Enzymes with a Kcat /Km Ratio of About 108 M-1s-1

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Enzymes with a kcat /Km ratio of about 108 M-1s-1 are considered to show optimal catalytic efficiency. Fumarase, which catalyzes the reversible-dehydration reaction Enzymes with a k<sub>cat </sub>/K<sub>m</sub> ratio of about 10<sup>8</sup> M<sup>-</sup><sup>1</sup>s<sup>-</sup><sup>1</sup> are considered to show optimal catalytic efficiency. Fumarase, which catalyzes the reversible-dehydration reaction has a ratio of turnover number to the Michaelis-Menten constant, (k<sub>cat</sub>/K<sub>m</sub>) of 1.6 × 10<sup>8</sup> for the substrate fumarate and 3.6 × 10<sup>7</sup> for the substrate malate. Because the turnover number for both substrates is nearly identical, what factors might be involved that explain the different ratio for the two substrates? has a ratio of turnover number to the Michaelis-Menten constant, (kcat/Km) of 1.6 × 108 for the substrate fumarate and 3.6 × 107 for the substrate malate. Because the turnover number for both substrates is nearly identical, what factors might be involved that explain the different ratio for the two substrates?

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