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

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

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
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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
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VLCAD is a rate-limiting enzyme in fatty acid beta-oxidation and is regulated by phosphorylation at Ser586
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
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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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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
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
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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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