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 AbstractScreening organic repellent compounds against Lutzomyia longipalpis (Diptera: Psychodidae) present in plant essential oils: Bioassay plus an in silico approach    Next AbstractValidation of selected analytical methods using accuracy profiles to assess the impact of a Tobacco Heating System on indoor air quality »

Proc Natl Acad Sci U S A


Title:"Pheromone gland-specific fatty-acyl reductase of the silkmoth, Bombyx mori"
Author(s):Moto K; Yoshiga T; Yamamoto M; Takahashi S; Okano K; Ando T; Nakata T; Matsumoto S;
Address:"RIKEN, Hirosawa 2-1, Wako, Saitama 351-0198, Japan"
Journal Title:Proc Natl Acad Sci U S A
Year:2003
Volume:20030718
Issue:16
Page Number:9156 - 9161
DOI: 10.1073/pnas.1531993100
ISSN/ISBN:0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking)
Abstract:"The C10-C18 unsaturated, acyclic, aliphatic compounds that contain an oxygenated functional group (alcohol, aldehyde, or acetate ester) are a major class of sex pheromones produced by female moths. In the biosynthesis of these pheromone components, the key enzyme required to produce the oxygenated functional groups is fatty-acyl reductase (FAR). This enzyme converts fatty-acyl pheromone precursors to their corresponding alcohols, which, depending on the moth species, can then be acetylated or oxidized to the corresponding aldehydes. Despite the significant role this enzyme has in generating the species-specific oxygenated constituents of lepidopteran sex pheromones, the enzyme has yet to be fully characterized and identified. In experiments designed to characterize a pheromone-gland-specific FAR in the silkmoth, Bombyx mori, we have isolated a cDNA clone encoding a protein homologous to a FAR from the desert shrub, Simmondsia chinensis, commonly known as jojoba. The deduced amino acid sequence of this clone predicts a 460-aa protein with a consensus NAD(P)H binding motif within the amino terminus. Northern blot analysis indicated that 2-kb transcripts of this gene were specifically expressed in the pheromone gland at 1 day before adult eclosion. Functional expression of this gene in the yeast Saccharomyces cerevisiae not only confirmed the long-chain FAR activity, but also indicated a distinct substrate specificity. Finally, the transformed yeast cells evoked typical mating behavior in male moths when cultured with the pheromone precursor fatty acid, (E,Z)-10,12-hexadecadienoic acid"
Keywords:"Alcohols/metabolism Aldehyde Oxidoreductases/*chemistry Amino Acid Motifs Amino Acid Sequence Animals Base Sequence Blotting, Northern Bombyx Cloning, Molecular DNA, Complementary/metabolism Female Gas Chromatography-Mass Spectrometry Male Molecular Seque;"
Notes:"MedlineMoto, Ken'ichi Yoshiga, Toyoshi Yamamoto, Masanobu Takahashi, Shunya Okano, Kazuhiro Ando, Tetsu Nakata, Tadashi Matsumoto, Shogo eng Research Support, Non-U.S. Gov't 2003/07/23 Proc Natl Acad Sci U S A. 2003 Aug 5; 100(16):9156-61. doi: 10.1073/pnas.1531993100. Epub 2003 Jul 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 26-12-2024