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Background
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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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Background
References
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- Soundar, S., et al., J. Biol. Chem. 278(52):52146-52153 (2003).
- Weiss, C., et al., Biochemistry 39(7):1807-1816 (2000).
- Kim, Y.O., et al., J. Biol. Chem. 274(52):36866-36875 (1999).
- Huh, T.L., et al., Genomics 32(2):295-296 (1996).
- Kim, Y.O., et al., Biochem. J. 308 (PT 1), 63-68 (1995) (): ().
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