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Ligand lauroyl-CoA

Basic Ligand Information

Molecular Structure

Related pathways

Pathway Source

Pathways

KEGG

Fatty acid degradation, Fatty acid elongation, Fatty acid metabolism

MetaCyc

(8E,10E)-dodeca-8,10-dienol biosynthesis, acylsucrose biosynthesis (Solanum habrochaites), diacylsucrose biosynthesis (Solanum), lauryl-hydroxychlorobactene glucoside biosynthesis, monoacylsucrose biosynthesis (Solanum), mycolate biosynthesis, palmitate biosynthesis I (type I fatty acid synthase), palmitate biosynthesis II (type II fatty acid synthase), sporopollenin precursors biosynthesis more

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Natural Substrate (8 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.42

dodecanoyl-CoA + NADPH + H+ = dodecanal + CoA + NADP+

724299

-

1.3.8.8

lauroyl-CoA + acceptor = 2-dodecenoyl-CoA + reduced acceptor

656313

-

2.3.1.301

lauroyl-CoA + malonyl-[acyl-carrier protein] = 3-oxomyristoyl-[acyl-carrier protein] + CoA + CO2

665474

-

2.3.1.51

lauroyl-CoA + 1-lauroyl-sn-glycerol 3-phosphate = CoA + 1,2-dilauroyl-sn-glycerol 3-phosphate

737242

-

2.3.3.2

lauroyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate + CoA

488155

-

2.3.3.4

dodecanoyl-CoA + H2O + 2-oxoglutarate = (3S,4S)-3-hydroxytetradecane-1,3,4-tricarboxylate + CoA

488164

-

3.1.2.20

dodecanoyl-CoA + H2O = dodecanoate + CoA

665707

-

7.6.2.4

ATP + H2O + lauroyl-CoA[side 1] = ADP + phosphate + lauroyl-CoA[side 2]

750514

-

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

7.6.2.4

ATP + H2O + lauroyl-CoA[side 1] = ADP + phosphate + lauroyl-CoA[side 2]

-

-

Substrate in Enzyme-catalyzed Reactions (123 results)

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Show Substrate (123 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.11.18

dodecanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxydodecanoyl-CoA + succinate + CO2

658428

-

1.2.1.42

dodecanoyl-CoA + NAD(P)H = dodecanal + NAD(P)+

288215

-

1.2.1.42

dodecanoyl-CoA + NADPH + H+ = dodecanal + CoA + NADP+

724299

-

1.2.1.50

lauroyl-CoA + NADP+ = dodecanal + CoA + NADPH

288215

-

1.2.1.50

lauroyl-CoA + NADPH + H+ = dodecanal + CoA + NADP+

724299

-

1.2.1.84

lauroyl-CoA + 2 NADPH + 2 H+ = dodecanal + CoA + 2 NADP+

763327

-

1.2.1.84

lauroyl-CoA + 2 NADPH + 2 H+ = dodecanol + 2 NADP+ + coenzyme A

743538

-

1.2.1.84

lauroyl-CoA + 2 NADPH + 2 H+ = dodecanol + CoA + 2 NADP+

762636

-

1.2.1.42

2 entries

1.2.1.50

2 entries

1.2.1.84

3 entries

1.2.1.B25

dodecanoyl-CoA + NADPH = dodecanal + CoA + NADP+

742484

-

1.3.3.6

dodecanoyl-CoA + O2 = (2E)-dodec-2-enoyl-CoA + H2O2

391052, 391065, 654352, 689649

-

1.3.3.6

dodecanoyl-CoA + O2 = trans-dodec-2-enoyl-CoA + H2O2

391069

-

1.3.3.6

lauroyl-CoA + O2 = trans-2-dodecenoyl-CoA + H2O2

391043, 391057, 391050, 391052, 391044, 674364

-

1.3.8.7

dodecanoyl-CoA + acceptor = 2-dodecenoyl-CoA + reduced acceptor

391343, 391282, 391201, 391272

-

1.3.8.7

dodecanoyl-CoA + electron transfer flavoprotein = dodecenoyl-CoA + reduced electron transfer flavoprotein

743247

-

1.3.8.7

dodecanoyl-CoA + electron-transfer flavoprotein = + trans-dodec-2-enoyl-CoA reduced electron-transfer flavoprotein

391371

-

1.3.8.7

dodecanoyl-CoA + tetrazolium salt = trans-dodec-2-enoyl-CoA + reduced tetrazolium salt

391275

-

1.3.8.7

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

674476

-

1.3.8.7

lauroyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol = 2-trans-dodecenoyl-CoA + reduced acceptor

391203

-

1.3.8.8

dodecanoyl-CoA + electron-transfer flavoprotein = 2-dodecenoyl-CoA + reduced electron-transfer flavoprotein

