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 AbstractCYPs in different families are involved in the divergent regio-specific epoxidation of alkenyl sex pheromone precursors in moths    Next AbstractGenomics of Aspergillus fumigatus »

Insect Biochem Mol Biol


Title:"Functional characterization of the epoxidase gene, Li_epo1 (CYP341B14), involved in generation of epoxyalkene pheromones in the mulberry tiger moth Lemyra imparilis"
Author(s):Rong Y; Fujii T; Naka H; Yamamoto M; Ishikawa Y;
Address:"Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, 113-8657, Japan. Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, 113-8657, Japan. Electronic address: takeshi.f0405@gmail.com. Faculty of Agriculture, Tottori University, Koyama Minami, Tottori, 680-8550, Japan"
Journal Title:Insect Biochem Mol Biol
Year:2019
Volume:20190208
Issue:
Page Number:46 - 52
DOI: 10.1016/j.ibmb.2019.02.001
ISSN/ISBN:1879-0240 (Electronic) 0965-1748 (Linking)
Abstract:"Epoxidation of alkenes derived from essential fatty acids is a key step in the biosynthesis of sex pheromones in moth species that utilize alkenyl sex pheromones. The position of the epoxy ring in the pheromone molecule differs depending on the species, thereby conferring diversities on sex pheromones. To date, only one pheromone gland (PG)-specific epoxidase, Hc_epo1 (CYP341B14), has been reported. Hc_epo1, which was identified from an arctiid moth Hyphantria cunea, catalyzes the epoxidation of a double bond at position 9 of the triene, Z3,Z6,Z9-21:H. In the present study, we investigated the PG-specific epoxidase from another arctiid, the mulberry tiger moth Lemyra imparilis, in order to verify whether cytochrome P450 in the CYP341B subfamily, to which Hc_epo1 belongs to, is responsible for the epoxidation of pheromone precursors at position 9 in moths other than H. cunea. A fragment of the Hc_epo1 homolog was amplified from cDNA prepared from the PG of L. imparilis by PCR with degenerate primers. The deduced amino acid sequence of the subsequently cloned homolog, Li_epo1, showed 88.5% identity to Hc_epo1. A functional assay using the Sf9 insect cell line-baculovirus expression system showed that Li_epo1 exhibited epoxidase activity with high selectivity to the double bond at position 9 of two trienes, Z3,Z6,Z9-21:H and Z3,Z6,Z9-23:H, precursors of epoxy diene sex pheromone components in L. imparilis"
Keywords:"Animals Insect Proteins/chemistry/*genetics/metabolism Larva/genetics/growth & development/metabolism Moths/*genetics/growth & development/metabolism Oxidoreductases/chemistry/*genetics/metabolism Sequence Homology, Amino Acid Cyp Cytochrome P450 Epoxidas;"
Notes:"MedlineRong, Yu Fujii, Takeshi Naka, Hideshi Yamamoto, Masanobu Ishikawa, Yukio eng Research Support, Non-U.S. Gov't England 2019/02/12 Insect Biochem Mol Biol. 2019 Apr; 107:46-52. doi: 10.1016/j.ibmb.2019.02.001. Epub 2019 Feb 8"

 
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 29-06-2024