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Information on EC 1.3.8.8 - long-chain acyl-CoA dehydrogenase and Organism(s) Rattus norvegicus

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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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Rattus norvegicus
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The taxonomic range for the selected organisms is: Rattus norvegicus
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-CoA hydrolase
-
-
long-chain acyl-coenzyme A dehydrogenase
-
-
-
-
palmitoyl-CoA dehydrogenase
-
-
-
-
palmitoyl-coenzyme A dehydrogenase
-
-
-
-
type-II acyl-CoA thioesterase
-
-
additional information
-
see also EC 3.1.2.2, palmitoyl-CoA hydrolase
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
arachidonoyl-CoA + phenazine methosulfate
(2E,5Z,8Z,11Z,14Z)-2,5,8,11,14-eicosapentaenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
butyryl-CoA + electron-transfer flavoprotein
2-butenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
butyryl-CoA + phenazine methosulfate
2-butenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
decanoyl-CoA + electron-transfer flavoprotein
2-decenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
decanoyl-CoA + phenazine methosulfate
(2E)-2-decenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
docosanoyl-CoA + electron-transfer flavoprotein
2-docosenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
docosanoyl-CoA + phenazine methosulfate
2-docosenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
dodecanoyl-CoA + electron-transfer flavoprotein
2-dodecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
dodecanoyl-CoA + phenazine methosulfate
(2E)-2-dodecenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
eicosanoyl-CoA + electron-transfer flavoprotein
trans-2-eicosenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
eicosanoyl-CoA + phenazine methosulfate
trans-2-eicosenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
erucoyl-CoA + phenazine methosulfate
(2E,13Z)-2,13-docosadienoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
hexanoyl-CoA + electron-transfer flavoprotein
2-hexenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
hexanoyl-CoA + phenazine methosulfate
2-hexenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
linolenoyl-CoA + phenazine methosulfate
(2E,6Z,9Z,12Z)2,6,9,12-octadecatetraenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
linoleoyl-CoA + phenazine methosulfate
(2E,9Z,12Z)-2,9,12-octadecatrienoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
octanoyl-CoA + acceptor
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + electron-transfer flavoprotein
2-octenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
octanoyl-CoA + phenazine methosulfate
2-octenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
oleoyl-CoA + acceptor
2,9-octadecadienoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + phenazine methosulfate
(2E,9Z)-2,9-octadecadienoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
omega-phenyldecanoyl-CoA + phenazine methosulfate
10-phenyl-2-decenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
omega-phenyldodecanoyl-CoA + phenazine methosulfate
12-phenyl-2-dodecenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
palmitoleoyl-CoA + phenazine methosulfate
(2E,9Z)-2,9-hexadecadienoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
palmitoyl-CoA + electron-transfer flavoprotein
(2E)-2-hexadecenoyl-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
palmitoyl-CoA + phenazine methosulfate
2-hexadecenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
stearoyl-CoA + electron-transfer flavoprotein
2-octadecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
stearoyl-CoA + phenazine methosulfate
2-octadecenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
tetradecanoyl-CoA + electron-transfer flavoprotein
2-tetradecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
tetradecanoyl-CoA + phenazine methosulfate
2-tetradecenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hexadecenoyl-CoA
-
-
2-mercaptoacetate
-
inhibition by administration in vivo
