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- W2006281465 abstract "A NADP-dependent isocitrate dehydrogenase was isolated from the zygomycetous fungus, Phycomyces blakesleeanus , and its physical and chemical properties were determined. The pH optimum for the forward reaction (NADP reduction) was ca. pH 7.5–8.5; the pH optimum for the reverse reaction (NADPH + H oxidation) was 6.0. Enzyme activity was significantly influenced by ionic strength. The molecular weight was estimated by means of gel filtration as 88,000. Purine and pyrimidine 5′-phosphorylated nucleosides, reduced glutathione, 2-mercaptoethanol, glyoxylate, and oxaloacetate neither inhibited nor activated the enzyme; however, sulfhydryl reagents moderately inhibited catalytic activity. The apparent K m values with respect to threo - d s -isocitrate, NADP, and Mn 2+ were 1.43 × 10 −4 , 3.52 × 10 −4 , and 3.36 × 10 −5 m , respectively. Hill plots indicated one binding site each for isocitric acid, NADP, and Mn 2+ . The enzyme had an absolute requirement for a metallic ion, the most effective being Mn 2+ . The action of the polydentate ligands triethylenetetramine, tetraethylenepentamine, and ethylenediaminetetraacetate on enzyme activity was examined and the significance of the binding data of these compounds is discussed." @default.
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- W2006281465 date "1979-09-01" @default.
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- W2006281465 title "Properties of NADP-dependent isocitrate dehydrogenase of Phycomyces blakesleeanus" @default.
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- W2006281465 doi "https://doi.org/10.1016/s0147-5975(79)80048-1" @default.
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