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Information on EC 1.3.8.8 - long-chain acyl-CoA dehydrogenase and Organism(s) Homo sapiens and UniProt Accession P49748

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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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Homo sapiens
UNIPROT: P49748
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The taxonomic range for the selected organisms is: Homo sapiens
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
very-long-chain acyl-CoA dehydrogenase
-
very-long-chain acyl-coenzyme A dehydrogenase
-
ACAD 9
-
-
acyl-CoA dehydrogenase 9
-
-
BACH
-
-
CTE-II
-
-
long chain acyl-CoA dehydrogenase
-
-
long-chain acyl-CoA dehydrogenase
-
-
long-chain acyl-CoA hydrolase
-
-
long-chain acyl-coenzyme A dehydrogenase
-
-
-
-
MCAD
-
-
medium long-chain acyl-CoA dehydrogenase
-
-
MTE-II
-
-
palmitoyl-CoA dehydrogenase
-
-
-
-
palmitoyl-coenzyme A dehydrogenase
-
-
-
-
type-II acyl-CoA thioesterase
-
-
very long chain acyl-CoA dehydrogenase
very long-chain acyl-CoA dehydrogenase
-
-
very-long-chain acyl-CoA dehydrogenase
VLCAD
VLMCAD
-
-
additional information
-
see also EC 3.1.2.2, palmitoyl-CoA hydrolase
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
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
palmitoyl-CoA + acceptor
2,3-unsaturated-palmitoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
palmitoyl-CoA + electron-transfer flavoprotein
(2E)-2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
(R/S)-2-methylpalmitoyl-CoA + electron-transfer flavoprotein
2,3-dehydro-2-methylpalmitoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
(S)-2-methylpentadecanoyl-CoA + electron-transfer flavoprotein
2-methyl-2-pentadecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
2,6-dimethylheptanoyl-CoA + oxidized flavin
2,3-dehydro-2,6-dimethylheptanoyl-CoA + reduced flavin
show the reaction diagram
-
specific LCAD substrate
-
-
?
3-keto-palmitoyl-CoA + acceptor
?
show the reaction diagram
-
-
-
-
?
arachidonoyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
-
48.9% activity compared to the wild type enzyme
-
-
?
arachidonoyl-CoA + electron transfer flavoprotein
(2E,5Z,8Z,11Z,14Z)-2,5,8,11,14-eicosapentaenoyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
-
48.9% activity compared to palmitoyl-CoA
-
-
?
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
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
-
-
-
?
hexanoyl-CoA + electron-transfer flavoprotein
2-hexenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
lineoyl-CoA + acceptor
2,9,12-octadecatrienoyl-CoA + reduced acceptor
show the reaction diagram
-
12.5% activity compared to the wild type enzyme
-
-
?
linoleoyl-CoA + acceptor
2,9,12-octadecatrienoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
linoleoyl-CoA + electron transfer flavoprotein
2,9,12-octadecatrienoyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
-
12.5% activity compared to palmitoyl-CoA
-
-
?
myristoyl-CoA + acceptor
2-tetradecenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
-
51.1% activity compared to the wild type enzyme
-
-
?
myristoyl-CoA + acceptor
trans(2)-tetradecenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
51.1% activity compared to palmitoyl-CoA
-
-
?
octanoyl-CoA + 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 + electron transfer flavoprotein
2,9-octadecadienoyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
-
40.8% activity compared to palmitoyl-CoA
-
-
?
palmitoleoyl-CoA + acceptor
(2E,9Z)-2,9-hexadecadienoyl-CoA + reduced acceptor
show the reaction diagram
-
34.8% activity compared to the wild type enzyme
-
-
?
palmitoleoyl-CoA + acceptor
?
show the reaction diagram
-
VLCAD activity assay
-
-
?
palmitoleoyl-CoA + electron transfer flavoprotein
(2E,9Z)-2,9-hexadecadienoyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
-
34.8% activity compared to palmitoyl-CoA
-
-
?
palmitoyl-CoA + acceptor
?
show the reaction diagram
palmitoyl-CoA + electron transfer flavoprotein
2-hexadecenoyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
-
100% activity with palmitoyl-CoA
-
-
?
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 + acceptor
2-octadecenoyl-CoA + reduced acceptor
show the reaction diagram
-
39% activity compared to the wild type enzyme
-
-
?
stearoyl-CoA + electron transfer flavoprotein
2-octadecenoyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
-
39.0% activity compared to palmitoyl-CoA
-
-
?