391325, 391371, 391272, 391282, 394650

-

1.3.8.8

dodecanoyl-CoA + Meldola's Blue = 2-dodecenoyl-CoA + reduced meldola blue

391275

-

1.3.8.8

dodecanoyl-CoA + phenazine methosulfate = (2E)-2-dodecenoyl-CoA + reduced phenazine methosulfate

394662, 391047, 391203, 391272, 391282, 394642, 394667, 391268

-

1.3.8.8

lauroyl-CoA + acceptor = 2-dodecenoyl-CoA + reduced acceptor

656313

-

2.3.1.137

dodecanoyl-CoA + L-carnitine = CoA + L-dodecanoylcarnitine

659372

-

2.3.1.137

dodecanoyl-CoA + L-carnitine = L-dodecanoyl-L-carnitine + CoA

486290, 486291, 486292, 486305

-

2.3.1.15

lauroyl-CoA + glycerol-3-phosphate = CoA + 1-lauroyl-sn-glycerol 3-phosphate

687685

-

2.3.1.15

lauroyl-CoA + sn-glycerol 3-phosphate = CoA + 1-lauroyl-sn-glycerol 3-phosphate

662902, 676839

-

2.3.1.15

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

486357, 486392, 486374, 486356

-

1.3.3.6

3 entries

1.3.8.7

6 entries

1.3.8.8

4 entries

2.3.1.137

2 entries

2.3.1.15

3 entries

2.3.1.16

dodecanoyl-CoA + H2O = dodecanoate + CoA

664215

-

2.3.1.179

malonyl-CoA + lauroyl-CoA = ?

718888

-

2.3.1.179

malonyl-phosphopantetheine + lauroyl-CoA = ?

718888

-

2.3.1.179

malonyl-phosphopantetheine-14-mer + lauroyl-CoA = ?

718888

-

2.3.1.179

malonyl-phosphopantetheine-16-mer + lauroyl-CoA = ?

718888

-

2.3.1.179

malonyl-phosphopantetheine-8-mer + lauroyl-CoA = ?

718888

-

2.3.1.179

5 entries

2.3.1.180

lauroyl-CoA + malonyl-[acyl-carrier protein] = 3-oxo-myristoyl-[acyl-carrier protein] + CoA + CO2

665474, 660466, 659724

-

2.3.1.199

lauroyl-CoA + malonyl-CoA = ?

487614

-

2.3.1.20

lauroyl-CoA + 1,2-diacylglycerol = CoA + 1,2-diacyl-3-lauroylglycerol

486488, 486509

-

2.3.1.20

lauroyl-CoA + 1,2-dioleoyl-sn-glycerol = CoA + 1,2-dioleoyl-3-lauroyl-sn-glycerol

758140

-

2.3.1.20

lauryl-CoA + 1,2-dipalmitoyl-sn-glycerol = CoA + 1,2-dipalmitoyl-3-lauryl-glycerol

755845

-

2.3.1.21

dodecanoyl-CoA + L-carnitine = CoA + L-dodecanoylcarnitine

718967

-

2.3.1.21

lauroyl-CoA + L-carnitine = CoA + L-lauroylcarnitine

486565, 486526, 486534, 486528, 718967

-

2.3.1.20

3 entries

2.3.1.21

2 entries

2.3.1.22

lauroyl-CoA + sn-2-monooleoylglycerol = CoA + 1-lauroyl-2-oleoylglycerol

486605

-

2.3.1.23

1-palmitoyl-lysophosphatidylcholine + lauroyl-CoA = CoA + 1-palmitoyl-2-lauroylphosphatidylcholine

687802

-

2.3.1.233

lauroyl-CoA = 1-(2,4,6-trihydroxyphenyl)-dodecan-1-one + 4-hydroxy-6-(2-oxotridecyl)-2H-pyran-2-one + CoA + CO2 + H2O

730606

-

2.3.1.24

sphingosine + lauroyl-CoA = N-lauroylsphingosine + CoA

754575, 752700

-

2.3.1.250

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

757228

-

2.3.1.253

lauroyl-CoA = 6-decyl-4-hydroxy-2H-pyran-2-one + 4-hydroxy-6-(2-oxotridecyl)-2H-pyran-2-one + CO2 + CoA

740681

-

2.3.1.26

lauroyl-CoA + cholesterol = CoA + cholesteryl laurate

486675

-

2.3.1.265

2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + lauroyl-CoA = 2-O-(alpha-D-mannosyl)-6-O-(6-O-lauroyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA

779275

-

2.3.1.265

lauroyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-lauroyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol

779275

-

2.3.1.265

2 entries

2.3.1.282

octan-1-ol + lauroyl-CoA = 1-octyl laurate + CoA

752024

-

2.3.1.294

lauroyl-CoA + malonyl-CoA = ?

