Information on EC 1.3.8.9 - very-long-chain acyl-CoA dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.8.9
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RECOMMENDED NAME
GeneOntology No.
very-long-chain acyl-CoA dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a very-long-chain acyl-CoA + electron-transfer flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(8E,10E)-dodeca-8,10-dienol biosynthesis
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Spodoptera littoralis pheromone biosynthesis
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lipid metabolism
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Fatty acid degradation
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
very-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 is most active toward long-chain acyl-CoAs such as C14, C16 and C18, but is also active with very-long-chain acyl-CoAs up to 24 carbons. It shows no activity for substrates of less than 12 carbons. Its specific activity towards palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase [1]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.8, long-chain acyl-CoA dehydrogenase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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phosphorylation of VLCAD at Ser586 is inhibited in myofibroblasts, resulting in a significant loss of enzyme activity coupled with lipid peroxidation.Thus Ser586 represents a critical site for VLCAD activity, whose dysregulation might contribute to the progression of idiopathic pulmonary fibrosis, IPF, a chronic interstitial lung disease, and other oxidative-stress mediated diseases
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
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
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?
palmitoyl-CoA + acceptor
2-hexadecenoyl-CoA + reduced acceptor
show the reaction diagram
additional information
?
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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
additional information
?
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acyl-CoA dehydrogenases, ACADs, constitute a family of FAD-dependent flavoproteins that catalyze the alpha,beta-dehydrogenation of thioester substrates
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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SIRT3 deacetylates and SIRT5 desuccinylates K299 which serves to stabilize the essential FAD cofactor in the active site of the enzyme
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
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about, size-exclusion chromatography coupled with in-line static light-scattering, refractive-index and ultraviolet measurements
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 x 45000, about, size-exclusion chromatography coupled with in-line static light-scattering, refractive-index and ultraviolet measurements
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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phosphorylation of Ser586 is essential for VLCAD function
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant cVLCAD, hanging-drop vapour-diffusion method, 0.002 ml of 12 mg/ml protein in 20 mM Tris-HCl pH 8.0, 150 mM NaCl are mixed with 0.002 ml of reservoir solution containing 100 mM Tris-HCl, pH 8.0, 150 mM NaCl, 200 mM magnesium formate and 13% PEG 3350, 16°C, 3 days, X-ray diffraction structure determination and analysis at 1.8-2.6 A resolution, molecular replacement
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose resin column chromatography
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recombinant His8-tagged VLCAD from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography, anion exchange chromatography, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning from cDNA library, His8-tagged VLCAD expression in Escherichia coli strain BL21 (DE3)
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expressed in Escherichia coli XL1Blue cells
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expression of wild-type enzyme and mutant S586A in HEK293 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S586A
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naturally occuring mutation leading to phosphorylation of VLCAD at Ser586 is inhibited in myofibroblasts, resulting in a significant loss of enzyme activity coupled with lipid peroxidation. The S586A mutant shows a significant reduction in electron transfer activity
T409M
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the mutation is associated with partial carnitine palmitoyltransferase II deficiency