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Information on EC 1.3.8.8 - long-chain acyl-CoA dehydrogenase and Organism(s) Mus musculus and UniProt Accession P51174

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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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Mus musculus
UNIPROT: P51174
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
CTE-II
-
-
long chain acyl coenzyme A dehydrogenase
-
-
long chain acyl-CoA dehydrogenase
-
-
long-chain acyl-CoA dehydrogenase
-
-
long-chain acyl-CoA hydrolase
-
-
long-chain acyl-coenzyme A dehydrogenase
-
-
-
-
MTE-II
-
-
palmitoyl-CoA dehydrogenase
-
-
-
-
palmitoyl-coenzyme A dehydrogenase
-
-
-
-
type-II acyl-CoA thioesterase
-
-
very long-chain acyl-CoA dehydrogenase
-
metabolizes C14-C18 acyl-carnitines
very-long-chain acyl-CoA dehydrogenase
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
dehydrogenation
-
-
-
-
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
2-methylheptanoyl-CoA + acceptor
?
show the reaction diagram
-
activity assay
-
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + acceptor
(2E,9Z)-2,9-octadecadienoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + acceptor
?
show the reaction diagram
-
activity assay
-
-
?
palmitoyl-CoA + electron-transfer flavoprotein
(2E)-2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
additional information
?
-
-
hydrolysis of acyl-CoAs
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + electron-transfer flavoprotein
(2E)-2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
enzyme does not affect all acyl-CoA utilizing cellular processes
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.06037
-
LCAD enzyme activity in livers of partially deficient LCAD mice 8 weeks after injection of recombinant adeno-associated viral mLCAD vector via the hepatic portal vein
0.2546
-
LCAD enzyme activity in tibialis anterior muscle of LCAD-heterozygous deficient mice 10 weeks post-injection 1 x 10exp11 vg recombinant adeno-associated viral mLCAD
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32
-
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
before postnatal day 10, BACH is detected at very low levelsthen, BACH content rapidly increases from postnatal day 14 and reaches maximum levels at postnatal day 21, remaining high until at least postnatal day 70
Manually annotated by BRENDA team
additional information
-
not detectable in spermatogonia
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
CTE-II
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACADL_MOUSE
430
0
47908
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
x * 43000
44000
-
determined by SDS-PAGE and Western Blot analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 43000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a vector plasmid pCB-mLCAD for transfection of LCAD-deficient mice is used
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transient and stable expression as C-terminally MYC-tagged enzyme in mouse C3H 10T1/2 fibroblastic cells using a mifepristone-inducible gene expression system, analysis of cell growth rates, enzyme expression rates, and effect on phospholipid synthesis, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
additional information
-
CTE-II expression is induced during embryogenesis in association with neuronal differentiation, and persists after terminal differentiation in neurons at postnatal stages, resulting in constitutive high expression in the adult brain in a neuron-specific manner
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kurtz, D.M.; Tolwani, R.J.; Wood, P.A.
Structural characterization of the mouse long-chain acyl-CoA dehydrogenase gene and 5' regulatory region
Mamm. Genome
9
361-365
1998
Mus musculus (P51174), Mus musculus
Manually annotated by BRENDA team
Takagi, M.; Yamakawa, H.; Watanabe, T.; Suga, T.; Yamada, J.
Inducible expression of long-chain acyl-CoA hydrolase gene in cell cultures
Mol. Cell. Biochem.
252
379-385
2003
Mus musculus
Manually annotated by BRENDA team
Berger, P.S.; Wood, P.A.
Disrupted blastocoele formation reveals a critical developmental role for long-chain acyl-CoA dehydrogenase
Mol. Genet. Metab.
82
266-272
2004
Mus musculus
Manually annotated by BRENDA team
Takagi, M.; Ohtomo, T.; Hiratsuka, K.; Kuramochi, Y.; Suga, T.; Yamada, J.
Localization of a long-chain acyl-CoA hydrolase in spermatogenic cells in mice
Arch. Biochem. Biophys.
446
161-166
2006
Mus musculus
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
Werdich, A.A.; Baudenbacher, F.; Dzhura, I.; Jeyakumar, L.H.; Kannankeril, P.J.; Fleischer, S.; LeGrone, A.; Milatovic, D.; Aschner, M.; Strauss, A.W.; Anderson, M.E.; Exil, V.J.
Polymorphic ventricular tachycardia and abnormal Ca2+ handling in very-long-chain acyl-CoA dehydrogenase null mice
Am. J. Physiol. Heart Circ. Physiol.
292
H2202-H2211
2007
Mus musculus
Manually annotated by BRENDA team
Primassin, S.; Ter Veld, F.; Mayatepek, E.; Spiekerkoetter, U.
Carnitine supplementation induces acylcarnitine production in tissues of very long-chain acyl-CoA dehydrogenase-deficient mice, without replenishing low free carnitine
Pediatr. Res.
63
632-637
2008
Mus musculus
Manually annotated by BRENDA team
Zhang, D.; Liu, Z.X.; Choi, C.S.; Tian, L.; Kibbey, R.; Dong, J.; Cline, G.W.; Wood, P.A.; Shulman, G.I.
Mitochondrial dysfunction due to long-chain acyl-CoA dehydrogenase deficiency causes hepatic steatosis and hepatic insulin resistance
Proc. Natl. Acad. Sci. USA
104
17075-17080
2007
Mus musculus
Manually annotated by BRENDA team
Beattie, S.G.; Goetzman, E.; Tang, Q.; Conlon, T.; Campbell-Thompson, M.; Matern, D.; Vockley, J.; Flotte, T.R.
Recombinant adeno-associated virus-mediated gene delivery of long chain acyl coenzyme A dehydrogenase (LCAD) into LCAD-deficient mice
J. Gene Med.
10
1113-1123
2008
Mus musculus
Manually annotated by BRENDA team