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Ligand octanoyl-CoA

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

octane oxidation, tryptophan metabolism

KEGG

Biosynthesis of cofactors, Biosynthesis of secondary metabolites, Fatty acid degradation, Fatty acid elongation, Fatty acid metabolism, Lipoic acid metabolism, Phenazine biosynthesis more

MetaCyc

2-heptyl-3-hydroxy-4(1H)-quinolone biosynthesis, 6-gingerol analog biosynthesis (engineered), fatty acid salvage, grayanate biosynthesis, lipoate biosynthesis and incorporation IV (yeast), octane oxidation, oleate beta-oxidation, penicillin K biosynthesis more

Show all BRENDA pathways known for octanoyl-CoA

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (12 results)

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Show Natural Substrate (12 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.42

octanoyl-CoA + NADPH + H+ = octanal + CoA + NADP+

724299

-

1.3.8.7

octanoyl-CoA + electron transferring flavoprotein = 2-octenoyl-CoA + reduced electron transferring flavoprotein

655491

-

2.3.1.137

L-carnitine + octanoyl-CoA = octanoyl-L-carnitine + CoA

486290, 486291, 486294, 486295, 486296, 486297, 486292, 486293, 486305

-

2.3.1.137

octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine

686028, 659306, 659372, 659511, 657546

-

2.3.1.137

2 entries

2.3.1.20

octanoyl-CoA + 1,2-di-(cis-9-octadecenoyl)-sn-glycerol = CoA + 1,2-di-(cis-9-octadecenoyl)-3-octanoyl-sn-glycerol

735764

-

2.3.1.207

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

719743

-

2.3.1.230

octanoyl-CoA + (2-aminobenzoyl)acetate = 2-heptyl-4-quinolone + CoA + CO2 + H2O

757171

-

2.3.1.273

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

749305

-

2.3.1.301

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

761425

-

2.3.1.B38

octanoyl-CoA + (2-aminobenzoyl)acetate = 2-heptyl-4-quinolone + CoA + CO2 + H2O

756793

-

2.3.1.B38

octanoyl-CoA + 2-aminobenzoylacetate = CoA + 2-heptylquinolin-4(1H)-one + CO2 + H2O

736509

-

2.3.1.B38

2 entries

3.1.2.20

octanoyl-CoA + H2O = octanoate + CoA

665707

-

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

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Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.38

trans-2-octenoyl-CoA + NADPH + H+ = octanoyl-CoA + NADP+

0, 390749

-

2.3.1.137

octanoyl-L-carnitine + CoA = L-carnitine + octanoyl-CoA

0

-

6.2.1.60

ATP + octanoic acid + CoA = AMP + diphosphate + octanoyl-CoA

0

-

Substrate in Enzyme-catalyzed Reactions (91 results)

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Show Substrate (91 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.11.18

octanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyoctanoyl-CoA + succinate + CO2

658428

-

1.2.1.42

octanoyl-CoA + NADPH + H+ = octanal + CoA + NADP+

724299

-

1.2.1.50

octanoyl-CoA + NADPH + H+ = octanal + NADP+

724299

-

1.3.1.85

octanoyl-CoA + NADPH + H+ = ?

724588

-

1.3.3.6

octanoyl-CoA + O2 = trans-2,3-dehydrooctanoyl-CoA + H2O2

763929

-

1.3.3.6

octanoyl-CoA + O2 = trans-2-octenoyl-CoA + H2O2

391043, 391044, 657279, 391057, 391050, 391060

-

1.3.8.1

octanoyl-CoA + electron acceptor = 2-octenoyl-CoA + reduced acceptor

673718

-

1.3.8.1

octanoyl-CoA + electron transfer flavoprotein = octenoyl-CoA + reduced acceptor

672004

-

1.3.8.1

octanoyl-CoA + electron transfer protein = 2-octenoyl-CoA + reduced acceptor

391307

-

1.3.8.1

octanoyl-CoA + Meldola's Blue + iodonitrotetrazolium chloride = 2-octenoyl-CoA + reduced acceptor

391269, 391275

-

1.3.3.6

2 entries

1.3.8.1

4 entries

1.3.8.4

octanoyl-CoA + acceptor = oct-2-enoyl-CoA + reduced acceptor

656288, 391219, 391209

-

1.3.8.5

octanoyl-CoA + electron-transfer flavoprotein = ? + reduced electron-transfer flavoprotein + H+

12302

-

1.3.8.5

octanoyl-CoA + electron-transfer flavoprotein = oct-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+

656288

-

1.3.8.5

2 entries

1.3.8.6

octanoyl-CoA + acceptor = ? + reduced acceptor

671986, 391408

-

1.3.8.7

n-octanoyl-CoA + acceptor = 2-octenoyl-CoA + reduced acceptor

690129

-

1.3.8.7

n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol = 2-octenoyl-CoA + reduced acceptor

