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This study compares the kinetic and optical properties of pyruvate kinase from rabbit muscle, sturgeon muscle, and yeast, focusing on the effects of various divalent metal ions and allosteric effectors. The findings indicate that all three enzymes exhibit similar activating efficiencies and pH-rate profiles, suggesting a common mechanism of action and conformational states influenced by substrate and allosteric binding. Notably, L-Phe inhibits rabbit muscle pyruvate kinase, while fructose-1,6-biphosphate ac

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filip.social97

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EN