• Author/Authors

    Weiping Le، نويسنده , , Azfar S. Abbas، نويسنده , , Howard Sprecher، نويسنده , , Jerry Vockley، نويسنده , , Horst Schulz، نويسنده ,

  • DocumentNumber
    1601599
  • Title Of Article

    Long-chain acyl-CoA dehydrogenase is a key enzyme in the mitochondrial β-oxidation of unsaturated fatty acids

  • شماره ركورد
    12226
  • Latin Abstract
    The first reaction of mitochondrial β-oxidation, which is catalyzed by acyl-CoA dehydrogenases, was studied with unsaturated fatty acids that have a double bond either at the 4,5 or 5,6 position. The CoA thioesters of docosahexaenoic acid, arachidonic acid, 4,7,10-cis-hexadecatrienoic acid, 5-cis-tetradecenoic acid, and 4-cis-decenoic acid were effectively dehydrogenated by both rat and human long-chain acyl-CoA dehydrogenases (LCAD), whereas they were poor substrates of very long-chain acyl-CoA dehydrogenases (VLCAD). VLCAD, however, was active with CoA derivatives of long-chain saturated fatty acids or unsaturated fatty acids that have double bonds further removed from the thioester function. Although bovine LCAD effectively dehydrogenated 5-cis-tetradecenoyl-CoA (14:1) and 4,7,10-cis-hexadecatrienoyl-CoA, it was nearly inactive toward the other unsaturated substrates. The catalytic efficiency of rat VLCAD with 14:1 as substrate was only 4% of the efficiency determined with tetradecanoyl-CoA, whereas LCAD acted equally well on both substrates. The conclusion of this study is that LCAD serves an important, if not essential function in the β-oxidation of unsaturated fatty acids.
  • From Page
    121
  • NaturalLanguageKeyword
    L-Oxidation , Unsaturated fatty acid , Long-chain acyl-CoA dehydrogenase , Very long-chain acyl-CoA dehydrogenase
  • JournalTitle
    Studia Iranica
  • To Page
    128
  • To Page
    128