718888

-

2.3.1.294

lauroyl-CoA + malonyl-phosphopantetheine 14-mer = ?

718888

-

2.3.1.294

lauroyl-CoA + malonyl-phosphopantetheine 16-mer = ?

718888

-

2.3.1.294

lauroyl-CoA + malonyl-phosphopantetheine 8-mer = ?

718888

-

2.3.1.294

lauroyl-CoA + malonyl-phosphopantetheine = ?

718888

-

2.3.1.301

dodecanoyl-CoA + malonyl-[ACP] = 3-oxotetradecanoyl-[ACP] + CoA + CO2

659493

-

2.3.1.301

dodecanoyl-CoA + malonyl-[acyl-carrier protein] = 3-oxotetradecanoyl-[acyl-carrier protein] + CoA + CO2

685507

-

2.3.1.301

lauroyl-CoA + malonyl-[acyl-carrier protein] = 3-oxomyristoyl-[acyl-carrier protein] + CoA + CO2

665474, 685507

-

2.3.1.294

5 entries

2.3.1.301

3 entries

2.3.1.314

dodecanoyl-CoA + 1,3-dihexanoylglycerol = ?

775088

-

2.3.1.332

lauroyl-CoA + 1-hexadecanol = CoA + hexadecyl laurate

659305

-

2.3.1.332

lauroyl-CoA + decanol = CoA + decyl dodecanoate

718651

-

2.3.1.332

lauroyl-CoA + hexadecanol = CoA + hexadecyl laurate

659380

-

2.3.1.332

lauryl-CoA + 1,2-dipalmitoyl-sn-glycerol = CoA + 1,2-dipalmitoyl-3-lauryl-glycerol

755845

-

2.3.1.332

lauryl-CoA + palmityl alcohol = CoA + palmityl laurate

755845

-

2.3.1.41

malonyl-ACP + lauroyl-CoA = ?

718888

1U6S, 3D-view

2.3.1.41

malonyl-[acyl-carrier protein] + lauroyl-CoA = ? + CO2 + [acyl-carrier protein]

659724

1U6S, 3D-view

2.3.1.42

dodecanoyl-CoA + dihydroxyacetone phosphate = CoA + dodecanoyldihydroxyacetone phosphate

486950, 486960, 486356

-

2.3.1.42

dihydroxyacetone phosphate + lauroyl-CoA = 1-lauroyl-glycerone phosphate + CoA

674766

-

2.3.1.42

lauroyl-CoA + glycerone phosphate = CoA + lauroylglycerone phosphate

758156

-

2.3.1.332

5 entries

2.3.1.41

2 entries

2.3.1.42

3 entries

2.3.1.50

lauroyl-CoA + L-serine = CoA + 2-amino-1-hydroxytetradecan-3-one + CO2

487172, 756627

-

2.3.1.51

lauroyl-CoA + 1-acyl-lysophosphatidic acid = CoA + 1-acyl-2-lauroyl-lysophosphatidic acid

748130

-

2.3.1.51

lauroyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1-acyl-2-lauroyl-sn-glycerol 3-phosphate

487203, 486635, 487204, 487206, 486374, 486486, 486634

-

2.3.1.51

lauroyl-CoA + 1-lauroyl-sn-glycerol 3-phosphate = CoA + 1,2-dilauroyl-sn-glycerol 3-phosphate

737242

-

2.3.1.51

lauroyl-CoA + 1-oleoyl-2-lysophosphatidic acid = CoA + 2-lauroyl-1-oleoyl-sn-glycerol 3-phosphate

748130

-

2.3.1.51

4 entries

2.3.1.52

lauroyl-CoA + 2-acyl-sn-glycerol 3-phosphate = CoA + 1-lauroyl-2-acyl-sn-glycerol 3-phosphate

486643

-

2.3.1.75

lauroyl-CoA + decanol = decyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + docosanol = docosyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + docosenol = docosenyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + dodecanol = dodecyl laurate + CoA

755872, 776627

-

2.3.1.75

lauroyl-CoA + eicosanol = eicosanyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + eicosenol = eicosenyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + hexadecan-1-ol = ?

756245

-

2.3.1.75

lauroyl-CoA + hexadecanol = CoA + hexadecyl laurate

756245

-

2.3.1.75

lauroyl-CoA + hexadecanol = hexadecanyl laurate + CoA

755845

-

2.3.1.75

lauroyl-CoA + hexadecanol = hexadecyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + hexadecenol = hexadecenyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + linolenyl alcohol = linolenyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + linoleyl alcohol = linoleyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + octadecanol = octadecyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + octadecenol = octadecenyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + phytol = phytyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + ricinoleyl alcohol = ricinoleyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + tetracosanol = tetracosyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + tetracosenol = tetracosenyl laurate + CoA

755872

-

2.3.1.75

lauroyl-CoA + tetradecanol = tetradecyl laurate + CoA

720358, 755872

-

2.3.1.75

lauryl-CoA + 1,2-dipalmitoyl-sn-glycerol = ?

