Structural and functional divergence of insect CYP6B proteins: From specialist to generalist cytochrome P450
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- Xianchun Li
- Department of Entomology, School of Chemical Sciences, and Department of Cell and Structural Biology, University of Illinois, Urbana, IL 61801; and Department of Plant Protection, Nanjing Agricultural University, Nanjing 210095, People's Republic of China
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- Jerome Baudry
- Department of Entomology, School of Chemical Sciences, and Department of Cell and Structural Biology, University of Illinois, Urbana, IL 61801; and Department of Plant Protection, Nanjing Agricultural University, Nanjing 210095, People's Republic of China
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- May R. Berenbaum
- Department of Entomology, School of Chemical Sciences, and Department of Cell and Structural Biology, University of Illinois, Urbana, IL 61801; and Department of Plant Protection, Nanjing Agricultural University, Nanjing 210095, People's Republic of China
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- Mary A. Schuler
- Department of Entomology, School of Chemical Sciences, and Department of Cell and Structural Biology, University of Illinois, Urbana, IL 61801; and Department of Plant Protection, Nanjing Agricultural University, Nanjing 210095, People's Republic of China
書誌事項
- 公開日
- 2004-02-23
- DOI
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- 10.1073/pnas.0308691101
- 公開者
- Proceedings of the National Academy of Sciences
この論文をさがす
説明
<jats:p> How polyphagous herbivores cope with the diversity and unpredictability of plant defenses remains largely unknown at both the genetic and molecular levels. To examine whether generalist counterdefense enzymes are structurally more flexible and functionally more diverse, two counterdefensive allelochemical-metabolizing cytochrome P450 proteins, CYP6B1 from the specialist <jats:italic>Papilio polyxenes</jats:italic> , feeding on furanocoumarin-containing plants, and CYP6B8 from the generalist <jats:italic>Helicoverpa zea</jats:italic> , feeding on hundreds of host plant species, are compared structurally and functionally. Molecular modeling indicates that CYP6B8 has more flexible overall folding, a more elastic catalytic pocket, and one more substrate access channel than CYP6B1. Baculovirus-mediated expression of the CYP6B8 and CYP6B1 proteins demonstrates that CYP6B8 metabolizes six biosynthetically diverse plant allelochemicals (xanthotoxin, quercetin, flavone, chlorogenic acid, indole-3-carbinol, and rutin) and three insecticides (diazinon, cypermethrin, and aldrin), whereas CYP6B1 metabolizes only two allelochemicals (xanthotoxin and flavone) and one insecticide (diazinon) of those tested. These results indicate that generalist counterdefense proteins are capable of accepting a more structurally diverse array of compounds compared with specialist counterdefense proteins. </jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 101 (9), 2939-2944, 2004-02-23
Proceedings of the National Academy of Sciences