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Information on EC 1.3.8.8 - long-chain acyl-CoA dehydrogenase and Organism(s) Sus scrofa

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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.
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Sus scrofa
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Word Map
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LCAD
-
-
-
-
long-chain acyl-coenzyme A dehydrogenase
-
-
-
-
palmitoyl-CoA dehydrogenase
-
-
-
-
palmitoyl-coenzyme A dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
59536-74-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
decanoyl-CoA + electron-transfer flavoprotein
2-decenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
dodecanoyl-CoA + electron-transfer flavoprotein
2-dodecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
eicosanoyl-CoA + electron-transfer flavoprotein
trans-2-eicosenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
hexanoyl-CoA + electron-transfer flavoprotein
2-hexenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
octanoyl-CoA + electron-transfer flavoprotein
2-octenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
palmitoyl-CoA + electron-transfer flavoprotein
2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
stearoyl-CoA + electron-transfer flavoprotein
2-octadecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
tetradecanoyl-CoA + electron-transfer flavoprotein
2-tetradecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-octynoyl-CoA
-
65% inhibition at 5 mol inhibitor/mol enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0022
decanoyl-CoA
-
-
0.0015
dodecanoyl-CoA
-
-
0.009
electron-transfer flavoprotein
-
saturating dodecanoyl-CoA
0.0063
hexanoyl-CoA
-
-
0.0033
octanoyl-CoA
-
-
0.0036
palmitoyl-CoA
-
-
0.0037
stearoyl-CoA
-
-
0.0023
tetradecanoyl-CoA
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
-
gel electrophoresis
44000
-
x * 44000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 44000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, zone electrophoresis
-
Q-Sepharose, hydroxyapatite I, hydroxyapatite II
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team