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Cytochrome P450–catalyzed L-tryptophan nitration in thaxtomin phytotoxin biosynthesis
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Barry, Sarah M., Kers, Johan A, Johnson, Evan G, Song, Lijiang, Aston, Philip R. , Patel, Bhumit, Krasnoff, Stuart B, Crane, Brian R, Gibson, Donna M, Loria, Rosemary and Challis, Gregory L.. (2012) Cytochrome P450–catalyzed L-tryptophan nitration in thaxtomin phytotoxin biosynthesis. Nature Chemical Biology, Vol. 8 (No.10). pp. 814-816. ISSN 1552-4450
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Official URL: http://dx.doi.org/10.1038/nchembio.1048
Abstract
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 O2.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > Q Science (General) Q Science > QD Chemistry Q Science > QR Microbiology |
| Divisions: | Faculty of Science > Chemistry |
| Journal or Publication Title: | Nature Chemical Biology |
| Publisher: | Nature Publishing Group |
| ISSN: | 1552-4450 |
| Date: | 2 September 2012 |
| Volume: | Vol. 8 |
| Number: | No.10 |
| Page Range: | pp. 814-816 |
| Identification Number: | 10.1038/nchembio.1048 |
| Status: | Peer Reviewed |
| Publication Status: | Published |
| Access rights to Published version: | Restricted or Subscription Access |
| URI: | http://wrap.warwick.ac.uk/id/eprint/50374 |
Data sourced from Thomson Reuters' Web of Knowledge
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