391343, 391362, 391201, 391272, 391268, 391203, 391354, 391325

-

1.3.8.7

octanoyl-CoA + 2,6-dichloroindophenol = 2-octenoyl-CoA + reduced 2,6-dichloroindophenol

685352

-

1.3.8.7

octanoyl-CoA + acceptor = 2-octenoyl-CoA + reduced acceptor

685133, 671331, 685980

-

1.3.8.7

octanoyl-CoA + electron transferring flavoprotein = 2-octenoyl-CoA + reduced electron transferring flavoprotein

391282, 655491, 391313, 391349, 391357, 391361

-

1.3.8.7

octanoyl-CoA + ferricenium = 2-octenoyl-CoA + reduced acceptor

655491, 654679

-

1.3.8.7

octanoyl-CoA + ferricenium hexafluorophosphate = 2-octenoyl-CoA + ferrocenium hexafluorophosphate

391313

-

1.3.8.7

octanoyl-CoA + ferriocenium hexfluorophosphate = 2-octenoyl-CoA + reduced acceptor

654644

-

1.3.8.7

octanoyl-CoA + meldola's blue = trans-oct-2-enoyl-CoA + reduced meldola's blue

391313

-

1.3.8.7

octanoyl-CoA + oxidized electron transfer flavoprotein = ? + reduced electron transfer flavoprotein

674476

-

1.3.8.7

octanoyl-CoA + phenazine ethosulfate = trans-oct-2-enoyl-CoA + reduced phenazine ethosulfate

391313

-

1.3.8.7

octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol = 2-octenoyl-CoA + reduced acceptor

657278, 672585

-

1.3.8.7

octanoyl-CoA + recombinant beta-Y16L electron transferring flavoprotein = trans-oct-2-enoyl-CoA + reduced recombinant beta-Y16L electron transferring flavoprotein

391373

-

1.3.8.7

octanoyl-CoA + recombinant electron transferring flavoprotein = trans-oct-2-enoyl-CoA + reduced recombinant electron transferring flavoprotein

391373

-

1.3.8.8

octanoyl-CoA + acceptor = 2-octenoyl-CoA + reduced acceptor

671584

-

1.3.8.8

octanoyl-CoA + acceptor = ?

700578, 700905

-

1.3.8.8

octanoyl-CoA + electron-transfer flavoprotein = 2-octenoyl-CoA + reduced electron-transfer flavoprotein

391371, 391272, 391282, 394650, 391361

-

1.3.8.8

octanoyl-CoA + Meldola's Blue = (2E)-2-octenoyl-CoA + reduced meldola blue

391275

-

1.3.8.8

octanoyl-CoA + phenazine methosulfate = 2-octenoyl-CoA + reduced phenazine methosulfate

394661, 391203, 391272, 391282, 394642, 394667, 391268

-

1.3.8.7

14 entries

1.3.8.8

5 entries

1.3.99.41

caprylyl-CoA + acceptor = ?

763984

-

1.3.99.B2

octanoyl-CoA + 2,6-dichlorophenolindophenol = cis-geranyl-CoA + reduced 2,6-dichlorophenolindophenol

694044

-

2.3.1.13

octanoyl-CoA + glycine = CoA + N-octanoylglycine

486272

-

2.3.1.137

L-carnitine + octanoyl-CoA = octanoyl-L-carnitine + CoA

486290, 486291, 486294, 486295, 486296, 486297, 486292, 486293, 486305

-

2.3.1.137

octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine

686028, 659306, 659372, 486303, 486302, 659511, 657546

-

2.3.1.137

2 entries

2.3.1.15

octanoyl-CoA + sn-glycerol 3-phosphate = CoA + 1-n-octanoyl-sn-glycerol 3-phosphate

486392

-

2.3.1.180

octanoyl-CoA + (3S,5Z,8Z)-3-hydroxytetradeca-5,8-dienoyl-CoA = (5S,7Z,10Z)-2-hexyl-5-hydroxy-3-oxohexadeca-7,10-dienoic acid + ?

757072

5v0p, 3D-view

2.3.1.180

octanoyl-CoA + (3S,5Z,8Z)-3-hydroxytetradeca-5,8-dienoyl-CoA = (5S,7Z,10Z)-2-hexyl-5-hydroxy-3-oxohexadeca-7,10-dienoic acid + ?

757072

5yoa, 3D-view

2.3.1.180

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

665474, 757685, 486937

5v0p, 3D-view

2.3.1.180

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

665474, 757685, 486937

5yoa, 3D-view

2.3.1.180

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

761373

5v0p, 3D-view

2.3.1.180

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

761373

5yoa, 3D-view

2.3.1.181

octanoyl-CoA + [glycine cleavage system 3]-L-lysine = [glycine cleavage system 3]-N6-octanoyl-L-lysine + CoA

737308

-

2.3.1.181

octanoyl-CoA + [oxoglutarate dehydrogenase]-L-lysine = [oxoglutarate dehydrogenase]-N6-octanoyl-L-lysine + CoA

737308

-

2.3.1.181

octanoyl-CoA + [pyruvate dehydrogenase]-L-lysine = [pyruvate dehydrogenase]-N6-octanoyl-L-lysine + CoA

737308

-

2.3.1.180

6 entries

2.3.1.181

3 entries

2.3.1.184

S-adenosyl-L-methionine + octanoyl-CoA = 5'-methylthioadenosine + N-octanoyl-L-homoserine-1,4-lactone + CoA

665363

-

2.3.1.199

octanoyl-CoA + malonyl-CoA = ?

