Algal neurotoxin biosynthesis repurposes the terpene cyclase structural fold into an N-prenyltransferase
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Algal neurotoxin biosynthesis repurposes the terpene cyclase structural fold into an N-prenyltransferase

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  • Journal Title:
    Proceedings of the National Academy of Sciences (PNAS)
  • Personal Author:
  • NOAA Program & Office:
    NOS (National Ocean Service)
  • Description:
    Prenylation is a common biological reaction in all domains of lifewherein prenyl diphosphate donors transfer prenyl groups ontosmall molecules as well as large proteins. The enzymes thatcatalyze these reactions are structurally distinct from ubiquitousterpene cyclases that, instead, assemble terpenes via intramolec-ular rearrangements of a single substrate. Herein, we report thestructure and molecular details of a new family of prenyltrans-ferases from marine algae that repurposes the terpene cyclasestructural fold for theN-prenylation of glutamic acid during thebiosynthesis of the potent neurochemicals domoic acid and kainicacid. We solved the X-ray crystal structure of the prenyltransferasefound in domoic acid biosynthesis, DabA, and show distinct activesite binding modifications that remodel the canonical magnesium(Mg2+)-binding motif found in terpene cyclases. We then appliedour structural knowledge of DabA and a homologous enzymefrom the kainic acid biosynthetic pathway, KabA, to reengineertheir isoprene donor specificities (geranyl diphosphate [GPP] ver-sus dimethylallyl diphosphate [DMAPP]) with a single amino acidchange. While diatom DabA and seaweed KabA enzymes share acommon evolutionary lineage, they are distinct from all other ter-pene cyclases, suggesting a very distant ancestor to the largerterpene synthase family.
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  • Source:
    Proceedings of the National Academy of Sciences (PNAS), 117(23) 1-7
  • DOI:
  • Pubmed Central ID:
    PMC7293706
  • Document Type:
    Journal Article
  • Funding:
    Grant no. NA19NOS4780181
  • Rights Information:
    Other
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    Submitted
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