PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10704209-1	2000	Previous work has demonstrated that the ferric form of soybean lipoxygenase-1 will catalyze an elimination reaction on 12-iodo-cis-9-octadecenoic acid (12-IODE) to produce 9, 11-octadecadienoic acid and iodide ion.	Ferric enterobactin ion	40-46	linoleate 9S-lipoxygenase-4	Glycine max	63-75	
1315759-1	1992	One proposed mechanism of the inactivation of lipoxygenase by inhibitors is the reduction of the catalytically active ferric form of the enzyme to its ferrous form.	Ferric enterobactin ion	118-124	linoleate 9S-lipoxygenase-4	Glycine max	46-58	
7819206-1	1995	The ferric form of soybean lipoxygenase catalyzes an elimination reaction on 12-iodo-cis-9-octadecenoic acid (12-IODE) to produce iodide ions and 9,11-octadecadienoic acid (9, 11-ODA).	Ferric enterobactin ion	4-10	linoleate 9S-lipoxygenase-4	Glycine max	27-39	
1850741-5	1991	This brings to (at least) five the number of classes of lipoxygenase inhibitors that are capable of reducing the active-site ferric ion and suggests the generality of this approach in the rational design of lipoxygenase inhibitors.	Ferric enterobactin ion	125-131	linoleate 9S-lipoxygenase-4	Glycine max	56-68	
1850741-5	1991	This brings to (at least) five the number of classes of lipoxygenase inhibitors that are capable of reducing the active-site ferric ion and suggests the generality of this approach in the rational design of lipoxygenase inhibitors.	Ferric enterobactin ion	125-131	linoleate 9S-lipoxygenase-4	Glycine max	207-219