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  • Title: L-Phenylalanine inhibition of muscle pyruvate kinase.
    Author: Palmer TN, Odedra BR.
    Journal: Biosci Rep; 1982 Oct; 2(10):825-33. PubMed ID: 7171746.
    Abstract:
    The allosteric inhibition of M1-type pyruvate kinase from rabbit skeletal muscle by phenylalanine is reciprocally dependent on Mg2+ and phosphoenolpyruvate concentrations. At pH 8, phenylalanine acts as a competitive inhibitor with respect to Mg2+ and phosphoenolpyruvate, and vice versa. Phenylalanine introduces sigmoidicity into the dependence of the reaction velocity on [Mg2+]. In vitro kinetic analysis indicates that phenylalanine inhibition of muscle pyruvate kinase is unlikely to have regulatory significance in vivo.
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