Isocitrate Dehydrogenase of Tetrahymena Pyriformis

Overview

Journal Mol Cell Biochem

Publisher Springer

Specialty Biochemistry

Date 1977 Oct 7

PMID 22034

Citations 1

Authors

P Vidal

A Machado

Affiliations

Soon will be listed here.

Abstract

We have studied the isocitrate dehydrogenase of Tetrahymena 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 signifance. Some of the factors that might regualte the NADP-dependent isocitrate dehydrogenase were also studied. This enzyme has an absolute requirement for divalent cations; Mg,+ 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 the Tetrahymena pyriformis enzyme is inhibited by NADPH. This inhibition is competitive with NADP. The Ki and Km values are, respectively, 20 micrometers and 18 micrometers.

Citing Articles

NADPH/NADP+ ratio: regulatory implications in yeast glyoxylic acid cycle.

Satrustegui J, Bautista J, Machado A Mol Cell Biochem. 1983; 51(2):123-7.

PMID: 6343836 DOI: 10.1007/BF00230397.

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