PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31234015-0	2019	The fatty acid oxidation enzyme long-chain acyl-CoA dehydrogenase can be a source of mitochondrial hydrogen peroxide.	Hydrogen Peroxide	99-116	acyl-CoA dehydrogenase long chain	Homo sapiens	32-65	
31234015-2	2019	Here, we established that the mitochondrial flavoprotein long-chain acyl-CoA dehydrogenase (LCAD), which catalyzes a key step in mitochondrial FAO, directly produces H2O2in vitro by leaking electrons to oxygen.	Hydrogen Peroxide	166-170	acyl-CoA dehydrogenase long chain	Homo sapiens	57-90	
31234015-2	2019	Here, we established that the mitochondrial flavoprotein long-chain acyl-CoA dehydrogenase (LCAD), which catalyzes a key step in mitochondrial FAO, directly produces H2O2in vitro by leaking electrons to oxygen.	Hydrogen Peroxide	166-170	acyl-CoA dehydrogenase long chain	Homo sapiens	92-96	
31234015-3	2019	Kinetic analysis of recombinant human LCAD showed that it produces H2O2 15-fold faster than the related mitochondrial enzyme very long-chain acyl-CoA dehydrogenase (VLCAD), but 50-fold slower than a bona fide peroxisomal acyl-CoA oxidase.	Hydrogen Peroxide	67-71	acyl-CoA dehydrogenase long chain	Homo sapiens	38-42	
31234015-4	2019	The rate of H2O2 formation by human LCAD is slow compared to its activity as a dehydrogenase (about 1%).	Hydrogen Peroxide	12-16	acyl-CoA dehydrogenase long chain	Homo sapiens	36-40	
31234015-5	2019	However, expression of hLCAD in HepG2 cells is sufficient to significantly increase H2O2 in the presence of fatty acids.	Hydrogen Peroxide	84-88	acyl-CoA dehydrogenase long chain	Homo sapiens	23-28	
31234015-8	2019	Based on our data, we propose that the presence of LCAD drives H2O2 formation in response to fatty acids in these tissues.	Hydrogen Peroxide	63-67	acyl-CoA dehydrogenase long chain	Homo sapiens	51-55