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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. NAD(+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein described here is the alpha subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase.
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Protein Aliases: H-IDH alpha; isocitrate dehydrogenase (NAD+) alpha chain; isocitrate dehydrogenase 3 (NAD+) alpha; Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial; Isocitric dehydrogenase subunit alpha; NAD(+)-specific ICDH subunit alpha; NAD(H)-specific isocitrate dehydrogenase alpha subunit; NAD+-specific ICDH
Gene Aliases: IDH3A
UniProt ID: (Human) P50213
Entrez Gene ID: (Human) 3419
Molecular Function: dehydrogenase