755845

-

2.3.1.75

lauryl-CoA + tetradecanol = tetradecanyl laurate + CoA

735353

-

2.3.1.75

22 entries

2.3.1.76

lauroyl-CoA + retinol = CoA + retinyllaurate

487488

-

2.3.1.86

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

487614

-

2.3.1.97

dodecanoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg = N-dodecanoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA

487750

-

2.3.1.97

lauroyl-CoA + brain acid soluble protein 1 = N-lauroyl-brain acid soluble protein 1 + CoA

735953

-

2.3.1.97

lauroyl-CoA + c-Src = N-lauroyl-c-Src + CoA

735953

-

2.3.1.97

lauroyl-CoA + glycylpeptide = N-lauroylglycylpeptide + CoA

487756, 487773

-

2.3.3.2

lauroyl-CoA + H2O + 2-oxoglutarate = ?

488156

-

2.3.3.2

lauroyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate + CoA

488155, 488156

-

2.3.3.2

lauroyl-CoA + H2O + pyruvate = ?

488156

-

2.3.3.20

2 lauroyl-CoA + H2O = (2R)-2-decanoyltetradecanoate + 2 CoA

745355

-

2.3.3.20

lauroyl-CoA + H2O = ?

745284

-

2.3.1.97

4 entries

2.3.3.2

3 entries

2.3.3.20

2 entries

2.3.3.4

dodecanoyl-CoA + H2O + 2-oxoglutarate = (3S,4S)-3-hydroxytetradecane-1,3,4-tricarboxylate + CoA

488164

-

2.7.8.7

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

760467

-

2.7.8.7

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

760467

-

2.7.8.7

2 entries

3.1.2.1

lauroyl-CoA = lauroate + CoA

94478

-

3.1.2.14

lauroyl-CoA + H2O = lauric acid + CoA

649400

-

3.1.2.2

dodecanoyl-CoA + H2O = CoA + dodecanoate

646165, 646175, 646200, 646119, 646123, 94478, 80783, 646128, 646129, 646140, 646162, 646139, 646143, 646179, 646145, 646176, 646136, 646130, 646181, 646168, 646156, 646195, 679171, 679724, 646166

-

3.1.2.2

lauroyl-CoA + H2O = CoA + laurate

646200, 646195, 679171, 682542, 678465, 678033

-

3.1.2.20

dodecanoyl-CoA + H2O = CoA + dodecanoate

646165, 646175, 646200, 646119, 646123, 94478, 80783, 646128, 646129, 646140, 646162, 646139, 646143, 646179, 646145, 646176, 646136, 646130, 646181, 646168, 646156, 646195, 679724, 646166

-

3.1.2.20

dodecanoyl-CoA + H2O = dodecanoate + CoA

665707

-

3.1.2.20

lauroyl-CoA + H2O = CoA + laurate

690932, 707486, 707477, 707430

-

3.1.2.20

lauroyl-CoA + H2O = CoA + lauric acid

679739

-

3.1.2.20

lauroyl-CoA + H2O = CoA + lauroate

707475, 732296

-

3.1.2.2

2 entries

3.1.2.20

5 entries

3.1.2.25

dodecanoyl-CoA + H2O = dodecanoate + CoA

751066

-

3.6.1.77

lauroyl-CoA + H2O = ?

772774

-

7.6.2.4

ATP + H2O + lauroyl-CoA[side 1] = ADP + phosphate + lauroyl-CoA[side 2]

750514, 768000

-

Product in Enzyme-catalyzed Reactions (25 results)

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Show Product (25 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.12.7