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
tetradecanoyl-CoA + phenazine methosulfate
2-tetradecenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
additional information
?
-
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
2,6-dimethylheptanoyl-CoA + oxidized flavin
2,3-dehydro-2,6-dimethylheptanoyl-CoA + reduced flavin
show the reaction diagram
-
specific LCAD substrate
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
-
a flavoenzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-octynoyl-CoA
N-ethylmaleimide
-
10% inhibition at 0.25 mM in control fibroblasts
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bezafibrate
increased VLCAD residual enzyme activity in the presence of 0.4 mM bezafibrate
bezafibrate
-
stimulates VLCAD gene expression to 44% in normal and to 150% in VLCAD-deficient fibroblasts, increases activity 2.2fold in normal fibroblasts, induces a dose-dependent increase in palmitate oxidation capacities in cells from patients with the myopathic form of VLCAD deficiency, complete normalization of cell fatty acid oxidation capacities after exposure to 500 mM for 48 h, but not in cells from severely affected patients
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
decanoyl-CoA
-
-
0.007
dodecanoyl-CoA
-
-
0.012
electron-transfer flavoprotein
-
saturating dodecanoyl-CoA, measured with ETF from pig kidney
0.029
hexanoyl-CoA
-
-
0.00471 - 0.008
octanoyl-CoA
0.00087 - 0.014
palmitoyl-CoA
0.008
stearoyl-CoA
-
-
0.01
tetradecanoyl-CoA
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.25
decanoyl-CoA
-
-
2.25
octanoyl-CoA
-
-
2.17
palmitoyl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00238
-
MCAD activity, controls
0.00695
-
VLCAD activity, controls, range 0.00195 to 0.01191
0.01241
-
fibroblast homogenates, palmitoyl-CoA
0.27
-
purified enzyme, (R/S)-2-methylpalmitoyl-CoA
0.34
-
purified enzyme, (S)-2-methylpentadecanoyl-CoA
0.39
-
purified enzyme, palmitoyl-CoA
15.27
-
purified enzyme, decanoyl-CoA
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
very low enzyme content
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
embryonic spinal cord shows low but significant activity, activity with 3-keto-palmitoyl-CoA as substrate is 23% and with palmitoyl-CoA 11% of the corresponding activity in adult liver
Manually annotated by BRENDA team
additional information
-
LCAD real-time RT-PCR expression analysis in different tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
CTE-II
Manually annotated by BRENDA team
-
CTE-II
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
long-chain acyl-CoA dehydrogenase is a mitochondrial flavoenzyme that plays no role in long-chain fatty acid beta-oxidation in heart, liver, and skeletal muscle, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACADV_HUMAN
655
0
70390
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
-
120000
-
HPLC gel filtration
180000
-
gel filtration
43000
-
x * 43000
44000
-
x * 44000, SDS-PAGE
70000
-
Western blot analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with myristoyl-CoA, hanging drop vapour diffusion method, in 0.1 M HEPES, pH 7.5, 17.6% polyethylene glycol 2000, 0.047 M MgCl2, and 5% glycerol
-
in complex with myristoyl-CoA, sitting drop vapour diffusion method, in 0.1 M HEPES, pH 7.5, 17.6% polyethylene glycol 2000, 0.047 M MgCl2, and 5% glycerol
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K259M
missense mutation leading to VLCAD deficiency
L462Q
missense mutation leading to VLCAD deficiency
997insT
-
frameshift, heterozygote mutation of exon 10, mutation of a myopathic-type very-long-chain acyl-CoA dehydrogenase deficiency
A364G
-
patient died suddenly in infancy, severe VLCAD deficiency
A450P
A985G
-
nearly all patients with residual MCAD activities below 2.5% are homozygous 985A>G carriers
E261Q
-
mutant exhibits less than 0.02% of the wild-type activity
G520A
-
patient symptomatic, with episodic rhabdomyolysis
K264E
-
A790G, heterozygote mutation of exon 9
L462P
R429W
R573W
T199C
-
all patients with the 199T>C mutation have residual activities above 10%
T220M
T848C
-
patients asymptomatic on dietary management
V243A
additional information
-
VLCAD deficient fibroblasts and pCMV-hVLCAD transiently transfected VLCAD deficient fibroblasts, show antibody specificity, transfected fibroblasts show correction of the metabolic block as demonstrated by normalization of C14- and C16-acylcarnitine species in cell culture media and restoration of VLCAD activity in cells
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
40-80% ammonium sulfate precipitation, Q-Sepharose I, Q-Sepharose II, hydroxyapatite
-
ammonium sulfate precipitation and DEAE-Sepharose Fast Flow column chromatography
-
ammonium sulfate precipitation, DEAE Sepharose column chromatography, and SP Sepharose column chromatography
-
DEAE-Sepharose Fast Flow column chromatography and SP-Sepharose Fast Flow column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C43 (DE3) cells
-
expressed in Escherichia coli strain C43 (DE3)
-
expressed in Escherichia coli strain C43(DE3)
-
expression in Escherichia coli
-
expression in Escherichia coli, strain BL21(DE)
-
into plasmid pCMV, expression in immune competent mice
-
LCAD real-time RT-PCR expression analysis in different tissues
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chalmers, R.A.; English, N.
