Information on EC 1.3.8.8 - long-chain acyl-CoA dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.3.8.8
-
RECOMMENDED NAME
GeneOntology No.
long-chain acyl-CoA dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain acyl-CoA + electron-transfer flavoprotein = a long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenation
-
-
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oxidation
redox reaction
-
-
-
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reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(8E,10E)-dodeca-8,10-dienol biosynthesis
-
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Fatty acid degradation
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Metabolic pathways
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lipid metabolism
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain M-1, gene acdB
SwissProt
Manually annotated by BRENDA team
strain M-1, gene acdB
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strains: TH181, TH182, TH183, RS3010
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-
Manually annotated by BRENDA team
common sunflower
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme belongs to the acyl-CoA dehydrogenases family of FAD-dependent flavoproteins that catalyze the alpha,beta-dehydrogenation of thioester substrates
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(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
-
-
?
2-methylheptanoyl-CoA + acceptor
?
show the reaction diagram
-
activity assay
-
-
?
3-keto-palmitoyl-CoA + acceptor
?
show the reaction diagram
-
-
-
-
?
4-cis-7-cis-decadienoyl-CoA + Meldola's Blue
2-trans-4,7-cis,cis-decatrienoyl-CoA + reduced meldola blue
show the reaction diagram
-
-
-
?
4-cis-decenoyl-CoA + Meldola's Blue
2-trans-4-cis-decadienoyl-CoA + reduced meldola blue
show the reaction diagram
-
-
-
?
5-cis-decenoyl-CoA + Meldola's Blue
2-trans-5-cis-decadienoyl-CoA + reduced meldola blue
show the reaction diagram
-
-
-
?
6-cis-decenoyl-CoA + Meldola's Blue
2-trans-6-cis-decadienoyl-CoA + reduced meldola blue
show the reaction diagram
-
-
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
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
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48.9% activity compared to palmitoyl-CoA
-
-
?
arachidonoyl-CoA + phenazine methosulfate
(2E,5Z,8Z,11Z,14Z)-2,5,8,11,14-eicosapentaenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
arachidonyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
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48.9% activity compared to the wild type enzyme
-
-
?
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
-
-
-
?
cis,cis,cis,cis-4,7,10,13-hexadecatetraenoyl-CoA + Meldola's Blue
2-trans-4,7,10,13-cis,cis,cis,cis-hexadecapentaenoyl-CoA + reduced meldola blue
show the reaction diagram
-
-
-
?
decanoyl-CoA + electron-transfer flavoprotein
2-decenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
decanoyl-CoA + Meldola's Blue
2-decenoyl-CoA + reduced meldola blue
show the reaction diagram
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-
trans-isomer
?
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 + Meldola's Blue
2-dodecenoyl-CoA + reduced meldola blue
show the reaction diagram
-
-
trans-isomer
?
dodecanoyl-CoA + phenazine methosulfate
(2E)-2-dodecenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
eicosanoyl-CoA + electron-transfer flavoprotein
2-eicosenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
eicosanoyl-CoA + phenazine methosulfate
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 + Meldola's Blue
(2E)-2-hexenoyl-CoA + reduced meldola blue
show the reaction diagram
-
-
trans-isomer
?
hexanoyl-CoA + phenazine methosulfate
2-hexenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
lauroyl-CoA + acceptor
2-dodecenoyl-CoA + reduced acceptor
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
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-
?
linolenoyl-CoA + phenazine methosulfate
(2E,6Z,9Z,12Z)2,6,9,12-octadecatetraenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
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
-
-
?
linoleoyl-CoA + phenazine methosulfate
(2E,9Z,12Z)-2,9,12-octadecatrienoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
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-
-
?
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
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
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-
-
-
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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 + Meldola's Blue
(2E)-2-octenoyl-CoA + reduced meldola blue
show the reaction diagram
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-
trans-isomer
?
octanoyl-CoA + phenazine methosulfate
2-octenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
oleoyl-CoA + acceptor
(2E,9Z)-2,9-octadecadienoyl-CoA + reduced acceptor
show the reaction diagram
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-
-
-
?
