NH3

3378, 6044, 0, 6045

-

4.2.1.55

3 entries

4.3.1.14

2 entries

5.3.3.3

vinylacetyl-CoA = (E)-but-2-enoyl-CoA

0

-

6.2.1.17

ATP + crotonate + CoA = AMP + diphosphate + crotonyl-CoA

0

-

6.2.1.2

ATP + crotonate + CoA = AMP + diphosphate + crotonyl-CoA

0

-

6.2.1.40

ATP + crotonate + CoA = AMP + diphosphate + crotonyl-CoA

0

-

6.2.1.44

ATP + crotonate + CoA = AMP + diphosphate + crotonyl-CoA

0

-

6.4.1.4

glutaconyl-CoA + H+ = crotonyl-CoA + CO2

648359

-

7.2.4.5

(2E)-4-carboxybut-2-enoyl-CoA + Na+[side 1] = (2E)-but-2-enoyl-CoA + CO2 + Na+[side 2]

0

-

7.2.4.5

4-carboxybut-2-enoyl-CoA + Na+[side 1] = but-2-enoyl-CoA + CO2 + Na+[side 2]

0, 648362

-

7.2.4.5

glutaconyl-CoA + Na+[side 1] = but-2-enoyl-CoA + CO2 + Na+[side 2]

0, 648362

-

7.2.4.5

glutaconyal-CoA + Na+[side 1] = crotonyl-CoA + CO2 + Na+[side 2]

0

-

7.2.4.5

4 entries

Inhibitor in Enzyme-catalyzed Reactions (14 results)

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Show Inhibitors (14 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.7.4

-

390468

-

1.3.1.44

-

686722

-

1.3.1.9

the addition of short-chain crotonoyl-CoA actually inhibits the oxidation of NADH by recombinant ENR in a dose-dependent manner

686787

-

1.3.8.1

competitive product inhibition

391272, 391287

-

1.3.8.5

0.1 mM, 53% inhibition

391254

-

1.3.8.5

-

12302

-

1.3.8.5

2 entries

1.3.8.6

-

391408

-

1.3.8.7

-

391320, 391358

-

2.3.1.157

-

756049

-

2.3.1.85

dehydrase activity

487573

-

4.2.1.150

-

33729

-

4.2.1.150

the enzyme is markedly sensitive to inhibition by crotonyl-CoA at concentrations greater than about 0.075 mM

33715

-

4.2.1.150

2 entries

4.2.1.17

-

33729

-

4.2.1.18

-

664032

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (65 results)

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Show Turnover Number (65 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.1.104

0.009627

-

at pH 7.0 and 25°C

763903

1.3.1.44

0.73

-

mutant Y240F, pH not specified in the publication, temperature not specified in the publication

