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Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila

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.
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Submitted on : Tuesday, May 9, 2017 - 2:35:15 PM
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Faisal Younus, Nicholas J. Fraser, Chris W. Coppin, Jian-Wei Liu, Galen J. Correy, et al.. Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila. Scientific Reports, Nature Publishing Group, 2017, 7, pp.46188. ⟨10.1038/srep46188⟩. ⟨hal-01519877⟩

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