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