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EC Tree
IUBMB Comments Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids beta-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80 and 70%, respectively . The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24 . cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.
The taxonomic range for the selected organisms is: Sus scrofa The enzyme appears in selected viruses and cellular organisms
Synonyms
vlcad, very long-chain acyl-coa dehydrogenase, long-chain acyl-coa dehydrogenase, very long chain acyl-coa dehydrogenase, long-chain acyl-coa hydrolase, long chain acyl-coa dehydrogenase, long-chain acyl-coenzyme a dehydrogenase, palmitoyl-coa dehydrogenase, acyl-coa dehydrogenase 9, very-long-chain acyl-coenzyme a dehydrogenase,
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long-chain acyl-coenzyme A dehydrogenase
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palmitoyl-CoA dehydrogenase
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-
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palmitoyl-coenzyme A dehydrogenase
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long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids beta-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80 and 70%, respectively [2]. The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24 [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.
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decanoyl-CoA + electron-transfer flavoprotein
2-decenoyl-CoA + reduced electron-transfer flavoprotein
dodecanoyl-CoA + electron-transfer flavoprotein
2-dodecenoyl-CoA + reduced electron-transfer flavoprotein
eicosanoyl-CoA + electron-transfer flavoprotein
trans-2-eicosenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
hexanoyl-CoA + electron-transfer flavoprotein
2-hexenoyl-CoA + reduced electron-transfer flavoprotein
octanoyl-CoA + electron-transfer flavoprotein
2-octenoyl-CoA + reduced electron-transfer flavoprotein
palmitoyl-CoA + electron-transfer flavoprotein
2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
stearoyl-CoA + electron-transfer flavoprotein
2-octadecenoyl-CoA + reduced electron-transfer flavoprotein
tetradecanoyl-CoA + electron-transfer flavoprotein
2-tetradecenoyl-CoA + reduced electron-transfer flavoprotein
decanoyl-CoA + electron-transfer flavoprotein
2-decenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
decanoyl-CoA + electron-transfer flavoprotein
2-decenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
dodecanoyl-CoA + electron-transfer flavoprotein
2-dodecenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
dodecanoyl-CoA + electron-transfer flavoprotein
2-dodecenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
hexanoyl-CoA + electron-transfer flavoprotein
2-hexenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
hexanoyl-CoA + electron-transfer flavoprotein
2-hexenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
octanoyl-CoA + electron-transfer flavoprotein
2-octenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
octanoyl-CoA + electron-transfer flavoprotein
2-octenoyl-CoA + reduced electron-transfer flavoprotein
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-
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?
palmitoyl-CoA + electron-transfer flavoprotein
2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
palmitoyl-CoA + electron-transfer flavoprotein
2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
stearoyl-CoA + electron-transfer flavoprotein
2-octadecenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
stearoyl-CoA + electron-transfer flavoprotein
2-octadecenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
tetradecanoyl-CoA + electron-transfer flavoprotein
2-tetradecenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
tetradecanoyl-CoA + electron-transfer flavoprotein
2-tetradecenoyl-CoA + reduced electron-transfer flavoprotein
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-
-
?
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2-octynoyl-CoA
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65% inhibition at 5 mol inhibitor/mol enzyme
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0.0015
dodecanoyl-CoA
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0.009
electron-transfer flavoprotein
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saturating dodecanoyl-CoA
0.0023
tetradecanoyl-CoA
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-
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brenda
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brenda
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brenda
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brenda
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ACADL_PIG
430
0
47957
Swiss-Prot
Mitochondrion (Reliability: 1 )
A0A8D0MPF3_PIG
405
0
45064
TrEMBL
Mitochondrion (Reliability: 1 )
A0A8D0I2H9_PIG
421
1
47389
TrEMBL
Mitochondrion (Reliability: 1 )
A0A480PCQ6_PIG
430
0
47957
TrEMBL
Mitochondrion (Reliability: 1 )
A0A4X1UX32_PIG
429
0
47886
TrEMBL
Mitochondrion (Reliability: 1 )
A0A4X1UW18_PIG
430
0
47985
TrEMBL
Mitochondrion (Reliability: 1 )
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200000
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gel electrophoresis
44000
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x * 44000, SDS-PAGE
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ammonium sulfate precipitation, zone electrophoresis
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Q-Sepharose, hydroxyapatite I, hydroxyapatite II
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Eder, M.; Krautle, F.; Dong, Y.; Vock, P.; Kieweg, V.; Kim, J.J.; Strauss, A.W.; Ghisla, S.
Characterization of human and pig kidney long-chain-acyl-CoA dehydrogenases and their role in beta-oxidation
Eur. J. Biochem.
245
600-607
1997
Homo sapiens, Sus scrofa
brenda
Hauge, J.G.; Crane, F.L.; Beinert, H.
On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A
J. Biol. Chem.
219
727-733
1956
Sus scrofa
brenda