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
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-
?
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 + acceptor
(2E,9Z)-2,9-hexadecadienoyl-CoA + reduced acceptor
show the reaction diagram
-
34.8% activity compared to the wild type enzyme
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-
?
palmitoleoyl-CoA + acceptor
?
show the reaction diagram
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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
-
-
?
palmitoleoyl-CoA + phenazine methosulfate
(2E,9Z)-2,9-hexadecadienoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
palmitoyl-CoA + acceptor
2,3-unsaturated-palmitoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
palmitoyl-CoA + acceptor
2-hexadecenoyl-CoA + reduced acceptor
show the reaction diagram
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
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-
?
palmitoyl-CoA + electron-transfer flavoprotein
2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
palmitoyl-CoA + Meldola's Blue
2-hexadecenoyl-CoA + reduced meldola blue
show the reaction diagram
-
-
trans-isomer
?
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
stearoyl-CoA + Meldola's Blue
2-octadecenoyl-CoA + reduced meldola blue
show the reaction diagram
-
-
trans-isomer
?
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 + Meldola's Blue
2-tetradecenoyl-CoA + reduced meldola blue
show the reaction diagram
-
-
trans-isomer
?
tetradecanoyl-CoA + phenazine methosulfate
2-tetradecenoyl-CoA + reduced phenazine methosulfate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
-
-
?
lauroyl-CoA + acceptor
2-dodecenoyl-CoA + reduced acceptor
show the reaction diagram
palmitoyl-CoA + acceptor
2-hexadecenoyl-CoA + reduced acceptor
show the reaction diagram
-
enzyme does not affect all acyl-CoA utilizing cellular processes
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
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a flavoenzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hexadecenoyl-CoA
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2-mercaptoacetate
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inhibition by administration in vivo
2-octynoyl-CoA
Ag+
1 mM, complete inhibition of the recombinant enzyme
AgNO3
-
strong inhibition of apo and holo forms at 0.1 mM
Cu2+
1 mM, complete inhibition of the recombinant enzyme
CuCl2
-
strong inhibition of apo and holo forms at 0.1 mM
Hg2+
1 mM, 61% inhibition of the recombinant enzyme
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
Mn2+
1 mM, 72% inhibition of the recombinant enzyme
N-ethylmaleimide
p-chloromercuribenzoate
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inhibition of enzyme-catalyzed C-2 proton-deuteron exchange reactions
p-hydroxymercuribenzoate
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strong inhibition of the apoenzyme at 0.1 mM, not inhibitory for the holo form even at higher concentrations like 1 mM
palmitoyl-CoA
-
inhibition by micelle formation at concentrations up to 0.004 mM, reversed by fatty acid free bovine serum albumin
Pb2+
1 mM, 23% inhibition of the recombinant enzyme
Zn2+
1 mM, 19% inhibition of the recombinant enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bezafibrate
Clofibrate
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activation, treated animals receiving 0.5% w/w neutralized acid for 2 weeks
peroxisome proliferator
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-
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Triton X-100
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restores activity during ischemia
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.32
4-cis,7-cis-decadienoyl-CoA
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-
0.25
4-cis-Decenoyl-CoA
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-
0.2
5-cis-decenoyl-CoA
-
-
0.32
6-cis-decenoyl-CoA
-
-
0.24
cis,cis,cis,cis-4,7,10,13-hexadecatetraenoyl-CoA
-
-
0.0022 - 0.13
decanoyl-CoA
0.0015 - 0.2
Dodecanoyl-CoA
0.0008 - 0.012
electron-transfer flavoprotein
0.0014 - 0.0025
FAD
0.0063 - 0.55
Hexanoyl-CoA
0.068
lauroyl-CoA
pH 8.5, recombinant enzyme
0.0033 - 0.23
Octanoyl-CoA
0.0065
oleoyl-CoA
-
-
0.00064
omega-phenyldecanoyl-CoA
-
-
0.00164
omega-phenyldodecanoyl-CoA
-
-
0.00087 - 0.78
palmitoyl-CoA
1 - 1.1
phenazine methosulfate
0.0037 - 0.29
stearoyl-CoA
0.0023 - 0.38
tetradecanoyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.25
decanoyl-CoA
Homo sapiens
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-
2.25
Octanoyl-CoA
Homo sapiens
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-
0.5 - 5.4
palmitoyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00034
