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

被引：0

作者：

Sarah M Barry

Johan A Kers

Evan G Johnson

Lijiang Song

Philip R Aston

Bhumit Patel

Stuart B Krasnoff

Brian R Crane

Donna M Gibson

Rosemary Loria

Gregory L Challis

机构：

[1] University of Warwick,Department of Chemistry

[2] Cornell University,Department of Plant Pathology and Plant

[3] Cornell University,Microbe Biology

[4] Agricultural Research Service,Department of Chemistry and Chemical Biology

[5] Robert W. Holley Center for Agriculture and Health,United States Department of Agriculture

[6] Present addresses: Department of Chemistry,undefined

[7] School of Biomedical Sciences,undefined

[8] King's College London,undefined

[9] London,undefined

[10] UK (S.M.B.); Industrial Products Division,undefined

[11] Intrexon Corporation,undefined

[12] San Carlos,undefined

[13] California,undefined

[14] USA (J.A.K.); Citrus Research and Education Center,undefined

[15] University of Florida,undefined

[16] Lake Alfred,undefined

[17] Florida,undefined

[18] USA (E.G.J.); Fraunhofer USA Center for Molecular Biotechnology,undefined

[19] Newark,undefined

[20] Delaware,undefined

[21] USA (B.P.); Plant Pathology Department,undefined

[22] University of Florida,undefined

[23] Gainesville,undefined

[24] Florida,undefined

[25] USA (R.L.).,undefined

来源：

Nature Chemical Biology | 2012年 / 8卷

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摘要：

The mechanism for nitro group formation in the thaxtomin family of natural products is unknown. Genetic and biochemical studies now show the cytochrome P450 TxtE catalyzes this direct and regioselective nitration, using NO and O2 to modify a tryptophan indole ring.[graphic not available: see fulltext]

引用

页码：814 / 816

页数：2

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