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 AbstractIpsdienol dehydrogenase (IDOLDH): a novel oxidoreductase important for Ips pini pheromone production    Next AbstractExhaled volatile organic compounds in individuals with a history of high altitude pulmonary edema and varying hypoxia-induced responses »

J Biochem


Title:"High substrate specificity of ipsdienol dehydrogenase (IDOLDH), a short-chain dehydrogenase from Ips pini bark beetles"
Author(s):Figueroa-Teran R; Pak H; Blomquist GJ; Tittiger C;
Address:"Department of Biochemistry and Molecular Biology, University of Nevada, Reno, Reno, NV 89557, USA. Department of Biochemistry and Molecular Biology, University of Nevada, Reno, Reno, NV 89557, USA crt@unr.edu"
Journal Title:J Biochem
Year:2016
Volume:20160306
Issue:3
Page Number:141 - 151
DOI: 10.1093/jb/mvw019
ISSN/ISBN:1756-2651 (Electronic) 0021-924X (Print) 0021-924X (Linking)
Abstract:"Ips spp. bark beetles use ipsdienol, ipsenol, ipsdienone and ipsenone as aggregation pheromone components and pheromone precursors. For Ips pini, the short-chain oxidoreductase ipsdienol dehydrogenase (IDOLDH) converts (-)-ipsdienol to ipsdienone, and thus likely plays a role in determining pheromone composition. In order to further understand the role of IDOLDH in pheromone biosynthesis, we compared IDOLDH to its nearest functionally characterized ortholog with a solved structure: human L-3-hydroxyacyl-CoA dehydrogenase type II/ amyloid-beta binding alcohol dehydrogenase (hHADH II/ABAD), and conducted functional assays of recombinant IDOLDH to determine substrate and product ranges and structural characteristics. Although IDOLDH and hHADH II/ABAD had only 35% sequence identity, their predicted tertiary structures had high identity. We found IDOLDH is a functional homo-tetramer. In addition to oxidizing (-)-ipsdienol, IDOLDH readily converted racemic ipsenol to ipsenone, and stereo-specifically reduced both ketones to their corresponding (-)-alcohols. The (+)-enantiomers were never observed as products. Assays with various substrate analogs showed IDOLDH had high substrate specificity for (-)-ipsdienol, ipsenol, ipsenone and ipsdienone, supporting that IDOLDH functions as a pheromone-biosynthetic enzyme. These results suggest that different IDOLDH orthologs and or activity levels contribute to differences in Ips spp. pheromone composition"
Keywords:Acyclic Monoterpenes Animals Coleoptera/*enzymology/genetics/metabolism Humans Insect Proteins/*chemistry/genetics/metabolism Monoterpenes/*chemistry/metabolism Octanols/*chemistry/metabolism Oxidoreductases/*chemistry/genetics/metabolism Pheromones/chemi;
Notes:"MedlineFigueroa-Teran, Rubi Pak, Heidi Blomquist, Gary J Tittiger, Claus eng P20 GM103440/GM/NIGMS NIH HHS/ England 2016/03/10 J Biochem. 2016 Sep; 160(3):141-51. doi: 10.1093/jb/mvw019. Epub 2016 Mar 6"

 
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 27-12-2024