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- W2066156768 abstract "Abstract Isocitrate dehydrogenase ( threo - d s -isocitrate: NAD oxidoreductase (decar☐ylating) EC 1.1.1.41) from Dictyostelium dicoideum was purified 161-fold. The purified enzyme was NAD specific and required Mn 2+ for activity. Isocitrate consumption and 2-oxoglutarate and NADH production were stoichiometric; no NADH oxidase or glutamate dehydrogenase activities were detected. The pH optimum range for activity was pH 7.5–8.5. Reductive car☐ylation of 2-oxoglutarate with NADH could not be demonstrated. Lineweaver - Burk plots of data from initial velocity studies were linear. There was no evidence of allosteric control by reported effectors (AMP, ADP, citrate) of isocitrate dehydrogenase activity. The reaction was inhibited by NADH. The inhibition by NADH was competitive when either isocitrate or NAD was the variable substrate. 2-Oxoglutarate was not inhibitory at concentrations below 4 m m . The Michaelis constant ( K m ) and dissociation constant ( K ib ) for isocitrate were 0.16 m m ; and K m and dissociation constant ( K ia ) for NAD were 0.34 m m . The inhibition constant for NADH was 0.02 m m . The data are consistent with a rapid equilibrium random bi-bi reaction mechanism (Cleland nomenclature). The NAD-linked isocitrate dehydrogenase activity was also demonstrated in crude extracts of isolated mitochondria." @default.
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- W2066156768 date "1982-09-01" @default.
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- W2066156768 title "Purification and characterization of NAD-dependent isocitrate dehydrogenase from Dictyostelium discoideum" @default.
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- W2066156768 doi "https://doi.org/10.1016/0147-5975(82)90120-7" @default.
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