lauric acid + ATP + CoA = lauroyl-CoA + AMP + diphosphate

-

-

1.3.1.10

dodec-2-enoyl-CoA + NADPH + H+ = dodecanoyl-CoA + NADP+

-

-

1.3.1.10

dodecenoyl-CoA + NADPH + H+ = dodecanoyl-CoA + NADP+

-

-

1.3.1.10

2 entries

1.3.1.118

trans-2-dodecenoyl-CoA + NADH + H+ = dodecanoyl-CoA + NAD+

-

-

1.3.1.37

cis-2-dodecenoyl-CoA + NADPH + H+ = dodecanoyl-CoA + NADP+

390746

-

1.3.1.44

dodec-2-enoyl-CoA + NADH + H+ = dodecanoyl-CoA + NAD+

-

-

1.3.1.44

trans-2-dodecenoyl-CoA + NADH + H+ = dodecanoyl-CoA + NAD+

-

-

1.3.1.44

trans-2-dodecenoyl-CoA + NADH = dodecanoyl-CoA + NAD+

390807, -

-

1.3.1.44

3 entries

1.3.1.8

2-trans-dodecenoyl-CoA + NAD(P)H = dodecanoyl-CoA + NAD(P)+

-

-

1.3.1.9

(2E)-2-dodecenoyl-CoA + NADH + H+ = dodecanoyl-CoA + NAD+

-

-

1.3.1.9

2-trans-dodecenoyl-CoA + NADH + H+ = dodecanoyl-CoA + NAD+

-

-

1.3.1.9

2-trans-dodecenoyl-CoA + NADH = dodecanoyl-CoA + NAD+

-

-

1.3.1.9

dodecenoyl-CoA + NADH + H+ = dodecanoyl-CoA + NAD+

-

-

1.3.1.9

trans-2-dodecenoyl-CoA + NADH + H+ = dodecanoyl-CoA + NAD+

-

-

1.3.1.9

trans-2-dodecenoyl-CoA + NADH = dodecanoyl-CoA + NAD+

-

-

1.3.1.9

6 entries

2.3.1.137

dodecanoyl-L-carnitine + CoA = dodecanoyl-CoA + L-carnitine

-

-

6.2.1.11

ATP + n-laurate + CoA = AMP + diphosphate + n-lauroyl-CoA

-

-

6.2.1.2

ATP + dodecanoate + CoA = AMP + diphosphate + dodecanoyl-CoA

650334, 649783, -

-

6.2.1.2

ATP + laurate + CoA = AMP + diphosphate + lauroyl-CoA

650950

-

6.2.1.3

ATP + dodecanoate + CoA = AMP + diphosphate + dodecanoyl-CoA

649717, 653493

-

6.2.1.3

ATP + laurate + CoA = AMP + diphosphate + lauroyl-CoA

-

-

6.2.1.3

lauric acid + ATP + CoA = lauroyl-CoA + AMP + diphosphate

-

-

6.2.1.3

ATP + laurate + CoA = AMP + diphosphate + lauryl-CoA

-

-

6.2.1.2

2 entries

6.2.1.3

4 entries

6.2.1.B3

dodecanoic acid + CoA + ATP = dodecanoyl-CoA + AMP + diphosphate

-

-

7.6.2.4

ATP + H2O + lauroyl-CoA[side 1] = ADP + phosphate + lauroyl-CoA[side 2]

-

-

Inhibitor in Enzyme-catalyzed Reactions (13 results)

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Show Inhibitors (13 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.19.1

competitive inhibition of enzyme activity greater than 90% at 0.002 mM

437658

-

1.14.19.1

competitive inhibitor

437646

-

1.14.19.1

2 entries

1.3.1.38

-

390748

-

1.3.1.44

-

724351

-

1.3.1.9

about 50% inhibition at 0.2 mM

739906

-

2.3.1.137

substrate inhibition

486291

-

2.3.3.16

-

488029

-

2.3.3.2

strong substrate inhibition, does not follow Michaelis-Menten kinetics

488155, 488156

-

2.3.3.8

-

488217

-

2.3.3.8

10 mM, 52% inhibition

488187

-

2.3.3.8

2 entries

3.1.2.2

substrate inhibition

646179

-

3.1.2.20

substrate inhibition

646179

-

4.1.2.9

-

5097

-

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

2.3.1.41

1U6S, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (33 results)

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Show Turnover Number (33 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.8.7

3.33

-

T255E/E376G double mutant enzyme

391369

1.3.8.7

7

-

-

391371

1.3.8.7

9.17

-

-

391369

1.3.8.7

9.5

-

K304E mutant enzyme, ferricenium assay

391370

1.3.8.7

4 entries

2.3.1.179

0.047

-

wild type protein, acceptor malonyl-CoA, 0.5 mM malonyl-CoA, pH 6.5, 25°C

718888

2.3.1.41

0.073

-

wild type protein, acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 6.5, 25°C