487614

-

2.3.1.20

octanoyl-CoA + 1,2-di-(cis-9-octadecenoyl)-sn-glycerol = CoA + 1,2-di-(cis-9-octadecenoyl)-3-octanoyl-sn-glycerol

735764

-

2.3.1.207

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

719743

-

2.3.1.21

octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine

486534, 486565, 486526, 718967

-

2.3.1.22

n-octanoyl-CoA + sn-2-monooleoylglycerol = CoA + 1-octanoyl-2-oleoylglycerol

486605

-

2.3.1.23

1-palmitoyl-lysophosphatidylcholine + n-octanoyl-CoA = CoA + 1-palmitoyl-2-octanoylphosphatidylcholine

687802

-

2.3.1.230

octanoyl-CoA + (2-aminobenzoyl)acetate = 2-heptyl-4-quinolone + CoA + CO2 + H2O

757171

-

2.3.1.233

octanoyl-CoA + malonyl-CoA = 4-hydroxy-6-(2',4',6'-trioxotridecyl)-2-pyrone + CoA + CO2 + H2O

729961

-

2.3.1.233

octanoyl-CoA = 6-heptyl-4-hydroxy-2-pyrone + 4-hydroxy-6-(2'-oxononyl)-2-pyrone + 4-hydroxy-6-(2',4',6'-trioxotridecyl)-2-pyrone + CoA + CO2 + H2O

729961

-

2.3.1.233

2 entries

2.3.1.250

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

757228

-

2.3.1.253

octanoyl-CoA = 6-heptyl-4-hydroxy-2H-pyran-2-one + 4-hydroxy-6-(2-oxononyl)-2H-pyran-2-one + 4-hydroxyl-6-(2',4',6'-trioxotridecyl)-2-pyrone + 4-hydroxyl-6-(2',4',6',8'-tetraoxopentadecyl)-2-pyrone + CO2 + CoA

740681

-

2.3.1.273

octanoyl-CoA + 2-O-(alpha-D-glucopyranosyl)-D-glycerate = ?

749305

-

2.3.1.273

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

749305

-

2.3.1.301

octanoyl-CoA + malonyl-[AcpM] = 3-oxodecanoyl-[ACP] + CoA + CO2

761437

-

2.3.1.301

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

760679, 761425

-

2.3.1.273

2 entries

2.3.1.301

2 entries

2.3.1.37

octanoyl-CoA + glycine = ? + CoA + CO2

706627

-

2.3.1.38

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

486864, 486866, 486865

6rop, 3D-view

2.3.1.47

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

758497

-

2.3.1.7

octanoyl-CoA + carnitine = CoA + O-octanoylcarnitine

672172, 756901, 659372

-

2.3.1.7

octanoyl-CoA + carnitine = octanoylcarnitine + CoASH

486295, 487416, 487427, 487407, 487408

-

2.3.1.7

octanoyl-CoA + L-carnitine = CoA + O-octanoylcarnitine

735697

-

2.3.1.74

malonyl-CoA + octanoyl-CoA = 1-(2,4,6-trihydroxyphenyl)-octan-1-one + CoA + CO2

487467

-

2.3.1.74

malonyl-CoA + octanoyl-CoA = 6-heptyl-4-hydroxy-2H-pyran-2-one + CoA + CO2

757938

-

2.3.1.74

malonyl-CoA + octanoyl-CoA = ?

758097, 758151

-

2.3.1.74

octanoyl-CoA + malonyl-CoA = 1-(2,4,6-trihydroxyphenyl)-octan-1-one + CoA + CO2

663042

-

2.3.1.75

octanoyl-CoA + hexadecan-1-ol = ?

756245

-

2.3.1.75

octanoyl-CoA + hexadecanol = CoA + hexadecyl octanoate

756245

-

2.3.1.7

3 entries

2.3.1.74

4 entries

2.3.1.75

2 entries

2.3.1.76

octanoyl-CoA + retinol = CoA + retinyloctanoate

487488

-

2.3.1.85

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

755686

6rop, 3D-view

2.3.1.85

octanoyl-CoA + n malonyl-CoA + 2n NADPH + 2n H+ = a long-chain fatty acid + (n+1) CoA + n CO2 + 2n NADP+

758301

6rop, 3D-view

2.3.1.85

2 entries

2.3.1.86

octanoyl-CoA + malonyl-CoA + NADPH + H+ = ?

