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Isocitrate dehydrogenase of Tetrahymena pyriformis

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Summary

We have studied the isocitrate dehydrogenase ofTetrahymena pyriformis. This enzyme is able to utilize both NAD and NADP, but kinetic studies suggest that the enzymatic activity with NAD is not of physiological significance.

Some of the factors that might regulate the NADP-dependent isocitrate dehydrogenase were also studied. This enzyme has an absolute requirement for divalent cations; Mg2+ and Mn2+ will serve as cofactors but the latter is more effective than the former.

It is known that this enzyme is subject to a concerted inhibition by oxaloacetate and glyoxylate. Either glyoxylate or oxaloacetate alone also are capable of inhibiting the enzyme although higher concentrations are required. We have found concerted inhibition also for the NAD-dependent isocitrate dehydrogenase from rat liver and yeast. The activity of theTetrahymena pyriformis enzyme is inhibited by NADPH. This inhibition is competitive with NADP. The Ki and Km values are, respectively, 23µ m and 18µ m.

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Authors and Affiliations

  1. Centro de Biologia Molecular, C.S.I.C. Universidad Autónoma de Madrid. Facultad de Ciencias, Madrid 34, Spain

    Pilar Vidal & Alberto Machado

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  1. Pilar Vidal
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  2. Alberto Machado
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Vidal, P., Machado, A. Isocitrate dehydrogenase of Tetrahymena pyriformis. Mol Cell Biochem 17, 151–156 (1977). https://doi.org/10.1007/BF01730835

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