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  • Title: Hysteretic nature of phosphoenolpyruvate carboxylase isolated from maize.
    Author: Jawali N.
    Journal: Arch Biochem Biophys; 1990 Feb 15; 277(1):69-73. PubMed ID: 2306126.
    Abstract:
    The hysteretic nature of phosphoenolpyruvate carboxylase from maize was investigated at pH 7 by (a) transient kinetic studies, (b) kinetics of inhibition by 2-PG, a structural analog of PEP, and (c) effect of 2-PG on equilibrium binding of Mg2+. The lag time as a function of substrate concentration was nonlinear with an oblique asymptote. During steady state, cooperative kinetics for Mg2+ was changed to hyperbolic kinetics in the presence of 2-PG. Studies on the equilibrium binding of Mg2+ with the help of an external fluorescent probe, 8-anilino-6-naphthalinosulfonate showed that the hyperbolic binding of Mg2+ was changed to cooperative binding in the presence of 2-PG. On the basis of these results along with the results presented in the preceding paper, a fully concerted sequential model with subunit interaction is proposed for PEPC.
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