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Literature summary extracted from

  • Li, Z.; Zhai, Y.; Fang, J.; Zhou, Q.; Geng, Y.; Sun, F.
    Purification, crystallization and preliminary crystallographic analysis of very-long-chain acyl-CoA dehydrogenase from Caenorhabditis elegans (2010), Acta Crystallogr. Sect. F, 66, 426-430.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.8.8 expression in Escherichia coli strain BL21(DE3) Caenorhabditis elegans
1.3.8.9 cloning from cDNA library, His8-tagged VLCAD expression in Escherichia coli strain BL21 (DE3) Caenorhabditis elegans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.8.8 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 Caenorhabditis elegans
1.3.8.9 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 Caenorhabditis elegans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.8.8 mitochondrion
-
 Caenorhabditis elegans 5739
-
1.3.8.9 mitochondrion
-
 Caenorhabditis elegans 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.8.9 180000
-
 about, size-exclusion chromatography coupled with in-line static light-scattering, refractive-index and ultraviolet measurements Caenorhabditis elegans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.8.9 additional information Caenorhabditis elegans acyl-CoA dehydrogenases, ACADs, constitute a family of FAD-dependent flavoproteins that catalyze the alpha,beta-dehydrogenation of thioester substrates ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.8 Caenorhabditis elegans
-
-
-
1.3.8.9 Caenorhabditis elegans
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.8.8 recombinant enzyme from Escherichia coli strain BL21(DE3) Caenorhabditis elegans
1.3.8.9 recombinant His8-tagged VLCAD from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography, anion exchange chromatography, and gel filtration Caenorhabditis elegans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.8.9 additional information acyl-CoA dehydrogenases, ACADs, constitute a family of FAD-dependent flavoproteins that catalyze the alpha,beta-dehydrogenation of thioester substrates Caenorhabditis elegans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.8.8 tetramer
-
 Caenorhabditis elegans
1.3.8.9 tetramer 4 x 45000, about, size-exclusion chromatography coupled with in-line static light-scattering, refractive-index and ultraviolet measurements Caenorhabditis elegans

Synonyms

EC Number Synonyms Comment Organism
1.3.8.8 LCAD
-
 Caenorhabditis elegans
1.3.8.9 acyl-CoA:(acceptor) 2,3-oxidoreductase
-
 Caenorhabditis elegans
1.3.8.9 very-long-chain acyl-CoA dehydrogenase
-
 Caenorhabditis elegans
1.3.8.9 VLCAD
-
 Caenorhabditis elegans

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.8.8 FAD
-
 Caenorhabditis elegans
1.3.8.9 FAD
-
 Caenorhabditis elegans

General Information

EC Number General Information Comment Organism
1.3.8.7 metabolism acyl-CoA dehydrogenase catalyzes the first reaction step in mitochondrial fatty-acid beta-oxidation Caenorhabditis elegans
1.3.8.8 evolution the enzyme belongs to the acyl-CoA dehydrogenases family of FAD-dependent flavoproteins that catalyze the alpha,beta-dehydrogenation of thioester substrates Caenorhabditis elegans
1.3.8.8 physiological function the enzyme is involved in the initial step of the mitochondrial beta-oxidation spiral, ACADs catalyze the dehydrogenation of acyl-CoAs with the formation of a trans double bond between the Calpha and Cbeta atoms Caenorhabditis elegans