487614

-

2.3.1.B38

octanoyl-CoA + (2-aminobenzoyl)acetate = 2-heptyl-4-quinolone + CoA + CO2 + H2O

756793

-

2.3.1.B38

octanoyl-CoA + 2-aminobenzoylacetate = CoA + 2-heptylquinolin-4(1H)-one + CO2 + H2O

736509

-

2.3.1.B38

2 entries

2.3.3.2

octanoyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxydecane-1,2,3-tricarboxylate + CoA

488156

-

2.3.3.20

octanoyl-CoA + H2O = ?

745284

-

3.1.2.1

octanoyl-CoA = octanoate + CoA

94468, 94476

-

3.1.2.19

octanoyl-CoA + H2O = CoA + octanoate

646111

-

3.1.2.2

octanoyl-CoA + H2O = CoA + octanoate

646175, 646162, 646179, 646176, 646181, 646166, 646199, 646200, 682542

-

3.1.2.20

n-octanoyl-CoA + H2O = CoA + n-octanoate

690932, 707486

-

3.1.2.20

octanoyl-CoA + H2O = CoA + octanoate

646175, 646162, 646179, 646176, 646181, 646166, 646199, 646200, 698975

-

3.1.2.20

octanoyl-CoA + H2O = octanoate + CoA

665707

-

3.1.2.20

3 entries

3.1.2.25

octanoyl-CoA + H2O = octanoate + CoA

751066

-

Product in Enzyme-catalyzed Reactions (31 results)

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Show Product (31 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.10

caprylaldehyde + CoA + NAD+ = caprylyl-CoA + NADH

0

-

1.3.1.118

trans-2-octenoyl-CoA + NADH + H+ = octanoyl-CoA + NAD+

0

-

1.3.1.37

cis-2-octenoyl-CoA + NADPH + H+ = octanoyl-CoA + NADP+

390746, 390747, 390745

-

1.3.1.38

octa-2-enoyl-CoA + NADPH = octanoyl-CoA + NADP+

0

-

1.3.1.38

trans-2-octenoyl-CoA + NADPH + H+ = octanoyl-CoA + NADP+

0, 390749

-

1.3.1.38

trans-2-octenoyl-CoA + NADPH = octanoyl-CoA + NADP+

0, 390749, 390750, 390760

-

1.3.1.38

3 entries

1.3.1.44

trans-2-octenoyl-CoA + NADH = octanoyl-CoA + NAD+

0

-

1.3.1.8

2-cis-octenoyl-CoA + NADPH = octanoyl-CoA + NADP+

390855, 0

-

1.3.1.8

2-trans-octenoyl-CoA + NAD(P)H = octanoyl-CoA + NADP+

0, 390755

-

1.3.1.8

2-trans-octenoyl-CoA + NADPH = octanoyl-CoA + NADP+

0

-

1.3.1.9

octenoyl-CoA + NADH + H+ = octanoyl-CoA + NAD+

0

-

1.3.1.9

trans-2-octenoyl-CoA + NADH + H+ = octanoyl-CoA + NAD+

0

-

2.3.1.137

CoA + L-octanoylcarnitine = octanoyl-CoA + L-carnitine

0

-

2.3.1.137

octanoyl-L-carnitine + CoA = L-carnitine + octanoyl-CoA

0

-

1.3.1.8

3 entries

1.3.1.9

2 entries

2.3.1.137

2 entries

2.3.1.155

3-oxodecanoyl-CoA + CoA = acetyl-CoA + octanoyl-CoA

0

-

2.3.1.16

3-oxodecanoyl-CoA + CoA = acetyl-CoA + octanoyl-CoA

0

-

2.3.1.16

CoA + 3-oxodecanoyl-CoA = acetyl-CoA + octanoyl-CoA

0

-

2.3.1.16

2 entries

2.3.1.7

octanoylcarnitine + CoASH = octanoyl-CoA + carnitine

0

-

2.8.3.1

acetyl-CoA + octanoate = acetate + octanoyl-CoA

0

-

2.8.3.9

octanoate + acetoacetyl-CoA = octanoyl-CoA + acetoacetate

0

-

6.2.1.1

ATP + octanoate + CoA = AMP + diphosphate + octanoyl-CoA

0

-

6.2.1.10

GTP + octanoate + CoA = GDP + phosphate + octanoyl-CoA

0

-

6.2.1.11

ATP + n-caprylate + CoA = AMP + diphosphate + n-capryloyl-CoA

0

-

6.2.1.12

ATP + octanoate + CoA = AMP + diphosphate + octanoyl-CoA

0

-

6.2.1.13

ATP + octanoate + CoA = ADP + phosphate + octanoyl-CoA

0

-

6.2.1.14

ATP + octanoate + CoA = AMP + diphosphate + octanoyl-CoA

0

-

6.2.1.2

ATP + octanoate + CoA = AMP + diphosphate + octanoyl-CoA

0, 650950, 650334, 650831

-

6.2.1.3

ATP + capryloate + CoA = AMP + diphosphate + capryloyl-CoA

0

-

6.2.1.3

ATP + octanoate + CoA = AMP + diphosphate + octanoyl-CoA

0, 649789

-

6.2.1.3

2 entries

6.2.1.30

ATP + caprylate + CoA = AMP + diphosphate + caprylyl-CoA

0

-

6.2.1.60

ATP + octanoic acid + CoA = AMP + diphosphate + octanoyl-CoA

0

-

Inhibitor in Enzyme-catalyzed Reactions (13 results)

