1. Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila
- Author
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Jian-Wei Liu, John G. Oakeshott, Colin J. Jackson, Faisal Younus, Chris W. Coppin, Nicholas J. Fraser, Gunjan Pandey, Thomas Chertemps, Galen J. Correy, Martine Maïbèche, Research School of Chemistry, Australian National University (ANU), CSIRO - Land & Water National Research Flagship, Institut d'écologie et des sciences de l'environnement de Paris (IEES), Centre National de la Recherche Scientifique (CNRS)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Recherche Agronomique (INRA), Institut d'écologie et des sciences de l'environnement de Paris (iEES), and Institut National de la Recherche Agronomique (INRA)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS)
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Arthropod Antennae ,Models, Molecular ,0301 basic medicine ,Cell type ,Biology ,Receptors, Odorant ,Esterase ,Article ,Carboxylesterase ,Substrate Specificity ,03 medical and health sciences ,Catalytic Domain ,Hydrolase ,Animals ,Drosophila Proteins ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Drosophila ,chemistry.chemical_classification ,Multidisciplinary ,Behavior, Animal ,Binding protein ,biology.organism_classification ,Kinetics ,Drosophila melanogaster ,030104 developmental biology ,Enzyme ,Biochemistry ,chemistry ,Structural Homology, Protein ,Odorants ,Olfactory Sensilla ,Pheromone - Abstract
Previous electrophysiological and behavioural studies implicate esterase 6 in the processing of the pheromone cis-vaccenyl acetate and various food odorants that affect aggregation and reproductive behaviours. Here we show esterase 6 has relatively high activity against many of the short-mid chain food esters, but negligible activity against cis-vaccenyl acetate. The crystal structure of esterase 6 confirms its substrate-binding site can accommodate many short-mid chain food esters but not cis-vaccenyl acetate. Immunohistochemical assays show esterase 6 is expressed in non-neuronal cells in the third antennal segment that could be accessory or epidermal cells surrounding numerous olfactory sensilla, including basiconics involved in food odorant detection. Esterase 6 is also produced in trichoid sensilla, but not in the same cell types as the cis-vaccenyl acetate binding protein LUSH. Our data support a model in which esterase 6 acts as a direct odorant degrading enzyme for many bioactive food esters, but not cis-vaccenyl acetate.
- Published
- 2017
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