AgNO3
-
strong inhibition of apo and holo forms at 0.1 mM
CuCl2
-
strong inhibition of apo and holo forms at 0.1 mM
HgCl2
iodoacetic acid
-
50% inhibition of apoenzyme at 2 mM, not inhibitory for the holo form
Methylmercury chloride
-
strong inhibition of apo and holo forms at 1 mM
Methylmercury iodide
N-ethylmaleimide
-
strong inhibition of the apoenzyme at 2 mM, not inhibitory for the holo form even at higher concentrations like 5 mM
p-chloromercuribenzoate
-
inhibition of enzyme-catalyzed C-2 proton-deuteron exchange reactions
p-hydroxymercuribenzoate
-
strong inhibition of the apoenzyme at 0.1 mM, not inhibitory for the holo form even at higher concentrations like 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Clofibrate
-
activation, treated animals receiving 0.5% w/w neutralized acid for 2 weeks
peroxisome proliferator
-
-
-
Triton X-100
-
restores activity during ischemia
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019 - 0.0243
decanoyl-CoA
0.00571 - 0.009
dodecanoyl-CoA
0.0008 - 0.0083
electron-transfer flavoprotein
0.0014 - 0.0025
FAD
0.123
octanoyl-CoA
-
-
0.0065
oleoyl-CoA
-
-
0.00064
omega-phenyldecanoyl-CoA
-
-
0.00164
omega-phenyldodecanoyl-CoA
-
-
0.0025 - 0.0111
palmitoyl-CoA
1 - 1.1
phenazine methosulfate
0.0054 - 0.0112
stearoyl-CoA
0.0074 - 0.0125
tetradecanoyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 5.4
palmitoyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.06
-
purified holoenzyme, arachidonoyl-CoA
0.3
-
purified holoenzyme, docosanoyl-CoA
0.38
-
purified holoenzyme, linolenoyl-CoA
0.7
-
purified holoenzyme, octanoyl-CoA
0.72
-
purified holoenzyme, linoleoyl-CoA
0.8
-
purified enzyme, decanoyl-CoA
0.82
-
purified enzyme, palmitoyl-CoA
0.9
-
purified holoenzyme, eicosanoyl-CoA
1.13
-
purified holoenzyme, oleoyl-CoA
1.48
-
purified apoenzyme, palmitoyl-CoA
1.51
-
purified holoenzyme, palmitoleoyl-CoA
1.52
-
purified apoenzyme, palmitoyl-CoA
1.6
-
purified holoenzyme, stearoyl-CoA
1.8
-
purified holoenzyme, dodecanoyl-CoA
1.96
-
purified holoenzyme, palmitoyl-CoA
2.1
-
purified holoenzyme, tetradecanoyl-CoA
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
activity declines 34% during 30 min of ischemia
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_RAT
430
0
47873
Swiss-Prot
Mitochondrion (Reliability: 1)
A0A8I6GMH0_RAT
406
0
45675
TrEMBL
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
168000
-
gel filtration
180000
-
gel filtration
44672
-
x * 44672, subunit, nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 44672, subunit, nucleotide sequence
tetramer
-
4 * 38000-45200, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.7
-
stable for at least 10 min at 37°C
391272
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20ºC, stable for at least 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
35-80% ammonium sulfate precipitation, DEAE-Sephadex A-50, hydroxyapatite
-
40-80% ammonium sulfate precipitation, DEAE-Sephadex A-50, hydroxyapatite, matrex gel blue A, agarose-hexane-CoA, bio-gel A-0.5m
-
DEAE-cellulose, blue dextran-sepharose, calcium phosphate gel-cellulose, blue dextran-sepharose, HPLC
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, strain XL1-blue
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
VLCAD represents a likely site for the modulation of substrate utilization during myocardial ischemia
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Suzuki, H.; Yamada, J.; Watanabe, T.; Suga, T.
Compartmentation of dicarboxylic acid beta-oxidation in rat liver: importance of peroxisomes in the metabolism of dicarboxylic acids
Biochim. Biophys. Acta
990
25-30
1989
Rattus norvegicus
Manually annotated by BRENDA team
Matsubara, Y.; Indo, Y.; Naito, E.; Ozasa, H.; Glassberg, R.; Vockley, J.; Ikeda, Y.; Kraus, J.; Tanaka, K.
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
J. Biol. Chem.
264
16321-16331
1989
Rattus norvegicus
Manually annotated by BRENDA team
Ikeda, Y.; Dabrowski, C.; Tanaka, K.
Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase
J. Biol. Chem.
258
1066-1076
1983
Rattus norvegicus
Manually annotated by BRENDA team
Ikeda, Y.; Keese, S.M.; Fenton, W.A.; Tanaka, K.
