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}
}
Fatty acid synthase (FAS; EC 2.3.1.85) of animal tissues is a complex multifunctional enzyme consisting of two identical monomers. The FAS monomer (∼270 kDa) contains six catalytic activities and from the N-terminus the order is β-ketoacyl synthase (KS), acetyl/malonyl transacylase (AT/MT), β-hydroxyacyl dehydratase (DH), enoyl reductase (ER), β-ketoacyl reductase (KR), acyl carrier protein (ACP), and thioesterase (TE). Although the FAS monomer contains all the activities needed for palmitate… Expand
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It is found that kallikrein cleavage sites occur in the least conserved regions of the FAS polypeptide subunit, and the order of the component activities in domain I is confirmed, paving the way for successful expression and characterization of the remaining activities. Expand
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The current model for the animal FAS must be revised to reflect the finding that the two constituent polypeptides are not simply positioned side-by-side in a fully extended conformation but are coiled in a manner that allows the dehydrase domain to access the beta-hydroxyacyl-ACP located more than 1100 residues distant on the same subunit. Expand
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The animal fatty acid synthase comprises two multifunctional polypeptide chains, each containing seven discrete functional domains, juxtaposed head‐to‐tail such that two separate centers for fattyExpand
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