4.8 Article

Cytochrome P450-catalyzed L-tryptophan nitration in thaxtomin phytotoxin biosynthesis

Journal

NATURE CHEMICAL BIOLOGY
Volume 8, Issue 10, Pages 814-816

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.1048

Keywords

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Funding

  1. UK Biotechnology and Biological Sciences Research Council [BB/H006281/1]
  2. National Research Initiative of the United States Department of Agriculture Cooperative State Research, Education and Extension Service [2008-35319-19202]
  3. Advantage West Midlands
  4. European Regional Development Fund
  5. BBSRC [BB/H006281/1, BB/H006265/1] Funding Source: UKRI
  6. Biotechnology and Biological Sciences Research Council [BB/H006265/1, BB/H006281/1] Funding Source: researchfish

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Thaxtomin phytotoxins produced by plant-pathogenic Streptomyces species contain a nitro group that is essential for phytotoxicity. The N,N'-dimethyldiketopiperazine core of thaxtomins is assembled from L-phenylalanine and L-4-nitrotryptophan by a nonribosomal peptide synthetase, and nitric oxide synthase-generated NO is incorporated into the nitro group, but the biosynthesis of the nonproteinogenic amino acid L-4-nitrotryptophan is unclear. Here we report that TxtE, a unique cytochrome P450, catalyzes L-tryptophan nitration using NO and O-2.

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