IDH is important in the citric acid cycle of cellular
respiration. It oxidizes isocitrate to a-ketoglutarate,
producing NADH + H+ and CO2. These products oxidize a-ketoglutarate to succinyl
CoA, and the cycle continues. (See
Purves et al. pg 153.)
IDP2 is cytosolic NADP+-specific isocitrate dehydrogenase. Haselbeck et al. showed IDP2 to be a homodimer with a translated region of 412 amino acids. After being analyzed, IDP2 and IDP1 were found to be identical in 71% of the amino acid sequence.
Read
abstracts about some cool IDP2 experiments:
1. Loftus TM, Hall LV, Anderson SL, McAlister-Henn L. Isolation, characterization, and disruption of the yeast gene encoding cytosolic NADP-specific isocitrate dehydrogenase. Biochemistry 1994 Aug 16;33(32):9661-7
2. Haselbeck RJ, McAlister-Henn L. Function and expression of yeast mitochondrial NAD- and NADP-specific isocitrate dehydrogenases. J Biol Chem 1993 Jun 5;268(16):12116-22
3. Jennings GT, Minard KI, McAlister-Henn L. Expression and mutagenesis of mammalian cytosolic NADP+-specific isocitrate dehydrogenase. Biochemistry 1997 Nov 4;36(44):13743-7
4. Narahari J, Ma R, Wang M, Walden WE. The aconitase function of iron regulatory protein 1. Genetic studies in yeast implicate its role in iron-mediated redox regulation. J Biol Chem. 2000 May 26;275(21):16227-34.