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Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. Each NADP(+)-dependent isozyme is a homodimer. IDH1 is the NADP(+)-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. IDH1 contains the PTS-1 peroxisomal targeting signal sequence. The presence of this enzyme in peroxisomes suggests roles in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid. The cytoplasmic enzyme serves a significant role in cytoplasmic NADPH production. IDH2 is the NADP(+)-dependent isocitrate dehydrogenase found in the mitochondria. IDH2 plays a role in intermediary metabolism and energy production and may tightly associate or interact with the pyruvate dehydrogenase complex.
Target Name: | IDH1/IDH2 / Isocitrate Dehydrogenase (NADP+) |
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