724351

1.3.1.44

0.73

-

pH and temperature not specified in the publication, mutant Y240F

724351

1.3.1.44

7.1

-

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

724351

1.3.1.44

7.1

-

pH and temperature not specified in the publication, mutant I287A

724351

1.3.1.44

15.6

-

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

724351

1.3.1.44

15.6

-

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

724351

1.3.1.44

18.9

-

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

724351

1.3.1.44

18.9

-

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

724351

1.3.1.44

37

-

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

724351

1.3.1.44

37

-

pH and temperature not specified in the publication, mutant L291A

724351

1.3.1.44

73

-

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

724351

1.3.1.44

73

-

pH and temperature not specified in the publication, mutant F295A

724351

1.3.1.44

91

-

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

724351

1.3.1.44

91

-

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

724351

1.3.1.44

92

-

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

724351

1.3.1.44

92

-

pH and temperature not specified in the publication, mutant Y370A

724351

1.3.1.85

0.0675

-

mutant enzyme V350G, pH and temperature not specified in the publication

739852

1.3.1.85

0.1197

-

mutant enzyme V350A, pH and temperature not specified in the publication

739852

1.3.1.85

0.1263

-

mutant enzyme V350F, pH and temperature not specified in the publication

739852

1.3.1.85

0.1519

-

mutant enzyme A182L, pH and temperature not specified in the publication

739852

1.3.1.85

0.172

-

mutant enzyme T82D, at pH 8.0 and 30°C

760072

1.3.1.85

0.1755

-

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

739852

1.3.1.85

1.79

-

mutant enzyme S119A, at pH 8.0 and 30°C

760072

1.3.1.85

5

-

mutant enzyme H365N, at pH 8.0 and 30°C

760072

1.3.1.85

5.1

-

mutant enzyme E171A, at pH 8.0 and 30°C

760072

1.3.1.85

8.3

-

mutant enzyme F170A, at pH 8.0 and 30°C

760072

1.3.1.85

83

-

mutant enzyme F170Y, at pH 8.0 and 30°C

760072

1.3.1.85

103

-

wild type enzyme, at pH 8.0 and 30°C

760072

1.3.1.44

16 entries

1.3.1.85

12 entries

1.3.1.86

19

-

pH 7.5, temperature not specified in the publication

725287

1.3.1.9

0.00278

-

-

390892

1.3.1.9

3.6

-

pH 6.8, 25°C

725221

1.3.1.9

5.3

-

at pH 7.5 and 30°C

739906

1.3.1.9

6.2

-

pH 7.5, 25°C

724889

1.3.1.9

22.25

-

pH 7.5, 25°C

726284

1.3.1.9

100

-

pH 5.5, 30°C

763022

1.3.8.1

19

-

pH 7.5, 37°C

725287

1.3.8.1

19

-

pH 7.5, temperature not specified in the publication

725287

1.3.1.9

6 entries

1.3.8.1

2 entries

1.3.8.7

0.00233

0.00783

hydratase activity, value depending on pH

391329

2.3.1.31

15

-

-

486788

2.3.1.85

6

-

didomain construct, pH not specified in the publication, 25°C

755686

2.3.3.13

0.04

-

hydrolysis, presence of MgCl2, pH 7.4, 25°C

672203

2.3.3.13

0.05

-

hydrolysis, absence of MgCl2, pH 7.4, 25°C

672203

2.7.8.7

0.005

-

pH 7.5, 22°C

674285

2.7.8.7

0.2

-

pH 7.5, 22°C

674285

2.3.3.13

2 entries

2.7.8.7

2 entries

3.1.2.2

0.0078

-

pH 7.5

679171

3.1.2.20

0.0076

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

0.014

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

0.92

-

absorbance of 5-thio-2-nitrobenzoate formed by reaction of 5,5'-dithiobis(2-nitrobenzoic acid) is measured

690932

3.1.2.20

11

-

pH 7.5, 37°C

732296

4.2.1.119

0.38

-

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

714098

4.2.1.119

2.3

-

-

684952

4.2.1.150

14.9

-

pH 7.0, 50°C, recombinant His-tagged enzyme

748405

4.2.1.150

19

-

pH 8.0, 70°C

726748

4.2.1.17

0.0011

-

pH 7.4, 25°C, mutant enzyme G141P

650113

4.2.1.17

0.0053

-

pH 7.4, 25°C, mutant enzyme E164Q

650113

4.2.1.17

0.53

-

pH 7.4, 25°C, mutant enzyme A98P

650113

4.2.1.17

0.6

-

pH 7.4, 25°C, mutant enzyme E144Q

650113

4.2.1.17

1.5

-

pH 7.4, 25°C, mutant enzyme E164D

650113

4.2.1.17

19

-

at pH 7.0 and 70°C

726748

4.2.1.17

1790

-

-

651567

4.2.1.17

1790

-

pH 7.4, 25°C, wild-type enzyme

650113

4.2.1.17

2238

-

pH 8.0, 22°C, wild-type enzyme

649889

4.2.1.17

5667

-

pH 7.5, 25°C

33730

3.1.2.20

4 entries

4.2.1.119

2 entries

4.2.1.150

2 entries

4.2.1.17

10 entries

4.2.1.18

6.8

-

-

679737

K_M Value (112 results)

