This web page was produced as an assignment for an undergraduate course at Davidson College.

 

 

Chime Images of Isocitrate Dehydrogenase

 

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.) 

 

 

 

Orthologs of IDP2

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.

 

This page is maintained by Nicole Hesson.

 

Nicole Hesson’s Molecular Biology Homepage

 

Molecular Bio Homepage