The β and γ subunits play distinct functional roles in the α2βγ heterotetramer of human NAD-dependent isocitrate dehydrogenase

Author:

Ma Tengfei,Peng Yingjie,Huang Wei,Liu Yabing,Ding Jianping

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Reference42 articles.

1. McAlister-Henn, L. Ligand binding and structural changes associated with allostery in yeast NAD(+)−specific isocitrate dehydrogenase. Arch Biochem Biophys 519, 112–117 (2012).

2. Ehrlich, R. S. & Colman, R. Separation, recombination, and characterization of dissimilar subunits of the DPN-dependent isocitrate dehydrogenase from pig heart. J Biol Chem 258, 7079–7086 (1983).

3. Ehrlich, R. S., Hayman, S., Ramachandran, N. & Colman, R. Re-evaluation of molecular weight of pig heart NAD-specific isocitrate dehydrogenase. J Biol Chem 256, 10560–10564 (1981).

4. Ehrlich, R. S. & Colman, R. F. Interrelationships among nucleotide binding sites of pig heart NAD-dependent isocitrate dehydrogenase. J Biol Chem 257, 4769–4774 (1982).

5. Ramachandran, N. & Colman, R. F. Chemical characterization of distinct subunits of pig heart DPN-specific isocitrate dehydrogenase. J Biol Chem 255, 8859–8864 (1980).

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