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Show KM Value (112 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.10

0.00963

-

pH 7.0, 25°C

762612

1.3.1.104

0.009627

-

at pH 7.0 and 25°C

763903

1.3.1.38

0.072

-

-

390748

1.3.1.39

0.0478

-

pH 7.5, 25°C

726431

1.3.1.44

0.0027

-

in potassium phosphate buffer pH 6.2, at 30°C

686722

1.3.1.44

0.049

-

mutant Y240F, pH not specified in the publication, temperature not specified in the publication

724351

1.3.1.44

0.049

-

pH and temperature not specified in the publication, mutant Y240F

724351

1.3.1.44

0.06

-

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

724351

1.3.1.44

0.06

-

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

724351

1.3.1.44

0.068

-

pH 6.2, 30°C

656287

1.3.1.44

0.068

-

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

656287

1.3.1.44

0.07

-

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

724351

1.3.1.44

0.07

-

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

724351

1.3.1.44

0.1

-

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

724351

1.3.1.44

0.1

-

pH and temperature not specified in the publication, mutant F295A

724351

1.3.1.44

0.11

-

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

724351

1.3.1.44

0.11

-

pH and temperature not specified in the publication, mutant L291A

724351

1.3.1.44

0.15

-

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

724351

1.3.1.44

0.15

-

pH and temperature not specified in the publication, mutant Y370A

724351

1.3.1.44

0.16

-

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

724351

1.3.1.44

0.16

-

pH and temperature not specified in the publication, mutant I287A

724351

1.3.1.44

0.21

-

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

724351

1.3.1.44

0.21

-

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

724351

1.3.1.8

0.0033

-

-

390852

1.3.1.8

0.02

-

-

390753

1.3.1.85

0.01

-

mutant enzyme F170Y, at pH 8.0 and 30°C

760072

1.3.1.85

0.0134

-

mutant enzyme T82D, at pH 8.0 and 30°C

760072

1.3.1.85

0.021

-

wild type enzyme, at pH 8.0 and 30°C

760072

1.3.1.85

0.0298

-

mutant enzyme H365N, at pH 8.0 and 30°C

760072

1.3.1.85

0.031

-

mutant enzyme F170A, at pH 8.0 and 30°C

760072

1.3.1.85

0.036

-

mutant enzyme S119A, at pH 8.0 and 30°C

760072

1.3.1.85

0.2

-

for reduction, pH and temperature not specified in the publication

713409

1.3.1.85

0.4

-

for reductive carboxylation, pH and temperature not specified in the publication

713409

1.3.1.85

0.4

-

in 100 mM Tris-HCl buffer (pH 7.9), temperature not specified in the publication

689745

1.3.1.85

0.49

-

mutant enzyme V350F, pH and temperature not specified in the publication

739852

1.3.1.85

0.5

-

mutant enzyme E171A, at pH 8.0 and 30°C

760072

1.3.1.85

1.17

-

mutant enzyme V350G, pH and temperature not specified in the publication

739852

1.3.1.85

1.21

-

mutant enzyme V350A, pH and temperature not specified in the publication

739852

1.3.1.85

1.31

-

mutant enzyme A182L, pH and temperature not specified in the publication

739852

1.3.1.85

1.58

-

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

739852

1.3.1.86

0.0025

-

pH 7.5, temperature not specified in the publication

725287

1.3.1.86

0.0033

-

in 200 mM potassium phosphate buffer, pH 6.8, at 26°C

390852

1.3.1.86

0.018

-

in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 1 mM dithioerythritol and 10% (v/v) glycerol, at 30°C

711884

1.3.1.9

0.007

-

-

689919

1.3.1.9

0.0138

-

pH 7, 25°C

763733

1.3.1.9

0.0175

-

at pH 7.5 and 28°C

741373

1.3.1.9

0.04

-

in 100 mM sodium phosphate (pH 7.5)

