PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9718682-5	1998	Binding in the active site of JHE is promoted by structural features found in JHIII and JHB3 including the epoxide groups in their natural orientations, methyl (rather than ethyl) side-chains, and the 2E, 3 double bond that is conjugated with the ester group.	Esters	247-252	Juvenile hormone esterase	Drosophila melanogaster	30-33	
30611903-5	2019	Our biochemical comparisons further show that DmJHE has sufficient substrate promiscuity and activity against odorant esters for a duplicate to evolve a general ODE function against a range of mid-long chain food esters, as is shown in DmJHEdup.	Esters	118-124	Juvenile hormone esterase	Drosophila melanogaster	46-51	
30611903-5	2019	Our biochemical comparisons further show that DmJHE has sufficient substrate promiscuity and activity against odorant esters for a duplicate to evolve a general ODE function against a range of mid-long chain food esters, as is shown in DmJHEdup.	Esters	213-219	Juvenile hormone esterase	Drosophila melanogaster	46-51	
28974761-2	2017	A carboxylesterase, specifically expressed in Drosophila antennae, called "juvenile hormone esterase duplication (JHEdup)" has been previously reported to hydrolyse different fruit esters in vitro.	Esters	181-187	Juvenile hormone esterase	Drosophila melanogaster	75-100