Membranes as acceptors for palmitoyl CoA in fatty acid biosynthesis

@article{Sumper1973MembranesAA,
  title={Membranes as acceptors for palmitoyl CoA in fatty acid biosynthesis},
  author={Manfred Sumper and Hermann Tr{\"a}uble},
  journal={FEBS Letters},
  year={1973},
  volume={30}
}
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Control of fatty-acid biosynthesis by long-chain acyl CoAs and by lipid membranes.
  • M. Sumper
  • Biology, Chemistry
    European journal of biochemistry
  • 1974
TLDR
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.
Chapter 3 Genetics of fatty acid biosynthesis in yeast
An appraisal of the functional significance of the inhibitory effect of long chain acyl‐CoAs on mitochondrial transports
A hypothesis on membranous proteins specialized in lateral transport
Fatty acid synthetase activity in Mycobacterium smegmatis. Characterization of the acyl carrier protein-dependent elongating system.
Effects of phosphatidylcholine liposomes on the fatty acid synthetase complex from Mycobacterium smegmatis.
Interaction of the fluorescent analogue palmitoyl-(1,N6) etheno-CoA with mitochondrial malate dehydrogenase and phospholipid vesicles.
Depletion of acyl-coenzyme A-binding protein affects sphingolipid synthesis and causes vesicle accumulation and membrane defects in Saccharomyces cerevisiae.
TLDR
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.
Inhibitory effects of long‐chain acyl coenzyme a analogues on rat liver acetyl coenzyme a carboxylase
Properties of microsomal acyl coenzyme A reductase in mouse preputial glands.
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References

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TLDR
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