Membranes as acceptors for palmitoyl CoA in fatty acid biosynthesis

  title={Membranes as acceptors for palmitoyl CoA in fatty acid biosynthesis},
  author={Manfred Sumper and Hermann Tr{\"a}uble},
  journal={FEBS Letters},
Control of fatty-acid biosynthesis by long-chain acyl CoAs and by lipid membranes.
  • M. Sumper
  • Biology, Chemistry
    European journal of biochemistry
  • 1974
It was shown that palmitoyl-CoA can be transferred from the fatty acid synthetase into natural membranes or into lipid bilayers, and it was suggested that the effects of inositol deficiency in vivo (overproduction of lipids) and the shift to shorter chain lengths of the fatty acids synthesized under anaerobic conditions are discussed and interpreted.
Depletion of acyl-coenzyme A-binding protein affects sphingolipid synthesis and causes vesicle accumulation and membrane defects in Saccharomyces cerevisiae.
The present results strongly suggest that Acb1p plays an important role in fatty acid elongation and membrane assembly and organization and is not required for general glycerolipid synthesis.
Properties of microsomal acyl coenzyme A reductase in mouse preputial glands.


The inhibition of the fatty acid synthetase multienzyme complex of yeast by long-chain acyl coenzyme A compounds.
Results support the hypothesis put forth earlier that the end products of the fatty acid synthetase are bound preferentially in the region of the thiol group which is part of the acyl-carrier-protein portion of the complex.
Lateral diffusion in spin-labeled phosphatidylcholine multilayers.
A study of the rate of lateral diffusion of a spin-labeled lipid in a phospholipid bilayer system finds that the bilayer appears to have the combined properties of a fluid and a rigid structure, which suggests that the lateral translation of molecules bound to membranes may sometimes have biological significance.