Biosynthesis of four rat liver mitochondrial acyl-CoA dehydrogenases: in vitro synthesis, import into mitochondria, and processing of their precursors in a cell-free system and in cultured cells
Arch. Biochem. Biophys.
252
662-674
1987
Rattus norvegicus
Manually annotated by BRENDA team
Ikeda, Y.; Okamura-Ikeda, K.; Tanaka, K.
Spectroscopic analysis of the interaction of rat liver short-chain, medium-chain, and long-chain acyl coenzyme A dehydrogenases with acyl coenzyme A substrates
Biochemistry
24
7192-7199
1985
Rattus norvegicus
Manually annotated by BRENDA team
Okamura-Ikeda, K.; Ikeda, Y.; Tanaka, K.
An essential cysteine residue located in the vicinity of the FAD-binding site in short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria
J. Biol. Chem.
260
1338-1345
1985
Rattus norvegicus
Manually annotated by BRENDA team
Ikeda, Y.; Hine, D.G.; Okamura-Ikeda, K.; Tanaka, K.
Mechanism of action of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases. Direct evidence for carbanion formation as an intermediate step using enzyme-catalyzed C-2 proton/deuteron exchange in the absence of C-3 exchange
J. Biol. Chem.
260
1326-1337
1985
Rattus norvegicus
Manually annotated by BRENDA team
Ikeda, Y.; Okamura-Ikeda, K.; Tanaka, K.
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
J. Biol. Chem.
260
1311-1325
1985
Rattus norvegicus
Manually annotated by BRENDA team
Furuta, S.; Miyazawa, S.; Hashimoto, T.
Purification and properties of rat liver acyl-CoA dehydrogenases and electron transfer flavoprotein
J. Biochem.
90
1739-1750
1981
Rattus norvegicus
Manually annotated by BRENDA team
Veitch, K.; Draye, J.P.; van Hoof, F.; Stanley, H.; Sherratt, H.S.
Effects of riboflavin deficiency and clofibrate treatment on the five acyl-CoA dehydrogenases in rat liver mitochondria
Biochem. J.
254
477-481
1988
Rattus norvegicus
Manually annotated by BRENDA team
Yamada, J.; Ogawa, S.; Horie, S.; Watanabe, T.; Suga, T.
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
Biochim. Biophys. Acta
921
292-301
1987
Rattus norvegicus
Manually annotated by BRENDA team
Bauche, F.; Sabourault, D.; Giudicelli, Y.; Nordmann, J.; Nordmann, R.
2-Mercaptoacetate administration depresses the beta-oxidation pathway through an inhibition of long-chain acyl-CoA dehydrogenase activity
Biochem. J.
196
803-809
1981
Rattus norvegicus
Manually annotated by BRENDA team
Furuta, S.; Miyazawa, S.; Hashimoto, T.
Induction of acyl-CoA dehydrogenases and electron transfer flavoprotein and their roles in fatty acid oxidation in rat liver mitochondria
J. Biochem.
90
1751-1756
1981
Rattus norvegicus
Manually annotated by BRENDA team
Veitch, K.; Draye, J.P.; Vamecq, J.; Causey, A.G.; Barlett, K.; Sherratt, H.S.A; Van Hoof,F.
Altered acyl-CoA metabolism in riboflavin deficiency
Biochim. Biophys. Acta
1006
335-343
1989
Rattus norvegicus
Manually annotated by BRENDA team
Aoyama, T.; Souri, M.; Ushikubo, S.; Kamijo, T.; Yamaguchi, S.; Kelley, R.I.; Rhead, W.J.; Uetake, K.; Tanaka, K.; Hashimoto, T.
Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients
J. Clin. Invest.
95
2465-2473
1995
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Yamada, J.
Long-chain acyl-CoA hydrolase in the brain
Amino Acids
28
273-278
2005
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Mason, K.E.; Stofan, D.A.; Szweda, L.I.
Inhibition of very long chain acyl-CoA dehydrogenase during cardiac ischemia
Arch. Biochem. Biophys.
437
138-143
2005
Rattus norvegicus
Manually annotated by BRENDA team