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crude extract, strain TH183, genotype fadR251(S), acetate and oleate as carbon source
0.00052
-
crude extract, strain TH18, genotype fadR251(S), acetate as carbon source
0.00064
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crude extract, strain TH182, genotype fadR250(S) acetate as carbon source
0.00083
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crude extract, strain TH182, genotype fadR250(S), acetate and oleate as carbon source
0.0011
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crude extract, strain TH181, genotype fadR+, acetate as carbon source
0.00238
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MCAD activity, controls
0.0038
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crude extract, strain TH181, genotype fadR+, acetate and oleate as carbon source
0.0046
-
crude extract, strain RS3010, genotype fadR1, acetate as carbon source
0.0055
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crude extract, strain RS3010, genotype fadR1, acetate and oleate as carbon source
0.00695
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VLCAD activity, controls, range 0.00195 to 0.01191
0.01241
-
fibroblast homogenates, palmitoyl-CoA
0.06
-
purified holoenzyme, arachidonoyl-CoA
0.06037
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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
0.076
-
purified enzyme, butyryl-CoA
0.19
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purified enzyme, palmitoyl-CoA, 0.12 nmol/ml ETF
0.2546
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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
0.259
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purified enzyme, palmitoyl-CoA, 0.24 nmol/ml ETF
0.27
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purified enzyme, (R/S)-2-methylpalmitoyl-CoA
0.272
-
purified enzyme, octanoyl-CoA
0.3
-
purified holoenzyme, docosanoyl-CoA
0.34
-
purified enzyme, (S)-2-methylpentadecanoyl-CoA
0.38
-
purified holoenzyme, linolenoyl-CoA
0.39
-
purified enzyme, palmitoyl-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
15.27
-
purified enzyme, decanoyl-CoA
32.5
-
purified enzyme, decanoyl-CoA
additional information
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heterozygous ACADVL mutation carriers show residual VLCAD activities of 23.7 to 54.2%; residual VLCAD activity of patients with confirmed VLCAD-deficiency is between 0.3 and 1.1%
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32
-
activity assay
37
-
activity assay
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
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embryonic axis of early-germinating
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
-
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44672
-
x * 44672, subunit, nucleotide sequence
64000
2 * 64833, amino acid sequence determination, 2 * 64000, recombinant enzyme, SDS-PAGE
64833
2 * 64833, amino acid sequence determination, 2 * 64000, recombinant enzyme, SDS-PAGE
70000
-
Western blot analysis
110000
-
-
120000
-
HPLC gel filtration
135000
recombinant enzyme, gel filtration
168000
-
gel filtration
172000
-
gel electrophoresis
180000
200000
-
gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purifed recombinant enzyme, hanging drop vapour diffusion method, 7 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 150 mM sodium chloride, is mixed with 100 mM Tris-HCl, pH 8.0, 150 mM NaCl, 200 mM magnesium formate and 13% PEG 3350, 16░C, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.7
-
stable for at least 10 min at 37░C
391272
8 - 10
recombinant enzyme
656313
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
purified recombinant enzyme, 30 min, 80% remaining activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20░C
-
-20║C, stable for at least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
35-80% ammonium sulfate precipitation, DEAE-Sephadex A-50, hydroxyapatite
-
40-60% ammonium sulfate precipitation, DEAE-Sepharose, hydroxyapatite
-
40-70% ammonium sulfate precipitation, Sephadex G-150, DEAE-cellulose, preparative electrophoresis
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40-75% ammonium sulfate precipitation, G-200 electrophoresis
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40-80% ammonium sulfate precipitation, DEAE-Sephadex A-50, hydroxyapatite, matrex gel blue A, agarose-hexane-CoA, bio-gel A-0.5m
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40-80% ammonium sulfate precipitation, Q-Sepharose I, Q-Sepharose II, hydroxyapatite
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ammonium sulfate precipitation and DEAE-Sepharose Fast Flow column chromatography; DEAE-Sepharose Fast Flow column chromatography and SP-Sepharose Fast Flow column chromatography