718888

2.3.1.50

0.11

-

wild type enzyme, at pH 7.5 and 25°C

756627

2.3.1.50

0.35

-

mutant enzyme R378K, at pH 7.5 and 25°C

756627

2.3.1.75

0.0202

-

isoform WSD4, at pH 7.4 and 37°C

756245

2.3.1.75

0.0202

-

pH 7.4, 37°C, recombinant enzyme

756245

2.3.1.75

0.243

-

isoform WSD5, at pH 7.4 and 37°C

756245

2.3.1.75

0.243

-

pH 7.4, 37°C, recombinant enzyme

756245

3.1.2.2

0.01

-

pH 7.5

679171

3.1.2.2

0.015

-

pH 7.5

679171

3.1.2.2

0.052

2.1

37°C, pH 7, wild-type enzyme

678033

3.1.2.2

0.052

2.1

native enzyme

678465

3.1.2.2

0.057

-

37°C, pH 7, mutant enzyme, S10A

678033

3.1.2.2

0.45

-

37°C, pH 7, mutant enzyme D154A

678033

3.1.2.2

0.57

-

mutant enzyme L109P

678465

3.1.2.2

0.77

-

37°C, pH 7, mutant enzyme G44A

678033

3.1.2.2

0.84

-

mutant enzyme P110A/L109P

678465

3.1.2.2

1.14

-

37°C, pH 7, mutant enzyme N73A

678033

3.1.2.2

3.8

-

mutant enzyme P110A

678465

3.1.2.2

10.13

-

37°C, pH 7, wild-type enzyme

678033

3.1.2.2

10.13

-

native enzyme

678465

3.1.2.20

0.019

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

0.038

-

-

707430

3.1.2.20

1.6

-

-

707477

3.1.2.20

2.57

-

N29A mutant protein

707475

3.1.2.20

5.3

-

pH 7.5, 37°C

732296

3.1.2.20

9.2

-

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

690932

3.1.2.20

9.2

-

wild-type protein

707475

3.1.2.20

9.6

-

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

690932

2.3.1.50

2 entries

2.3.1.75

4 entries

3.1.2.2

13 entries

3.1.2.20

8 entries

K_M Value (77 results)

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Show KM Value (77 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.3.6

0.002

-

MCOX

391069

1.3.3.6

0.013

-

-

391043

1.3.3.6

0.0157

-

isozyme AtACX3

391065

1.3.3.6

0.0189

-

isozyme AtACX1

391065

1.3.3.6

0.024

-

-

391050

1.3.3.6

0.025

-

pH 7.0-9.5

391052

1.3.3.6

0.027

-

liver enzyme

391043

1.3.3.6

0.071

-

pH 6.2

391052

1.3.3.6

0.1

-

30°C

654352

1.3.8.7

0.0025

-

-

391369

1.3.8.7

0.0033

-

K304E mutant enzyme, ferricenium assay

391370

1.3.8.7

0.0043

-

-

391275

1.3.8.7

0.0057

-

-

391272

1.3.8.7

0.0066

-

T255E/E376G double mutant enzyme

391369

1.3.8.7

0.05

-

T255E/E376T double mutant enzyme

391369

1.3.8.8

0.0015

-

-

391371

1.3.8.8

0.00571

-

-

391047

1.3.8.8

0.007

-

-

391371

1.3.8.8

0.009

-

-

391272

1.3.8.8

0.068

-

pH 8.5, recombinant enzyme

656313

1.3.8.8

0.2

-

-

391275

1.3.3.6

9 entries

1.3.8.7

6 entries

1.3.8.8

6 entries

2.3.1.179

0.0537

-

wild type protein, acceptor malonyl-CoA, 0.5 mM malonyl-CoA, pH 6.5, 25°C

718888

2.3.1.199

0.05

-

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

0.004

-

-

486528

2.3.1.21

0.011

-

-

486565

2.3.1.21

0.013

-

-

486534

2.3.1.21

3 entries

2.3.1.24

0.358

-

pH 7.5, 37°C

754575

2.3.1.41

0.0586

-

wild type protein, acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 6.5, 25°C