689328

1.3.1.9

0.063

-

pH 7.5, 25°C

724889

1.3.1.9

0.165

-

-

390898

1.3.1.9

0.178

-

-

390877

1.3.1.9

0.188

-

pH 6.8, 25°C

725221

1.3.1.9

0.288

-

in 10 mM sodium phosphate, pH 7.2, at 25°C

689612

1.3.1.9

0.293

-

pH 7.5, 25°C

726284

1.3.1.9

0.457

-

K0.5 value, Hill coefficient 1.5, pH 8, 30°C

763271

1.3.1.9

0.667

-

reductase I

285669

1.3.1.9

1.178

-

native enzyme, in 0.1 M sodium phosphate buffer (pH 7)

687702

1.3.1.9

1.26

-

pH 5.5, 30°C

763022

1.3.1.9

2.5

-

-

390500

1.3.1.9

4

-

-

390892

1.3.1.9

4.6

-

at pH 7.5 and 30°C

739906

1.3.1.44

19 entries

1.3.1.8

2 entries

1.3.1.85

15 entries

1.3.1.86

3 entries

1.3.1.9

17 entries

1.3.1.95

0.008

-

in 0.1 M phosphate buffer pH 6.4, at 22°C

696519

1.3.8.1

0.0025

-

pH 7.5, 37°C

725287

1.3.8.1

0.0025

-

pH 7.5, temperature not specified in the publication

725287

1.3.8.1

0.008

-

22°C, pH 6.4

696519

1.3.8.1

3 entries

1.3.8.6

0.004

-

-

391418

1.3.8.7

0.016

0.038

hydratase reaction, value depending on pH

391329

2.3.1.31

0.13

-

-

486788

2.3.1.85

0.00136

-

didomain construct, pH not specified in the publication, 25°C

755686

2.3.3.13

0.05

-

hydrolysis, absence of MgCl2, pH 7.4, 25°C

672203

2.3.3.13

0.95

-

hydrolysis, presence of MgCl2, pH 7.4, 25°C

672203

2.7.8.7

0.0052

-

pH 7.5, 22°C

674285

2.7.8.7

0.018

-

pH 7.5, 22°C

674285

2.3.3.13

2 entries

2.7.8.7

2 entries

2.8.3.9

0.167

-

pH 7.0, 25°C, cosubstrate acetoacetate

643838

3.1.2.2

0.08735

-

pH 7.5

679171

3.1.2.20

0.0059

-

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

690932

3.1.2.20

0.0682

-

pH 7.5, 37°C

732296

3.1.2.20

0.18

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

0.22

-

wild-type protein, pH7.5, 25°C

707486

4.2.1.119

0.024

-

pH 8, 30°C, wild-type

649389

4.2.1.119

0.029

-

pH 8.0, 30°C

33736

4.2.1.119

0.03

-

-

33737

4.2.1.119

0.033

-

pH 8, 30°C, L65A mutant

649389

4.2.1.119

0.0853

-

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

714098

4.2.1.119

0.11

-

pH 8.0, 25°C

697692

4.2.1.119

0.154

-

pH 8, 30°C, V130G mutant

649389

4.2.1.119

60

-

-

684952

4.2.1.149

0.038

-

at pH 7.5 and 37°C

726932

4.2.1.149

0.52

-

37°C, pH 7.5

724139

4.2.1.150

0.03

-

25°C, pH 7.5

33729

4.2.1.150

0.03

-

at pH 8.0 and 25°C

33715

4.2.1.150

0.03

-

pH 7.0, 50°C, recombinant His-tagged enzyme

748405

4.2.1.150

0.07

-

pH 8.0, 70°C

726748

4.2.1.150

0.3

-

pH 8.0, 65°C

727751

4.2.1.17

0.003

-

pH 7.4, 25°C, mutant enzyme G141P

650113

4.2.1.17

0.013

-

pH 9.0

5866

4.2.1.17

0.015

-

pH 7.4, 25°C, wild-type enzyme

650113

4.2.1.17

0.022

-

pH 8, 25°C

33718

4.2.1.17

0.025

-

pH 7.4, 25°C, mutant enzyme E144Q

650113

4.2.1.17

0.03

-

25°C

33729

4.2.1.17

0.032

-

pH 7.4, 25°C, mutant enzyme E164D

650113

4.2.1.17

0.041

-

pH 7.4, 25°C, mutant enzyme E164Q

650113

4.2.1.17

0.0499

-

pH 8.0, 22°C, wild-type enzyme