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Show Inhibitors (13 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.38

-

390748

-

1.3.8.7

0.0045 mM, 98% inhibition of enoyl-CoA hydratase activity

391329

-

2.3.1.137

substrate inhibition

486291

-

2.3.1.181

0.5 mM, 67% inhibition

663308

-

2.3.1.273

0.16 mM, about 60% inhibition

749305

-

2.3.1.5

0.1 mM, 74% inhibition

657884

-

2.3.1.85

competitively inhibits malonyl-transferase reaction

487576

6rop, 3D-view

2.3.3.10

-

488091

-

2.7.1.33

-

641390

-

3.1.2.17

noncompetitive inhibition

643853

-

4.2.1.17

-

33734, 699508

2dub, 3D-view

4.2.1.17

competitive inhibitor, binding structure, overview

730574

2dub, 3D-view

4.2.1.17

2 entries

5.1.99.1

-

2434

-

3D Structure of Enzyme-Ligand-Complex (PDB) (55 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (55 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.1.1.100

6rop, 3D-view

1.3.1.39

6rop, 3D-view

1.3.99.3

1egc, 3D-view

1.3.99.3

3mde, 3D-view

1.3.99.3

1egc, 3D-view

1.3.99.3

3mde, 3D-view

1.3.99.3

1egc, 3D-view

1.3.99.3

3mde, 3D-view

1.3.99.3

1egc, 3D-view

1.3.99.3

3mde, 3D-view

1.3.99.3

1egc, 3D-view

1.3.99.3

3mde, 3D-view

1.3.99.3

10 entries

2.3.1.176

6hsp, 3D-view

2.3.1.180

5v0p, 3D-view

2.3.1.180

5yoa, 3D-view

2.3.1.180

5v0p, 3D-view

2.3.1.180

5yoa, 3D-view

2.3.1.180

5v0p, 3D-view

2.3.1.180

5yoa, 3D-view

2.3.1.180

5v0p, 3D-view

2.3.1.180

5yoa, 3D-view

2.3.1.180

5v0p, 3D-view

2.3.1.180

5yoa, 3D-view

2.3.1.180

10 entries

2.3.1.38

6rop, 3D-view

2.3.1.39

6rop, 3D-view

2.3.1.41

5yoa, 3D-view

2.3.1.41

6rop, 3D-view

2.3.1.41

5yoa, 3D-view

2.3.1.41

6rop, 3D-view

2.3.1.41

5yoa, 3D-view

2.3.1.41

6rop, 3D-view

2.3.1.41

5yoa, 3D-view

2.3.1.41

6rop, 3D-view

2.3.1.41

5yoa, 3D-view

2.3.1.41

6rop, 3D-view

2.3.1.41

10 entries

2.3.1.85

6rop, 3D-view

3.1.2.14

6rop, 3D-view

3.3.2.12

6jqn, 3D-view

4.2.1.17

2dub, 3D-view

4.2.1.59

6rop, 3D-view

5.3.3.8

1k39, 3D-view

5.3.3.8

1sg4, 3D-view

5.3.3.8

4zdc, 3D-view

5.3.3.8

1k39, 3D-view

5.3.3.8

1sg4, 3D-view

5.3.3.8

4zdc, 3D-view

5.3.3.8

1k39, 3D-view

5.3.3.8

1sg4, 3D-view

5.3.3.8

4zdc, 3D-view

5.3.3.8

1k39, 3D-view

5.3.3.8

1sg4, 3D-view

5.3.3.8

4zdc, 3D-view

5.3.3.8

1k39, 3D-view

5.3.3.8

1sg4, 3D-view

5.3.3.8

4zdc, 3D-view

5.3.3.8

15 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (60 results)

top print hide

Show Turnover Number (60 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.3.6

