PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3138991-1	1988	Since H2O2 is one of the major biologically available peroxides, its ability to support hydroperoxidase activity of highly purified soybean lipoxygenase was examined by monitoring co-oxidation of selected xenobiotics.	Peroxides	54-63	linoleate 9S-lipoxygenase-4	Glycine max	140-152	
8904293-7	1996	We propose that a synergistic interaction may occur between the peroxides inserted into LDL as a consequence of the enzymatic action of lipoxygenase with haem proteins or copper, which decreases the potency of the endogenous antioxidants and enhances oxidation.	Peroxides	64-73	linoleate 9S-lipoxygenase-4	Glycine max	136-148	
10602300-3	1999	The reactivity of lipoxygenase with peroxides in the gallic acid solidus hydroperoxide system was in the order of methylethyl hydroperoxide (MEK-OOH, 4800 cps) > tert-butyl hydroperoxide (tert-BuOOH, 607 cps) > hydrogen peroxide (H(2)O(2), 455 cps) > cumene hydroperoxide (cumene-OOH, 261 cps).	Peroxides	36-45	linoleate 9S-lipoxygenase-4	Glycine max	18-30