-
ammonium sulfate precipitation, DEAE Sepharose column chromatography, and SP Sepharose column chromatography
-
ammonium sulfate precipitation, zone electrophoresis
-
DEAE-cellulose, blue dextran-sepharose, calcium phosphate gel-cellulose, blue dextran-sepharose, HPLC
-
Q-Sepharose, hydroxyapatite I, hydroxyapatite II
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recombinant acdB-encoded enzyme from Escherichia coli
recombinant enzyme from Escherichia coli strain BL21(DE3)
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a vector plasmid pCB-mLCAD for transfection of LCAD-deficient mice is used
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expressed in Escherichia coli C43 (DE3) cells
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expressed in Escherichia coli strain C43 (DE3); expressed in Escherichia coli strain C43(DE3)
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expression in Escherichia coli
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expression in Escherichia coli strain BL21(DE3)
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expression in Escherichia coli, strain BL21(DE)
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expression in Escherichia coli, strain XL1-blue
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gene acdB, DNA and amino acid sequence determination and analysis, genes acdA and acdB are arranged in a tandem, expression of gene acdB in Escherichia coli strain JM109
into plasmid pCMV, expression in immune competent mice
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LCAD real-time RT-PCR expression analysis in different tissues
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
997insT
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frameshift, heterozygote mutation of exon 10, mutation of a myopathic-type very-long-chain acyl-CoA dehydrogenase deficiency
A364G
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patient died suddenly in infancy, severe VLCAD deficiency
A450P
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mutant shows normal wild type activity and greatly reduced mitochondrial membrane association; unpurified recombinant enzyme shows increased activity, pure mutant enzyme has wild type activity
A985G
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nearly all patients with residual MCAD activities below 2.5% are homozygous 985A>G carriers
E261Q
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mutant exhibits less than 0.02% of the wild-type activity
G520A
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patient symptomatic, with episodic rhabdomyolysis
K259M
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missense mutation leading to VLCAD deficiency
K264E
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A790G, heterozygote mutation of exon 9
L462P
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in the pure form, mutant has roughly 30% of wild type activity and greatly reduced mitochondrial membrane association; unpurified recombinant enzyme shows increased activity, pure mutant enzyme has 30% activity compared to the wild type enzyme
L462Q
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missense mutation leading to VLCAD deficiency
R429W
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mutant shows 0.2% of wild type activity, the mutation leads to a severe form of VLCAD deficiency; the mutation is observed in the severe form of VLCAD deficiency
R573W
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no activity, the mutation leads to a severe form of VLCAD deficiency; shows 0.2% of wild type activity
T199C
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all patients with the 199T>C mutation have residual activities above 10%
T220M
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mutant shows 3% of wild type activity, the mutation leads to a mild form of VLCAD deficiency; shows 3% of wild type activity, the mutation is observed in the mild form of VLCAD deficiency
T848C
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patients asymptomatic on dietary management
V243A
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mutant shows 22% of wild type activity, the mutation leads to a mild form of VLCAD deficiency; shows 22% of wild type activity, the mutation is observed in the mild form of VLCAD deficiency
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
additional information
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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
Show AA Sequence (273 entries)
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