649889

4.2.1.17

0.05

-

-

700005, 651567

4.2.1.17

0.07

-

at pH 7.0 and 70°C

726748

4.2.1.17

0.195

-

pH 7.4, 25°C, mutant enzyme A98P

650113

3.1.2.20

4 entries

4.2.1.119

8 entries

4.2.1.149

2 entries

4.2.1.150

5 entries

4.2.1.17

12 entries

4.2.1.18

12.1

-

-

679737

4.2.1.55

0.00926

-

-

5792

4.3.1.14

0.045

-

-

6045

4.3.1.14

55

-

-

680885

6.4.1.4

0.11

-

-

1896

6.4.1.4

0.138

-

-

1886

6.4.1.4

0.225

-

-

1884

4.3.1.14

2 entries

6.4.1.4

3 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

1.2.7.4

1.4

-

inhibition of CO/acetyl-CoA exchange reaction

390468

1.3.1.44

0.000198

-

in potassium phosphate buffer pH 6.2, at 30°C

686722

1.3.8.1

0.00036

-

-

391287

1.3.8.1

0.0102

-

-

391272

1.3.8.7

0.0144

-

uncompetitive vs. electron transferring flavoprotein

391358

1.3.8.7

0.015

-

-

391320

1.3.8.7

0.0165

0.0184

competitive vs. butanoyl-CoA

391358

1.3.8.1

2 entries

1.3.8.7

3 entries

4.2.1.18

0.0949

-

pH 7.9, 25°C, wild-type enzyme

664032

IC₅₀ Value (1 result)

top print hide

Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

2.3.1.157

1

-

pH 7.5, 30°C

756049

References & Links

Literature References (217)

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Show Reference (217 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1873

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Metabolism of propionic acid in animal tissues. VIII. Crystalline propionyl carboxylase

1961

Kaziro, Y.; Ochoa, S.; Warner, R.C.; Chen, J.Y.

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236

1917-1923

1884

7469416

Isolation of 3-methylcrotonyl-coenzyme A carboxylase from bovine kidney

1980

Lau, E.P.; Cochran, B.C.; Fall, R.R.

Arch. Biochem. Biophys.

205

352-359

1886

7278686

3-Methylcrotonyl-CoA and geranyl-CoA carboxylases from Pseudomonas citronellolis

1981

Fall, R.R.

Methods Enzymol.

71

791-799

1896

8161223

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

1994

Diez, T.A.; Wurtele, E.S.; Nikolau, B.J.

Arch. Biochem. Biophys.

310

64-75

2207

7012144

The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli

1981

Pawar, S.; Schulz, H.

J. Biol. Chem.

256

3894-3899

2966

8344309

Purification and properties of an iron-sulfur and FAD-containing 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA DELTA3-DELTA2-isomerase from Clostridium aminobutyricum

1993

Scherf, U.; Buckel, W.

Eur. J. Biochem.

215

421-429

3378

6811551

Pathway of lysine degradation in Fusobacterium nucleatum

1982

Barker, H.A.; Kahn, J.M.; Hedrick, L.

J. Bacteriol.

152

201-207

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

6044

7410315

Enzymes involved in 3,5-diaminohexanoate degradation by Brevibacterium sp.

1980

Barker, H.A.; Kahn, J.M.; Chew, S.

J. Bacteriol.

143

1165-1170

6045

4420467

Purification and properties of L-3-aminobutyryl coenzyme A deaminase from a lysine-fermenting Clostridium

1974

Jeng, I.M.; Barker, H.A.

