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The role of tandem acyl carrier protein domains in polyunsaturated fatty acid biosynthesis

Academic Article
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Overview

authors

  • Jiang, H.
  • Zirkle, R.
  • Metz, J. G.
  • Braun, L.
  • Richter, L.
  • Van Lanen, S. G.
  • Shen, Ben

publication date

  • May 2008

journal

  • Journal of the American Chemical Society  Journal

abstract

  • Acyl carrier protein (ACP) plays an essential role in fatty acid and polyketide biosynthesis, and most of the fatty acid synthases (FASs) and polyketide synthases (PKSs) known to date are characterized with a single ACP for each cycle of chain elongation. Polyunsaturated fatty acid (PUFA) biosynthesis is catalyzed by the PUFA synthase, and all PUFA synthases known to date contain tandem ACPs (ranging from 5 to 9). Using the Pfa PUFA synthase from Shewanella japonica as a model system, we report here that these tandem ACPs are functionally equivalent regardless of their physical location within the PUFA synthase subunit, but the total number of ACPs controls the overall PUFA titer. These findings set the stage to interrogate other domains and subunits of PUFA synthase for their roles in controlling the final PUFA products and could potentially be exploited to improve PUFA production.

subject areas

  • Acyl Carrier Protein
  • Docosahexaenoic Acids
  • Eicosapentaenoic Acid
  • Escherichia coli
  • Fatty Acid Synthase, Type II
  • Fatty Acids, Unsaturated
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Shewanella
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Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja801911t

PubMed ID

  • 18444614
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Additional Document Info

start page

  • 6336

end page

  • 6337

volume

  • 130

issue

  • 20

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