Fatty acid oxidation in cultured skin fibroblasts from patients with inherited disorders of fatty acid metabolism: studies on the specificity of acyl-CoA dehydrogenases
Biochem. Soc. Trans.
15
489-491
1987
Homo sapiens
-
Manually annotated by BRENDA team
Nandy, A.; Kieweg, V.; Kraeutle, F.G.; Vock, P.; Kuechler, B.; Bross, P.; Kim, J.J.P.; Rasched, I.; Ghisla, S.
Medium-long-chain chimeric human acyl-CoA dehydrogenase: medium-chain enzyme with the active center base arrangement of long-chain acyl-CoA dehydrogenase
Biochemistry
35
12402-12411
1996
Homo sapiens
Manually annotated by BRENDA team
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
Gohil, K.; Jones, D.A.; Edwards, R.H.T.
Fatty acid oxidation in human skeletal muscle mitochondria
Biochem. Soc. Trans.
11
728-729
1983
Homo sapiens
-
Manually annotated by BRENDA team
Ijlst, L.; Wanders,R.J.A.
A simple spectrophotometric assay for long-chain acyl-CoA dehydrogenase activity measurements in human skin fibroblasts
Ann. Clin. Biochem.
30
293-297
1993
Homo sapiens
-
Manually annotated by BRENDA team
Djordjevic, S.; Dong, Y.; Paschke, R.; Frerman, F.E.; Strauss, A.W.; Kim, J.J.
Identification of the catalytic base in long chain acyl-CoA dehydrogenase
Biochemistry
33
4258-4264
1994
Homo sapiens
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
Battaile, K.P.; McBurney, M.; Van Veldhoven, P.P.; Vockley, J.
Human long chain, very long chain and medium chain acyl-CoA dehydrogenases are specific for the S-enantiomer of 2-methylpentadecanoyl-CoA
Biochim. Biophys. Acta
1390
333-338
1998
Homo sapiens
Manually annotated by BRENDA team
Clark-Taylor, T.; Clark-Taylor, B.E.
Is autism a disorder of fatty acid metabolism? Possible dysfunction of mitochondrial beta-oxidation by long chain acyl-CoA dehydrogenase
Med. Hypotheses
62
970-975
2004
Homo sapiens
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
Oey, N.A.; Ruiter, J.P.N.; Ijlst, L.; Attie-Bitach, T.; Vekemans, M.; Wanders, R.J.A.; Wijburg, F.A.
Acyl-CoA dehydrogenase 9 (ACAD 9) is the long-chain acyl-CoA dehydrogenase in human embryonic and fetal brain
Biochem. Biophys. Res. Commun.
346
33-37
2006
Homo sapiens
Manually annotated by BRENDA team
Djouadi, F.; Aubey, F.; Schlemmer, D.; Ruiter, J.P.N.; Wanders, R.J.A.; Strauss, A.W.; Bastin, J.
Bezafibrate increases very-long-chain acyl-CoA dehydrogenase protein and mRNA expression in deficient fibroblasts and is a potential therapy for fatty acid oxidation disorders
Hum. Mol. Genet.
14
2695-2703
2005
Homo sapiens
Manually annotated by BRENDA team
Merritt II, J.L.; Matern, D.; Vockley, J.; Daniels, J.; Ngyen, T.V.; Schowalter, D.B.
