5thm | pdb_00005thm
Esterase-6 from Drosophila melanogaster
Structural highlights
FunctionEST6_DROME Transferred from the ejaculatory bulbs of males to the female genitals upon copulation, plays an important role in the reproductive biology. Publication Abstract from PubMedPrevious 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. See AlsoReferences
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