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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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