Allosteric inhibition of muscle pyruvate kinase by phenylalanine

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L-Phenylalanine inhibition of muscle pyruvate kinase.

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 kinet...

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Allosteric properties of skeletal muscle pyruvate kinase.

The phenylalanine inhibition of skeletal muscle pyruvate kinase has been further studied. Even at high levels of the inhibitor the plots of reaction rates as a function of phosphoenolpyruvate concentration give hyperbolic curves; the inhibition by phenylalanine is of the mixed type. The enzyme exhibits a homotropic cooperative effect with respect to this inhibitor. This property is strongly dep...

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The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate.

BACKGROUND Yeast pyruvate kinase (PK) catalyzes the final step in glycolysis. The enzyme therefore represents an important control point and is allosterically activated by fructose-1,6-bisphosphate (FBP). In mammals the enzyme is found as four different isozymes with different regulatory properties: two of these isozymes are produced by alternate splicing. The allosteric regulation of PK is dir...

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Mechanism of pyruvate inhibition of kidney pyruvate dehydrogenasea kinase and synergistic inhibition by pyruvate and ADP.

Pyruvate has been shown to both stimulate and inhibit kidney pyruvate dehydrogenase, (PDH,) kinase activity. The present study investigates the inhibitory effect of pyruvate under conditions in which the stimulatory effect is invariant. Inhibition of PDH, kinase activity by dichloroacetate, a pyruvate analog, is also characterized. Both pyruvate and dichloroacetate are uncompetitive, hyperbolic...

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Pyruvate has been shown to both stimulate and inhibit kidney pyruvate dehydrogenase, (PDH,) kinase activity. The present study investigates the inhibitory effect of pyruvate under conditions in which the stimulatory effect is invariant. Inhibition of PDH, kinase activity by dichloroacetate, a pyruvate analog, is also characterized. Both pyruvate and dichloroacetate are uncompetitive, hyperbolic...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 1970

ISSN: 0014-5793

DOI: 10.1016/0014-5793(70)80549-x