718888

2.3.1.50

0.25

-

wild type enzyme, at pH 7.5 and 25°C

756627

2.3.1.50

0.56

-

mutant enzyme R378K, at pH 7.5 and 25°C

756627

2.3.1.75

0.00014

-

isoform WSD4, at pH 7.4 and 37°C

756245

2.3.1.75

0.00014

-

pH 7.4, 37°C, recombinant enzyme

756245

2.3.1.75

0.0259

-

pH 7.4, 37°C, recombinant enzyme

756245

2.3.1.75

0.02593

-

isoform WSD5, at pH 7.4 and 37°C

756245

2.3.1.50

2 entries

2.3.1.75

4 entries

2.3.1.86

0.05

-

-

487614

2.3.3.2

0.0001

-

-

488155

2.3.3.4

0.001

-

-

488164

3.1.2.2

0.0018

-

pH 7.8, 22°C

646176

3.1.2.2

0.0036

-

-

679724

3.1.2.2

0.0038

-

pH 7.5, 37°C

646165

3.1.2.2

0.0076

-

pH 7.4, 30°C

646166

3.1.2.2

0.0077

-

-

646143

3.1.2.2

0.014

-

pH 7.0, 30°C

646179

3.1.2.2

0.0178

-

-

646195

3.1.2.2

0.018

-

pH 8.0

646195

3.1.2.2

0.01913

-

pH 7.5

679171

3.1.2.2

0.03852

-

pH 7.5

679171

3.1.2.2

0.04468

-

-

646145

3.1.2.2

0.059

-

37°C, pH 7, mutant enzyme D154A

678033

3.1.2.2

0.073

-

mutant enzyme P110A/L109P

678465

3.1.2.2

0.075

-

37°C, pH 7, mutant enzyme G44A

678033

3.1.2.2

0.085

-

37°C, pH 7, mutant enzyme N73A

678033

3.1.2.2

0.089

-

-

679724

3.1.2.2

0.113

-

mutant enzyme P110A

678465

3.1.2.2

0.127

-

37°C, pH 7, mutant enzyme, S10A

678033

3.1.2.2

0.146

-

37°C, pH 7, wild-type enzyme

678033

3.1.2.2

0.146

-

native enzyme

678465

3.1.2.2

0.185

-

mutant enzyme L109P

678465

3.1.2.2

0.325

-

-

646168

3.1.2.20

0.0018

-

pH 7.8, 22°C

646176

3.1.2.20

0.00348

-

37°C, pH 7.6

679739

3.1.2.20

0.0038

-

pH 7.5, 37°C

646165

3.1.2.20

0.0042

-

N29A mutant protein

707475

3.1.2.20

0.006

-

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

690932

3.1.2.20

0.0066

-

wild-type protein

707475

3.1.2.20

0.0076

-

pH 7.4, 30°C

646166

3.1.2.20

0.0077

-

-

646143

3.1.2.20

0.0079

-

pH 7.5, 37°C

732296

3.1.2.20

0.0099

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

0.0104

-

pH 8.0

665707

3.1.2.20

0.013

-

-

707477

3.1.2.20

0.014

-

pH 7.0, 30°C

646179

3.1.2.20

0.018

-

pH 8.0

646195

3.1.2.20

0.02

-

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

690932

3.1.2.20

0.0275

-

-

707430

3.1.2.20

0.04468

-

-

646145

3.1.2.20

0.325

-

-

646168

3.1.2.2

22 entries

3.1.2.20

18 entries

K_i Value (10 results)

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Show KI Value (10 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.38

0.045

-

-

390748

1.3.1.44

0.00003

-

pH and temperature not specified in the publication, 0.0001 mM inhibitor, mutant I287A

724351

1.3.1.44

0.00006

-

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

724351

1.3.1.44

0.00006

-

pH and temperature not specified in the publication, 0.00025 mM inhibitor, mutant I287A

724351

1.3.1.44

0.0004

-

pH and temperature not specified in the publication, 0.0015 mM inhibitor, wild-type

724351

1.3.1.44

0.0005

-

pH and temperature not specified in the publication, 0.001 mM inhibitor, wild-type

724351

1.3.1.44

0.0005

-

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

724351

1.3.1.44

0.001

-

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

724351

1.3.1.44

0.003

-

pH and temperature not specified in the publication, 0.010 mM inhibitor, mutant I287A

724351

1.3.1.44

0.01

-

pH and temperature not specified in the publication, 0.005 mM inhibitor, mutant I287A

724351

1.3.1.44

9 entries

References & Links

Literature References (184)

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Show Reference (184 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

5097

-

Phosphoketolase in Rhodotorula graminis and other yeasts

1977

Whitworth, D.A.; Ratledge, C.

J. Gen. Microbiol.

102

397-401

80783

39553

Differences between microsomal and mitochondrial-matrix palmitoyl-coenzyme A hydrolase, and palmitoyl-L-carnitine hydrolase from rat liver

1979

Berge, R.K.; Dossland, B.

Biochem. J.

181

119-125

94478

6151837

Carnitine acyltransferase and acyl-coenzyme A hydrolase activities in human liver. Quantitative analysis of their subcellular localization

1984

Bronfman, M.; Leighton, F.

Biochem. J.

224

721-730

288215

11872467

Wax ester production from n-alkanes by Acinetobacter sp. strain M-1: ultrastructure of cellular inclusions and role of acyl coenzyme A reductase

2002

Ishige, T.; Tani, a.; Takabe, K.; Kawasaki, K.; Sakai, Y.; Kato, N.

Appl. Environ. Microbiol.

68

1192-1195

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

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

390807

7251572

Purification and characterization of 2-enoyl-CoA reductase of Mycobacterium smegmatis

1981

Shimakata, T.; Kusaka, T.