J. Biol. Chem.

249

6578-6584

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

33713

6378901

Binding of the enzymes of fatty acid beta-oxidation and some related enzymes to pig heart inner mitochondrial membrane

1984

Sumegi, B.; Srere, P.A.

J. Biol. Chem.

259

8748-8752

33715

7024731

Enoyl-CoA hydratases from Clostridium acetobutylicum and Escherichia coli

1981

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

Methods Enzymol.

71

421-430

33718

1416981

Inhibition of enoyl-CoA hydratase by long-chain L-3-hydroxyacyl-CoA and its possible effect on fatty acid oxidation

1992

He, X.Y.; Yang, S.Y.; Schulz, H.

Arch. Biochem. Biophys.

298

527-531

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

33926

-

Lactyl-CoA dehydrase

1966

Baldwin, R.L.; Wood, W.A.

Methods Enzymol.

9

683-685

33929

3026450

Fe-S centers in lactyl-CoA dehydratase

1986

Kuchta, R.D.; Hanson, G.R.; Holmquist, B.; Abeles, R.H.

Biochemistry

25

7301-7307

33930

1597194

(R)-lactyl-CoA dehydratase from Clostridium propionicum. Stereochemistry of the dehydration of (R)-2-hydroxybutyryl-CoA to crotonyl-CoA

1992

Hofmeister, A.E.M.; Buckel.W.

Eur. J. Biochem.

206

547-552

94488

16667687

Identification and characterization of mitochondrial acetyl-coenzyme A hydrolase from Pisum sativum L. seedlings

1990

Zeiher, C.A.; Randall, D.D.

Plant Physiol.

94

20-27

285669

7125663

The procaryotic nature of the fatty acid synthetase of developing Carthamus tinctorius L. (Safflower) seeds

1982

Shimakata, T.; Stumpf, P.K.

Arch. Biochem. Biophys.

217

144-154

286051

35524

Enzymology of butyrate formation by Butyrivibrio fibrisolvens

1979

Miller, T.L.; Jenesel, S.E.

J. Bacteriol.

138

99-104

286058

8655474

Cloning, sequencing, and expression of clustered genes encoding beta-hydroxybutyryl-coenzyme A (CoA) dehydrogenase, crotonase, and butyryl-CoA dehydrogenase from Clostridium acetobutylicum ATCC 824

1996

Boynton, Z.L.; Bennett, G.N.; Rudolph, F.B.

J. Bacteriol.

178

3015-3024

390468

2905170

Kinetic characterization of the carbon monoxide-acetyl-CoA (carbonyl group) exchange activity of the acetyl-CoA synthesizing CO dehydrogenase from Clostridium thermoaceticum

1988

Raybuck, S.A.; Bastian, N.R.; Orme-Johnson, W.H.; Walsh, C.T.

Biochemistry

27

7698-7702

390500

4384650

Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli

1968

Weeks, G.; Wakil, S.J.

J. Biol. Chem.

243

1180-1189

390505

11007778

The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis

2000

Heath, R.J.; Su, N.; Murphy, C.K.; Rock, C.O.

J. Biol. Chem.

275

40128-40133

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

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

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

390761

-

Comparison of two unusual enoyl-CoA reductases in Streptomyces collinus

1993

Reynolds, K.A.

J. Nat. Prod.

56

175-185

390806

3102464

Purification and some properties of short chain-length specific trans-2-enoyl-CoA reductase in mitochondria of Euglena gracilis

1986

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

J. Biochem.

100

995-1000

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

390849

6501266

Purification of NADPH-dependent enoyl-CoA reductase involved in the malonyl-CoA dependent fatty acid elongation system of Mycobacterium smegmatis

1984

Kikuchi, S.; Kusaka, T.

J. Biochem.

96

841-848

390850

-

Activation and inhibition of crotonyl-coenzyme A reductase activity of bovine mammary fatty acid synthetase

1979

Strom, K.A.; Kumar, S.

