Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractDiagnosis of aged prescribed burning plumes impacting an urban area    Next AbstractAge matters: the effects of volatile organic compounds emitted by Trichoderma atroviride on plant growth »

Proc Natl Acad Sci U S A


Title:Herbivore-induced and floral homoterpene volatiles are biosynthesized by a single P450 enzyme (CYP82G1) in Arabidopsis
Author(s):Lee S; Badieyan S; Bevan DR; Herde M; Gatz C; Tholl D;
Address:"Department of Biological Sciences, Virginia Tech, Blacksburg, VA 24061, USA"
Journal Title:Proc Natl Acad Sci U S A
Year:2010
Volume:20101118
Issue:49
Page Number:21205 - 21210
DOI: 10.1073/pnas.1009975107
ISSN/ISBN:1091-6490 (Electronic) 0027-8424 (Print) 0027-8424 (Linking)
Abstract:"Terpene volatiles play important roles in plant-organism interactions as attractants of pollinators or as defense compounds against herbivores. Among the most common plant volatiles are homoterpenes, which are often emitted from night-scented flowers and from aerial tissues upon herbivore attack. Homoterpene volatiles released from herbivore-damaged tissue are thought to contribute to indirect plant defense by attracting natural enemies of pests. Moreover, homoterpenes have been demonstrated to induce defensive responses in plant-plant interaction. Although early steps in the biosynthesis of homoterpenes have been elucidated, the identity of the enzyme responsible for the direct formation of these volatiles has remained unknown. Here, we demonstrate that CYP82G1 (At3g25180), a cytochrome P450 monooxygenase of the Arabidopsis CYP82 family, is responsible for the breakdown of the C(20)-precursor (E,E)-geranyllinalool to the insect-induced C(16)-homoterpene (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT). Recombinant CYP82G1 shows narrow substrate specificity for (E,E)-geranyllinalool and its C(15)-analog (E)-nerolidol, which is converted to the respective C(11)-homoterpene (E)-4,8-dimethyl-1,3,7-nonatriene (DMNT). Homology-based modeling and substrate docking support an oxidative bond cleavage of the alcohol substrate via syn-elimination of the polar head, together with an allylic C-5 hydrogen atom. CYP82G1 is constitutively expressed in Arabidopsis stems and inflorescences and shows highly coordinated herbivore-induced expression with geranyllinalool synthase in leaves depending on the F-box protein COI-1. CYP82G1 represents a unique characterized enzyme in the plant CYP82 family with a function as a DMNT/TMTT homoterpene synthase"
Keywords:Animals Arabidopsis Proteins/*metabolism Cytochrome P-450 Enzyme System/*metabolism Flowers/chemistry Insecta Substrate Specificity Terpenes/*metabolism Transcriptional Activation Volatile Organic Compounds/*metabolism;
Notes:"MedlineLee, Sungbeom Badieyan, Somayesadat Bevan, David R Herde, Marco Gatz, Christiane Tholl, Dorothea eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. 2010/11/23 Proc Natl Acad Sci U S A. 2010 Dec 7; 107(49):21205-10. doi: 10.1073/pnas.1009975107. Epub 2010 Nov 18"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 05-12-2024