0.054

-

mutant enzyme Y401F, at pH 7.4 and 30°C

763929

1.3.3.6

0.056

-

mutant enzyme Y232G, at pH 7.4 and 30°C

763929

1.3.3.6

0.07

-

-

391060

1.3.3.6

0.3

-

mutant enzyme Y232F, at pH 7.4 and 30°C

763929

1.3.3.6

0.5

-

mutant enzyme Y232S, at pH 7.4 and 30°C

763929

1.3.3.6

2.18

-

pH 7.4, 30°C, mutant enzyme E421D

657279

1.3.3.6

3.47

-

pH 7.4, 30°C, wild-type enzyme

657279

1.3.3.6

3.47

-

wild type enzyme, at pH 7.4 and 30°C

763929

1.3.8.1

0.00183

-

-

673718

1.3.8.1

0.1

-

-

391269

1.3.8.7

0.0024

-

pH 7.6, 25°C, mutant enzyme E376Q

654644

1.3.8.7

0.038

-

mutant enzyme Y375K, in 50 mM potassium phosphate buffer, pH 7.6

685352

1.3.8.7

0.047

-

25°C, with ferricenium as acceptor, pig enzyme reconstituted with 2'-deoxy-FAD

654679

1.3.8.7

0.071

-

mutant enzyme R256K

657278

1.3.8.7

0.167

-

T255E/E376G double mutant enzyme

391369

1.3.8.7

0.22

-

mutant enzyme Y375A, in 50 mM potassium phosphate buffer, pH 7.6

685352

1.3.8.7

0.37

-

mutant enzyme Y375F, in 50 mM potassium phosphate buffer, pH 7.6

685352

1.3.8.7

3.17

-

-

391329

1.3.8.7

3.17

-

phenazine methosulfate as electron carrier

391359

1.3.8.7

3.2

-

wild-type enzyme

657278

1.3.8.7

3.25

-

phenazine methosulfate and 2,6-dichlorophenolindophenol as electron acceptors

391351

1.3.8.7

3.3

-

C-2 proton/deuteron exchange

391271

1.3.8.7

3.3

-

wild type enzyme, in 50 mM potassium phosphate buffer, pH 7.6

685352

1.3.8.7

8.33

-

with electron transferring flavoprotein as electron carrier

391359

1.3.8.7

11.2

-

general acyl-CoA dehydrogenase

391354

1.3.8.7

13.2

-

T255E mutant enzyme

391369

1.3.8.7

16.2

-

K304E mutant enzyme, ferricenium assay

391370

1.3.8.7

16.3

-

-

391369

1.3.8.7

17

-

pH 7.6, 25°C, wild-type enzyme

654644

1.3.8.7

18.3

-

ferricenium assay

391370

1.3.8.7

18.8

-

25°C, with ferricenium as acceptor, recombinant wild-type enzyme

654679

1.3.8.7

19.2

-

-

391367

1.3.8.7

19.6

-

-

391367, 671331

1.3.8.7

19.6

-

25°C, with ferricenium as acceptor, native enzyme

654679

1.3.8.7

20

-

25°C, with ferricenium as acceptor, pig enzyme reconstituted with commercial FAD

654679

1.3.8.7

27.2

-

-

391271

1.3.8.7

33.3

-

-

391350, 391362

1.3.8.7

35.7

-

-

671331

1.3.3.6

8 entries

1.3.8.1

2 entries

1.3.8.7

28 entries

1.3.8.8

2.25

-

-

394661

2.3.1.137

0.367

-

-

486294

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

0.00033

-

37°C, pH 8.0, cosubstrate: 45 mM 2-O-(alpha-D-glucopyranosyl)-D-glycerate

749305

2.3.1.273

0.002

-

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

749305

2.3.1.273

0.037

-

37°C, pH 8.0, cosubstrate: 45 mM 2-O-[alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-D-glycerate

749305

2.3.1.37

0.00002

-

mutant R85L/T430V, pH 7.5, 30°C

706627

2.3.1.37

0.03

-

mutant R85L, pH 7.5, 30°C

706627

2.3.1.37

0.172

-

mutant R85K, pH 7.5, 30°C

706627

2.3.1.37

0.34

-

wild-type, pH 7.5, 30°C

706627

2.3.1.273

4 entries

2.3.1.37

4 entries

2.3.1.74

0.066

-

pH 8.0, 30°C

663042

2.3.1.75

0.0185

-

isoform WSD4, at pH 7.4 and 37°C

756245

2.3.1.75

0.0185

-

pH 7.4, 37°C, recombinant enzyme

756245

2.3.1.75

0.102

-

isoform WSD5, at pH 7.4 and 37°C

756245

2.3.1.75

0.102

-

pH 7.4, 37°C, recombinant enzyme

756245

2.3.1.75

4 entries

2.3.1.85

4.1

-

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

755686

2.3.1.B38

6.8

-

pH 8.2, temperature not specified in the publication

736509

3.1.2.2

159

-

pH 7.4, 25°C

646199

3.1.2.2

159

-

pH 8.0, 25°C

646199

3.1.2.20

0.0047

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

4.6

-

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

690932

3.1.2.20

159

-

pH 7.4, 25°C

646199

3.1.2.2

2 entries

3.1.2.20

3 entries

K_M Value (89 results)

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Show KM Value (89 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.3.6

