Structure and function of animal fatty acid synthase

@article{Chirala2004StructureAF,
  title={Structure and function of animal fatty acid synthase},
  author={Subrahmanyam S. Chirala and Salih J. Wakil},
  journal={Lipids},
  year={2004},
  volume={39},
  pages={1045-1053},
  url={https://api.semanticscholar.org/CorpusID:4043407}
}
Analysis of FAS particle images by using a simultaneous multiple model single particle refinement method confirmed that FAS structure exists in various conformational states and predicted that the intersubunit hinge region and the intrasubunit hinge located between domains II and III are highly flexible.
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51 References

Animal fatty acid synthase: functional mapping and cloning and expression of the domain I constituent activities.

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Human fatty acid synthase: assembling recombinant halves of the fatty acid synthase subunit protein reconstitutes enzyme activity.

The successful reconstitution of the human FAS activity from its domain I and domains II and III fully supports the model for the structure-function relationship of FAS in animal tissues.

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The results of this study reveal an unanticipated element of redundancy in the FAS reaction mechanism in that the amino-terminal KS and MAT domains can make functional contact with the penultimate carboxy-Terminal ACP domain of either subunit.

Human fatty acid synthase: Role of interdomain in the formation of catalytically active synthase dimer

It is shown that the fatty acid synthase activity could not be reconstituted when the ID sequences present in the two recombinant halves are deleted, suggesting that these ID sequences are essential for fatty Acid synthase dimer formation.

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The structure revealed the presence of a hydrophobic groove with a distal pocket at the interface of the two subdomains, which constitutes the candidate substrate binding site and is consistent with the high selectivity of the thioesterase for palmitoyl acyl substrate.

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All the partial activities of human FAS are comparable to those of other animal FASs, except for the beta-ketoacyl synthase, whose significantly lower activity is attributable to the low 4'-phosphopantetheine content of HepG2 FAS.

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