Specific site inhibitors of NAD-specific isocitrate dehydrogenase from bovine heart.

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Re-evaluation of molecular weight of pig heart NAD-specific isocitrate dehydrogenase.

NAD-specific pig heart isocitrate dehydrogenase was earlier reported, on the basis of gel filtration experiments, to have a molecular weight of approximately 340,000. In the present study, the enzyme is shown by equilibrium ultracentrifugation to have a weight average molecular weight of approximately 224,000 which can be attributed to a rapidly associating-dissociating protein system. The resu...

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Yeast NAD(+)-specific isocitrate dehydrogenase (IDH) is an octamer containing two types of homologous subunits. Ligand-binding analyses were conducted to examine effects of residue changes in putative catalytic and regulatory isocitrate-binding sites respectively contained in IDH2 and IDH1 subunits. Replacement of homologous serine residues in either subunit site, S98A in IDH2 or S92A in IDH1, ...

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In most living organisms, isocitrate dehydrogenases (IDHs) convert isocitrate into ɑ-ketoglutarate (ɑ-KG). Phylogenetic analyses divide the IDH protein family into two subgroups: types I and II. Based on cofactor usage, IDHs are either NAD+-specific (NAD-IDH) or NADP+-specific (NADP-IDH); NADP-IDH evolved from NAD-IDH. Type I IDHs include NAD-IDHs and NADP-IDHs; however, no type II NAD-IDHs hav...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1982

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)34291-1