J. Biol. Chem.

254

8159-8162

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

390852

4149043

Crotonyl coenzyme A reductase activity of bovine mammary fatty acid synthetase

1974

Maitra, S.K.; Kumar, S.

J. Biol. Chem.

249

111-117

390875

2706276

Inhibition and covalent modification of rape seed (Brassica napus) enoyl ACP reductase by phenylglyoxal

1989

Cottingham, I.R.; Austin, A.J.; Slabas, A.R.

Biochim. Biophys. Acta

995

273-278

390876

-

Purified enoyl-[acyl-carrier-protein] reductase frome rape seed (Brassica napus) contains two closely related polypeptides which differ by a six-amino-acid N-terminal extension

1988

Cottingham, I.R.; Austin, A.; Sidebottom, C.; Slabas, A.R.

Biochim. Biophys. Acta

854

201-207

390877

-

Induction, purification and characterization of NADH-specific enoyl acyl carrier protein reductase from developing seeds of oil seed rape (Brassica napus)

1986

Slabas, A.R.; Sidebottom, C.M.; Hellyer, A.; Kessell, R.M.J.; Tombs, M.P.

Biochim. Biophys. Acta

877

271-280

390887

3732599

Oilseed rape NADH enoyl acyl-carrier protein reductase

1986

Slabas, A.R.; Sidebottom, C.M.; Kessell, R.M.J; Hellyer, A.; Tombs, M.P.

Biochem. Soc. Trans.

14

581-582

390892

10493822

Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan

1999

Ward, W.H.J.; Holdgate, G.A.; Rowsell, S.; McLean, E.G.; Pauptit, R.A.; Clayton, E.; Nichols, W.W.; Colls, J.G.; Minshull, C.A.; Jude, D.A.; Mistry, A.; Timms, D.; Camble, R.; Hales, N.J.; Britton, C.J.; Taylor, I.W.F.

Biochemistry

38

12514-12525

390897

11368521

Enoyl-ACP reductase (FabI) of Haemophilus influenzae: steady-state kinetic mechanism and inhibition by triclosan and hexachlorophene

2001

Marcinkeviciene, J.; Jiang, W.; Kopcho, L.M.; Locke, G.; Luo, Y.; Copeland, R.A.

Arch. Biochem. Biophys.

390

101-108

390898

11735121

Kinetic determinants of the interaction of enoyl-ACP reductase from Plasmodium falciparum with its substrates and inhibitors

2001

Kapoor, M.; Jamal Dar, M.; Surolia, A.; Surolia, N.

Biochem. Biophys. Res. Commun.

289

832-837

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

391199

2777793

Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family

1989

Matsubara, Y.; Indo, Y.; Naito, E.; Ozasa, H.; Glassberg, R.; Vockley, J.; Ikeda, Y.; Kraus, J.; Tanaka, K.

J. Biol. Chem.

264

16321-16331

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

391202

6401713

Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria

1983

Ikeda, Y.; Tanaka, K.

J. Biol. Chem.

258

1077-1085

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

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

391256

2331485

Selective inactivation of various acyl-CoA dehydrogenases by (methylenecyclopropyl)acetyl-CoA

1990

Ikeda, Y.; Tanaka, K.

Biochim. Biophys. Acta

1038

216-221

391259

2802610

Glucose metabolism and NADH recycling by Treponema hyodysenteriae, the agent of swine dysentery

1989

Stantom, T.B.

Appl. Environ. Microbiol.

55

2365-2371

391261

3580384

CoA-persulphide: a possible in vivo inhibitor of mammalian short-chain acyl-CoA dehydrogenase

1987

Shaw, L.; Engel, P.C.

Biochim. Biophys. Acta

919

171-174

391264

3607039

Regulation of the butyryl-CoA dehydrogenase by substrate and product binding

1987

Stankovich, M.T.; Soltysik, S.

Biochemistry

26

2627-2632

391266

3790549

Oxidation-reduction potentials of butyryl-CoA dehydrogenase

1986

Fink, C.W.; Stankovich, M.T.; Soltysik, S.