0.042

-

-

391050

1.3.3.6

0.043

-

mutant enzyme Y232G, at pH 7.4 and 30°C

763929

1.3.3.6

0.0443

-

pH 7.4, 30°C, wild-type enzyme

657279

1.3.3.6

0.0443

-

wild type enzyme, at pH 7.4 and 30°C

763929

1.3.3.6

0.0502

-

mutant enzyme Y401F, at pH 7.4 and 30°C

763929

1.3.3.6

0.0546

-

pH 7.4, 30°C, mutant enzyme E421D

657279

1.3.3.6

0.0573

-

mutant enzyme Y232S, at pH 7.4 and 30°C

763929

1.3.3.6

0.058

-

-

391043

1.3.3.6

0.061

-

-

391060

1.3.3.6

0.0612

-

mutant enzyme Y232F, at pH 7.4 and 30°C

763929

1.3.3.6

0.087

-

liver enzyme

391044

1.3.8.1

0.0011

-

E368G/G247E double mutant enzyme

391307

1.3.8.1

0.005

-

E368D mutant enzyme

391307

1.3.8.1

0.0081

-

wild-type enzyme

391307

1.3.8.1

0.032

-

-

391275

1.3.8.1

0.04231

-

-

673718

1.3.8.7

0.00084

-

mutant enzyme Y375K, in 50 mM potassium phosphate buffer, pH 7.6

685352

1.3.8.7

0.001

-

-

391346, 391357

1.3.8.7

0.001

-

T255E/E376G double mutant enzyme

391369

1.3.8.7

0.002

-

-

391283

1.3.8.7

0.0021

-

pH 7.6, 25°C, mutant enzyme E376Q

654644

1.3.8.7

0.0022

-

25°C, with ferricenium as acceptor, pig enzyme reconstituted with 2'-deoxy-FAD

654679

1.3.8.7

0.00221

-

-

391354

1.3.8.7

0.0023

-

-

391367, 671331

1.3.8.7

0.0023

-

25°C, with ferricenium as acceptor, native enzyme

654679

1.3.8.7

0.0023

-

wild type enzyme, in 50 mM potassium phosphate buffer, pH 7.6

685352

1.3.8.7

0.0023

-

wild-type enzyme

657278

1.3.8.7

0.00242

-

mutant enzyme Y375F, in 50 mM potassium phosphate buffer, pH 7.6

685352

1.3.8.7

0.0025

-

25°C, with ferricenium as acceptor, recombinant wild-type enzyme

654679

1.3.8.7

0.0026

-

25°C, with ferricenium as acceptor, pig enzyme reconstituted with commercial FAD

654679

1.3.8.7

0.003

-

-

391367

1.3.8.7

0.003

-

pH 7.6, 25°C, wild-type enzyme

654644

1.3.8.7

0.0032

-

-

391275

1.3.8.7

0.0034

-

-

391369

1.3.8.7

0.0035

-

-

391370

1.3.8.7

0.0037

-

wild-type enzyme

655491

1.3.8.7

0.004

-

-

391272, 671331

1.3.8.7

0.0059

-

mutant enzyme K304E

655491

1.3.8.7

0.00684

-

mutant enzyme Y375A, in 50 mM potassium phosphate buffer, pH 7.6

685352

1.3.8.7

0.008

-

T255E mutant enzyme

391369

1.3.8.7

0.0082

-

mutant enzyme R256K

657278

1.3.8.7

0.012

-

K304E mutant enzyme, ferricenium assay

391370

1.3.8.7

1.47

-

with phenazine methosulfate

391203

1.3.8.8

0.0033

-

-

391371

1.3.8.8

0.00471

-

acyl-CoA dehydrogenase activity skin fibroblasts, lab data of a 6-year old male patient with VLCAD deficiency during rhabdomyolysis

700578

1.3.8.8

0.008

-

-

391371

1.3.8.8

0.123

-

-

391272

1.3.8.8

0.23

-

-

391275

1.3.3.6

11 entries

1.3.8.1

5 entries

1.3.8.7

27 entries

1.3.8.8

5 entries

1.3.99.41

0.01

-

pH and temperature not specified in the publication

763984

1.3.99.B2

0.13

-

pH 7.0, 30°C

694044

2.3.1.13

108.6

-

-

486272

2.3.1.13

198

-

-

486272

2.3.1.13

2 entries

2.3.1.137

0.015

-

-

486309

2.3.1.184

0.015

-

pH 8.5, 25°C, recombinant MBP-AinS

665363

2.3.1.199

0.33

-

in 10 mM Tris/maleic acid pH 6.7, 0.65 M mannitol and 0.36 mM EGTA, at 30°C

487614

2.3.1.21

0.0085

-

-

486534

2.3.1.21

0.023

-

-

486565

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: 45 mM 2-O-(alpha-D-glucopyranosyl)-D-glycerate

749305

2.3.1.273

0.03

-

37°C, pH 8.0, cosubstrate: 45 mM 2-O-[alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-D-glycerate

