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Literature summary for 1.3.8.8 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
Search for more literature for 1.3.8.8

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain BL21(DE3) Caenorhabditis elegans

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Caenorhabditis elegans 5739
-

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) Caenorhabditis elegans

Subunits

Subunits Comment Organism
tetramer
-
 Caenorhabditis elegans

Synonyms

Synonyms Comment Organism
LCAD
-
 Caenorhabditis elegans

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Caenorhabditis elegans

General Information

General Information Comment Organism
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
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