J. Biochem.

89

1075-1080

391043

7400120

Purification and properties of acyl-CoA oxidase from rat liver

1980

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

J. Biochem.

87

1735-1746

391044

3342250

Acyl-CoA oxidase activity and peroxisomal fatty acid oxidation in rat tissues

1988

Reubsaet, F.A.G.; Veerkamp, J.H.; Bukkens, S.G.F.; Trijbels, J.M.F.; Monnens, L.A.H.

Biochim. Biophys. Acta

958

434-442

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

391050

518611

Acyl-CoA oxidase from Candida tropicalis

1979

Shimizu, S.; Yasui, K.; Tani, Y.; Yamada, H.

Biochem. Biophys. Res. Commun.

91

108-113

391052

6639056

Chemical and catalytic properties of the peroxisomal acyl-coenzyme A oxidase from Candida tropicalis

1983

Coudron, P.E.; Frerman, F.E.; Schowalter, D.B.

Arch. Biochem. Biophys.

226

324-336

391057

-

Substrate specificity of peroxisomal acyl-CoA oxidase

1985

Gerhardt, B.

Phytochemistry

24

251-252

391065

10859203

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

2000

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

Plant Physiol.

123

733-741

391069

8973574

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

1996

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

Biochem. J.

320

607-614

391201

3597357

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

1987

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

J. Biol. Chem.

262

7982-7989

391203

6401712

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

1983

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

J. Biol. Chem.

258

1066-1076

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

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

391325

-

Fatty acid oxidation in cultured skin fibroblasts from patients with inherited disorders of fatty acid metabolism: studies on the specificity of acyl-CoA dehydrogenases

1987

Chalmers, R.A.; English, N.

Biochem. Soc. Trans.

15

489-491

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

391369

8823175

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

1996

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

Biochemistry

35

12402-12411

391370

9208949

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

1997

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

Eur. J. Biochem.

246

548-556

391371

9182995

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

1997

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

Eur. J. Biochem.

245

600-607

394642

3651489

Participation of peroxisomes in the metabolism of xenobiotic acyl compounds: comparison between peroxisomal and mitochondrial beta-oxidation of omega-phenyl fatty acids in rat liver

1987

Yamada, J.; Ogawa, S.; Horie, S.; Watanabe, T.; Suga, T.

Biochim. Biophys. Acta

921

292-301

394650

13319294

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

1956

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

J. Biol. Chem.

219

727-733

394662

7769092

Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients

1995

Aoyama, T.; Souri, M.; Ushikubo, S.; Kamijo, T.; Yamaguchi, S.; Kelley, R.I.; Rhead, W.J.; Uetake, K.; Tanaka, K.; Hashimoto, T.

J. Clin. Invest.

95

2465-2473

394667

10198089

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

1999

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

Plant Physiol.

119

1305-1314

437646

6116157

Terminal enzyme of stearoyl-CoA desaturation from chicken liver

1981

Joshi, V.C.; Prasad, M.R.; Sreekrishna, K.

Methods Enzymol.

71

252-258

437658

36392

Purification and properties of hen liver microsomal terminal enzyme involved in stearoyl coenzyme A desaturation and its quantitation in neonatal chicks

1979

Prasad, M.R.; Joshi, V.C.

J. Biol. Chem.

254

6362-6369

486290

4629977

Different carnitine acyltransferases in calf liver

1972

Solberg, H.E.

Biochim. Biophys. Acta

280

422-433

486291

4417128

Acyl group specificity of mitochondrial pools of carnitine acyltransferases

1974

Solberg, H.E.

Biochim. Biophys. Acta

360

101-112

486292

-

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

1976

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

Arch. Biochem. Biophys.

176

479-488

486305

10486279

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

1999

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

Biochem. Biophys. Res. Commun.

263

213-218

486356

25265

Glycerolipid biosynthesis in Saccharomyces cerevisiae: sn-glycerol-3-phosphate and dihydroxyacetone phosphate acyltransferase activities

1978

Schlossman, D.M.; Bell, R.M.

J. Bacteriol.

133

1368-1376

486357

7026564

Membrane phospholipid synthesis in Escherichia coli. Purification, reconstitution, and characterization of sn-glycerol-3-phosphate acyltransferase

1981

Green, P.R.; Merrill, A.H.; Bell, R.M.

J. Biol. Chem.

256

11151-11159

486374

770468

Factors affecting the acyl selectivities of acyltransferases in Escherichia coli

1976

Okuyama, H.; Yamada, K.; Ikezawa, H.; Wakil, S.J.

J. Biol. Chem.

251

2487-2492

486392

11284717

Purification and characterization of thiol-reagent-sensitive glycerol-3-phosphate acyltransferase from the membrane fraction of an oleaginous fungus

2001

Mishra, S.; Kamisaka, Y.

Biochem. J.

355

315-322

486486

6268930

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