749305

2.3.1.273

0.06

-

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

749305

2.3.1.37

0.0018

-

mutant R85L, pH 7.5, 30°C

706627

2.3.1.37

0.0034

-

wild-type, pH 7.5, 30°C

706627

2.3.1.37

0.0103

-

mutant R85K, pH 7.5, 30°C

706627

2.3.1.37

0.0172

-

mutant R85L/T430V, pH 7.5, 30°C

706627

2.3.1.7

0.011

-

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

659372

2.3.1.7

0.0191

-

-

486295

2.3.1.7

0.025

-

recombinant enzyme from yeast, pH 7.8, 30°C

659372

2.3.1.7

0.0503

-

-

487416

2.3.1.21

2 entries

2.3.1.273

4 entries

2.3.1.37

4 entries

2.3.1.7

4 entries

2.3.1.74

0.0122

-

pH 8.0, 30°C

663042

2.3.1.75

0.01225

-

isoform WSD5, at pH 7.4 and 37°C

756245

2.3.1.75

0.0123

-

pH 7.4, 37°C, recombinant enzyme

756245

2.3.1.75

0.02993

-

isoform WSD4, at pH 7.4 and 37°C

756245

2.3.1.75

0.02993

-

pH 7.4, 37°C, recombinant enzyme

756245

2.3.1.75

4 entries

2.3.1.85

0.00073

-

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

755686

2.3.1.86

0.33

-

-

487614

2.3.1.B38

0.006

-

pH 8.2, temperature not specified in the publication

736509

3.1.2.2

0.007

-

pH 7.8, 22°C

646176

3.1.2.2

0.014

-

pH 7.4, 30°C

646166

3.1.2.2

0.043

-

pH 7.0, 30°C

646179

3.1.2.2

0.118

-

pH 7.4, 25°C

646199

3.1.2.2

0.118

-

pH 8.0, 25°C

646199

3.1.2.20

0.0019

-

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

690932

3.1.2.20

0.007

-

pH 7.8, 22°C

646176

3.1.2.20

0.014

-

pH 7.4, 30°C

646166

3.1.2.20

0.0175

-

pH 8.0

665707

3.1.2.20

0.026

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

0.043

-

pH 7.0, 30°C

646179

3.1.2.20

0.118

-

pH 7.4, 25°C

646199

3.1.2.2

5 entries

3.1.2.20

7 entries

K_i Value (3 results)

top print hide

Show KI Value (3 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.38

0.198

-

-

390748

2.3.3.10

0.0081

-

pH 8.0

488091

3.1.2.17

0.5

-

pH 6.0, 30°C

643853

References & Links

Literature References (174)

top print hide

Show Reference (174 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

2434

2862845

Isolation and characterization of DL-methylmalonyl-coenzyme A racemase from rat liver

1985

Stabler, S.P.; Marcell, P.D.; Allen, R.H.

Arch. Biochem. Biophys.

241

252-264

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

33734

9480773

The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule

1998

Engel, C.K.; Kiema, T.R.; Hiltunen, J.K.; Wierenga, R.K.

J. Mol. Biol.

275

847-859

94468

9939

Studies on rat brain acyl-coenzyme A hydrolase (short chain)

1976

Robinson, J.B.; Mahan, D.E.; Koeppe, R.E.

Biochem. Biophys. Res. Commun.

71

959-965

94476

6136404

Factors affecting the cold inactivation of an acetyl-coenzyme-A hydrolase purified from the supernatant fraction of rat liver

1983

Isohashi, F.; Nakanishi, Y.; Sakamoto, Y.

Eur. J. Biochem.

134

447-452

390745

6751582

Studies on the the metabolism of unsaturated fatty acids. VI. Stereochemical studies of the reaction catalyzed by cis-2-enoyl-coenzyme A reductase of escherichia coli

1982

Mizugaki, M.; Unuma, T.; Nishimaki, T.; Shiraishi, T.; Kawaguchi, A.; Saito, K.; Okuda, S.; Yamanaka, H.

Chem. Pharm. Bull.

30

2155-2160

390746

43196

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

1979

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

Chem. Pharm. Bull.

27

2334-2337

390747

-

Studies on the metabolism of unsaturated fatty acids. V. Isomerization of thiol esters of cis-2-alkenoic acids during their preparation and alkaline hydrolysis

1982

Mizugaki, M.; Ito, Y.; Hoshino, T.; Shiraishi, t.; Yamanaka, H.

Chem. Pharm. Bull.

30

206-213

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

390750

6759504

Studies on the metabolism of unsaturated fatty acids. IX. Stereochemical studies of the reaction catalyzed by trans-2-enoyl-coenzyme A reductase of Escherichia coli

1982

Mizugaki, M.; Nishimaki, T.; Shiraishi, T.; Kawaguchi, A.; Okuda, S.; Yamanaka, H.

J. Biochem.

92

1649-1654

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

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

390855

4763659

Stereospecific hydrogen transfer by NADPH-enoyl coenzyme A reductase to cis- and trans-isomers of 2-enoic acid

1973

Mizugaki, M.; Uchiyama, M.

J. Biochem.

74

691-696

391043

7400120

Purification and properties of acyl-CoA oxidase from rat liver

1980

Osumi, T.; Hashimoto, T.; Ui, N.

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