In vitro characterization and in vivo expression of human very-long chain acyl-CoA dehydrogenase
Mol. Genet. Metab.
88
351-358
2006
Homo sapiens
Manually annotated by BRENDA team
Gobin-Limballe, S.; Djouadi, F.; Aubey, F.; Olpin, S.; Andresen, B.S.; Yamaguchi, S.; Mandel, H.; Fukao, T.; Ruiter, J.P.; Wanders, R.J.; McAndrew, R.; Kim, J.J.; Bastin, J.
Genetic basis for correction of very-long-chain acyl-coenzyme A dehydrogenase deficiency by bezafibrate in patient fibroblasts: toward a genotype-based therapy
Am. J. Hum. Genet.
81
1133-1143
2007
Homo sapiens (P49748), Homo sapiens
Manually annotated by BRENDA team
Law, L.K.; Tang, N.L.; Tong, M.K.; Mak, T.W.; Wanders, R.J.; Lam, C.W.
Novel missense mutations in the first Chinese patient with very-long-chain acyl-CoA dehydrogenase deficiency
Clin. Chim. Acta
375
173-174
2007
Homo sapiens (P49748)
Manually annotated by BRENDA team
McAndrew, R.P.; Wang, Y.; Mohsen, A.W.; He, M.; Vockley, J.; Kim, J.J.
Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase
J. Biol. Chem.
283
9435-9443
2008
Homo sapiens
Manually annotated by BRENDA team
Zia, A.; Kolodny, E.H.; Pastores, G.M.
Very long chain acyl-CoA dehydrogenase deficiency in a pair of mildly affected monozygotic twin sister in their late fifties
J. Inherit. Metab. Dis.
30
817-817
2007
Homo sapiens
Manually annotated by BRENDA team
Goetzman, E.S.; Wang, Y.; He, M.; Mohsen, A.W.; Ninness, B.K.; Vockley, J.
Expression and characterization of mutations in human very long-chain acyl-CoA dehydrogenase using a prokaryotic system
Mol. Genet. Metab.
91
138-147
2007
Homo sapiens
Manually annotated by BRENDA team
Tajima, G.; Sakura, N.; Shirao, K.; Okada, S.; Tsumura, M.; Nishimura, Y.; Ono, H.; Hasegawa, Y.; Hata, I.; Naito, E.; Yamaguchi, S.; Shigematsu, Y.; Kobayashi, M.
Development of a new enzymatic diagnosis method for very-long-chain acyl-CoA dehydrogenase deficiency by detecting 2-hexadecenoyl-CoA production and its application in tandem mass spectrometry-based selective screening and newborn screening in Japan
Pediatr. Res.
64
667-672
2008
Homo sapiens
Manually annotated by BRENDA team
Arnold, G.L.; Van Hove, J.; Freedenberg, D.; Strauss, A.; Longo, N.; Burton, B.; Garganta, C.; Ficicioglu, C.; Cederbaum, S.; Harding, C.; Boles, R.G.; Matern, D.; Chakraborty, P.; Feigenbaum, A.
A Delphi clinical practice protocol for the management of very long chain acyl-CoA dehydrogenase deficiency
Mol. Genet. Metab.
96
85-90
2009
Homo sapiens
Manually annotated by BRENDA team
Korematsu, S.; Kosugi, Y.; Kumamoto, T.; Yamaguchi, S.; Izumi, T.
Novel mutation of early, perinatal-onset, myopathic-type very-long-chain acyl-CoA dehydrogenase deficiency
Pediatr. Neurol.
41
151-153
2009
Homo sapiens
Manually annotated by BRENDA team
ter Veld, F.; Mueller, M.; Kramer, S.; Haussmann, U.; Herebian, D.; Mayatepek, E.; Laryea, M.D.; Primassin, S.; Spiekerkoetter, U.
A novel tandem mass spectrometry method for rapid confirmation of medium- and very long-chain acyl-CoA dehydrogenase deficiency in newborns
PLoS ONE
4
e6449
2009
Homo sapiens
Manually annotated by BRENDA team
Maher, A.C.; Mohsen, A.W.; Vockley, J.; Tarnopolsky, M.A.
Low expression of long-chain acyl-CoA dehydrogenase in human skeletal muscle
Mol. Genet. Metab.
100
163-167
2010
Homo sapiens
Manually annotated by BRENDA team