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Membrane-bound phospholipid desaturases

  • Symposium: Polyunsaturated Fatty Acids and Their Metabolites
  • Published:
Lipids

Abstract

This review covers studies on membrane-bound phospholipid desaturases in yeast and rat liver carried out in this laboratory. In yeast the desaturase system was shown to effect the direct desaturation of dioleoyl-lecithin to dilinoleoyl-lecithin. In rat liver the desaturase was capable of converting 2-eicosatrienoyl-lecithin to 2-arachidonoyl-lecithin. Both systems required reduced pyridine nucleotides, O2 and cytochrome b5. Eicosatrienoyl-lecithin desaturase along with eicosatrienoyl-CoA desaturase of rat liver microsomes was solubilized with detergents and purified 7–8-fold from the microsomal pellets. Both activities were reconstituted in the presence of deoxycholate on addition of the other components of the cytochrome b5-electron transport chain (cytochrome b5 and NADH-cytochrome b5 reductase) to the solubilized desaturase; addition of lecithin further stimulated the activities. The demonstration of desaturation of eicosatrienoyl-lecithin by a solubilized and partially purified desaturase provides strong evidence for the direct desaturation of the lecithin substrate without prior conversion to the acyl-CoA thiolester.

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Authors and Affiliations

  1. Department of Biochemistry, University of Ottawa, K1N 6N5, Ottawa, Canada

    E. L. Pugh & M. Kates

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  1. E. L. Pugh
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  2. M. Kates
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Pugh, E.L., Kates, M. Membrane-bound phospholipid desaturases. Lipids 14, 159–165 (1979). https://doi.org/10.1007/BF02533867

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  • DOI: https://doi.org/10.1007/BF02533867

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