5thm

Publication Abstract from PubMed

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.

Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila.,Younus F, Fraser NJ, Coppin CW, Liu JW, Correy GJ, Chertemps T, Pandey G, Maibeche M, Jackson CJ, Oakeshott JG Sci Rep. 2017 Apr 10;7:46188. doi: 10.1038/srep46188. PMID:28393888^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.