Evidence for a critical glutamyl and an aspartyl residue in the function of pig heart diphosphopyridine nucleotide dependent isocitrate dehydrogenase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00627a006
Reference29 articles.
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4. Purification of NAD-specific isocitrate dehydrogenase from porcine heart
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1. Identification of Mn2+-binding Aspartates from α, β, and γ Subunits of Human NAD-dependent Isocitrate Dehydrogenase;Journal of Biological Chemistry;2006-07
2. Two NAD+-Isocitrate Dehydrogenase Forms in Phycomyces blakesleeanus. Induction in Response to Acetate Growth and Characterization, Kinetics, and Regulation of Both Enzyme Forms;Biochemistry;1996-01-01
3. Cadmium-113 and magnesium-25 NMR study of the divalent metal binding sites of isocitrate dehydrogenases from pig heart;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1995-01
4. Cloning of a cDNA encoding bovine mitochondrial NADP+-specific isocitrate dehydrogenase and structural comparison with its isoenzymes from different species;Biochemical Journal;1993-06-15
5. Selectivity in the binding of NAD(P)+ analogs to NAD- and NADP-dependent pig heart isocitrate dehydrogenases. A nuclear magnetic resonance study;Biochemistry;1992-12-15
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