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

被引:0
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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]
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页码:814 / 816
页数:2
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