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 Abstract"Female sex pheromone of a lichen moth Eilema japonica (Arctiidae, Lithosiinae): components and control of production"    Next Abstract"Discovery of a disused desaturase gene from the pheromone gland of the moth Ascotis selenaria, which secretes an epoxyalkenyl sex pheromone" »

Insect Biochem Mol Biol


Title:Molecular and functional characterization of an acetyl-CoA acetyltransferase from the adzuki bean borer moth Ostrinia scapulalis (Lepidoptera: Crambidae)
Author(s):Fujii T; Ito K; Katsuma S; Nakano R; Shimada T; Ishikawa Y;
Address:"Laboratory of Applied Entomology, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan. pippi.boo@gmail.com"
Journal Title:Insect Biochem Mol Biol
Year:2010
Volume:20100101
Issue:1
Page Number:74 - 78
DOI: 10.1016/j.ibmb.2009.12.012
ISSN/ISBN:1879-0240 (Electronic) 0965-1748 (Linking)
Abstract:"Two types of thiolases are involved in the synthesis and catabolism of fatty acids; acetyl-CoA acetyltransferase (AT) which catalyzes the formation of acetoacetyl-CoA from acetyl-CoA by transferring an acetyl group from one acetyl-CoA molecule to another, and 3-ketoacyl-CoA thiolase which catalyzes a reversible thiolytic cleavage of 3-ketoacyl-CoA into acetyl-CoA and acyl-CoA. Although many mammalian thiolases have been characterized in detail, no thiolases from insects have been functionally characterized to date. Here we report first characterization of an insect AT gene, Osat1, from the pheromone gland of the adzuki bean borer moth Ostrinia scapulalis (Lepidoptera; Crambidae). Osat1 encodes a 41.2 kDa protein comprising 396 amino acid residues (OsAT1), which possesses structural features of the thiolase family. An Osat1 homologue of Bombyx mori (Bmat1) was cloned through exploration of an EST library of the silkworm. Subsequent survey of the genome database revealed that B. mori has at least six Osat1 homologues, among which Bmat1 was most closely related to Osat1. We expressed recombinant OsAT1 using a baculovirus expression system, and verified that OsAT1 catalyzes the formation of acetoacetyl-CoA from acetyl-CoA. Osat1 was expressed in all adult tissues examined. These results indicate that OsAT1 is a functional AT ubiquitously expressed in O. scapulalis tissues"
Keywords:"Acetyl-CoA C-Acetyltransferase/chemistry/*genetics/*metabolism Amino Acid Sequence Animals Base Sequence Cell Line Cloning, Molecular Female Gene Expression Regulation, Enzymologic Insect Proteins/chemistry/*genetics/*metabolism Insecta/chemistry/classifi;"
Notes:"MedlineFujii, Takeshi Ito, Katsuhiko Katsuma, Susumu Nakano, Ryo Shimada, Toru Ishikawa, Yukio eng Research Support, Non-U.S. Gov't England 2010/01/02 Insect Biochem Mol Biol. 2010 Jan; 40(1):74-8. doi: 10.1016/j.ibmb.2009.12.012. Epub 2010 Jan 1"

 
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 22-11-2024