Biochemistry

25

6637-6643

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

391276

6712627

The purification and properties of ox liver short-chain acyl-CoA dehydrogenase

1984

Shaw, L.; Engel, P.C.

Biochem. J.

218

511-520

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

391287

-

Acyl Coenzyme A dehydrogenase

1963

Beinert, H.

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

7

447-466

391291

5550959

Stereochemie der Butyryl-CoA-Dehydrogenase in Clostridium kluyveri

1971

La Roche, H.J.; Kellner, M.; Gunther, H.; Simon, H.

Hoppe-Seyler's Z. Physiol. Chem.

352

399-402

391293

6261796

Mechanism of action of glutaryl-CoA and butyryl-CoA dehydrogenases. Purification of glutaryl-CoA dehydrogenase

1981

Gomes, B.; Fendrich, G.; Abeles, R.H.

Biochemistry

20

1481-1490

391297

-

Crotonase activity in preparations of butyryl-CoA dehydrogenase from Megasphaera elsdenii

1986

Ellison, P.A.; Engel, P.C.

Biochem. Soc. Trans.

14

158-159

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

391303

-

Evidence of reversed electron transport in syntrophic butyrate or benzoate oxidation by Syntrophomonas wolfei and Syntrophus buswellii

1994

Wallrabenstein, C.; Schink, B.

Arch. Microbiol.

162

136-142

391308

9009069

NAD-independent lactate and butyryl-CoA dehydrogenases of Clostridium acetobutylicum P262

1997

Diez-Gonzalez, F.; Russell, J.B.; Hunter, J.B.

Curr. Microbiol.

34

162-166

391310

9671517

Oxidase activity of the acyl-CoA dehydrogenases

1998

DuPlessis, E.R.; Pellett, J.; Stankovich, M.T.; Thorpe, C.

Biochemistry

37

10469-10477

391312

2340267

Regulation of the redox potential of general acyl-CoA dehydrogenase by substrate binding

1990

Lenn, N.D.; Stankovich, M.T.; Liu, H.W.

Biochemistry

29

3709-3715

391320

3219356

Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple. A new investigation of the rapid reaction kinetics

1988

Schopfer, L.M.; Massey, V.; Ghisla, S.; Thorpe, C.

Biochemistry

27

6599-6611

391329

3756134

Medium-chain acyl coenzyme A dehydrogenase from pig kidney has intrinsic enoyl coenzyme A hydratase activity

1986

Lau, S.M.; Powell, P.; Buettner, H.; Ghisla, S.; Thorpe, C.

Biochemistry

25

4184-4189

391331

3711105

Energetics of beta-oxidation. Reduction potentials of general fatty acyl-CoA dehydrogenase, electron transfer flavoprotein, and fatty acyl-CoA substrates

1986

Gustafson, W.G.; Feinberg, B.A.; McFarland, J.T.

J. Biol. Chem.

261

7733-7741

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

391358

429316

General acyl-CoA dehydrogenase from pig liver. Kinetic and binding studies

1979

McKean, M.C.; Frerman, F.E.; Mielke, D.M.

J. Biol. Chem.

254

2730-2735

391361

1015826

Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef hart mitochondria

1976

Hall, C.L.; Heijkenskjöld, L.; Bartfai, T.; Ernster, L.; Kamin, H.

Arch. Biochem. Biophys.

177

402-414

391406

2340266

Spectral and electrochemical properties of glutaryl-CoA dehydrogenase from Paracoccus denitrificans

1990

Byron, C.M.; Stankovich, M.T.; Husain, M.

Biochemistry

29

3691-3700

391407

3182847

Conservation of central nervous system glutaryl-coenzyme A dehydrogenase in fruit-eating bats with glutaric aciduria and deficient hepatic glutaryl-coenzyme A dehydrogenase

1988

McMillan, T.A.; Gibson, K.M.; Sweetman, L.; Meyers, G.S.; Green, R.

J. Biol. Chem.

263

17258-17261

391408

3081514

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