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« Previous Abstract"Degradation of pheromone and plant volatile components by a same odorant-degrading enzyme in the cotton leafworm, Spodoptera littoralis"    Next AbstractNeuroligin 1 expression is linked to plasticity of behavioral and neuronal responses to sex pheromone in the male moth Agrotis ipsilon »

Commun Integr Biol


Title:"Antennal carboxylesterases in a moth, structural and functional diversity"
Author(s):Durand N; Chertemps T; Maibeche-Coisne M;
Address:
Journal Title:Commun Integr Biol
Year:2012
Volume:5
Issue:3
Page Number:284 - 286
DOI: 10.4161/cib.19701
ISSN/ISBN:1942-0889 (Electronic) 1942-0889 (Linking)
Abstract:"Pheromone-degrading enzymes (PDEs) are supposed to be involved in the signal inactivation step within the olfactory sensilla of insects by quickly degrading pheromone molecules. Because esters are widespread insect pheromone components, PDEs belonging to the carboxylesterase (CCE) family have been the most studied. However, only two CCEs were both identified at the molecular level and functionally characterized as PDEs until recently. In the pest moth Spodoptera littoralis, we have identified an unsuspected diversity of antennal CCEs, with a total number of 30 genes. Two CCEs, enriched in antennae and belonging to distinct clades, were shown to present different substrate specificities toward pheromone and plant compounds. A same CCE was also shown to efficiently degrade both pheromone and plant components. Our results suggest that the structural evolution of antennal CCEs reflects their functional diversity and that a complex set of CCE-mediated reactions take place is the olfactory organs of moths"
Keywords:carboxylesterase lepidoptera noctuidae odorant-degrading enzymes olfaction pheromone;
Notes:"PubMed-not-MEDLINEDurand, Nicolas Chertemps, Thomas Maibeche-Coisne, Martine eng 2012/08/17 Commun Integr Biol. 2012 May 1; 5(3):284-6. doi: 10.4161/cib.19701"

 
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