F. Common table sugar is hydrolyzed to glucose and fructose in a classic ties of amino acids (3 marks) proper experiment in kinetics. The reaction is catalysed by the enzyme invertase. Using the following data, determine, by the lineweaver-Burk method, the \( \mathrm{K}_{\mathrm{m}} \) and \( V_{\text {max }} \) of the enzyme. The reaction is inhibited by adding 2 M urea. Determine whether the inhibition is competitive or non-competitive ( 12 marks) \begin{tabular}{|l|l|l|} \hline \begin{tabular}{l} Common table sugar \\ con \( \left(\mathrm{mol} \mathrm{L}^{-1}\right) \) \end{tabular} & \begin{tabular}{l} V, no inhibitor \\ (arbitrary units) \end{tabular} & \begin{tabular}{l} V, inhibitor present \\ (same arbitrary \\ units) \end{tabular} \\ \hline 0.0292 & 0.182 & 0.083 \\ \hline 0.0584 & 0.265 & 0.119 \\ \hline 0.0876 & 0.311 & 0.154 \\ \hline 0.117 & 0.330 & 0.167 \\ \hline 0.175 & 0.372 & 0.192 \\ \hline \end{tabular}
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0292, 0.0584, 0.0876, 0.117, 0.175 - Velocity \(V\) (no inhibitor, arbitrary units): 0.182, 0.265, 0.311, 0.330, 0.372 - Velocity \(V\) (inhibitor present, arbitrary units): 0.083, 0.119, 0.154, 0.167, 0.192 Show more…
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Sucrose (common table sugar) is hydrolyzed to glucose and fructose (Section 16.3) in a classic experiment in kinetics. The reaction is catalyzed by the enzyme invertase. Using the following data, determine, by the Lineweaver-Burk method, whether the inhibition of this reaction by 2 M urea is competitive or noncompetitive.
Jenny W.
On some baking product labels, you might see an ingredient called "invert sugar." This is made by hydrolyzing sucrose (common table sugar) to glucose and fructose. The reaction is catalyzed by the enzyme invertase. Using the following data, determine whether the inhibition by 2 M urea is competitive or noncompetitive.
2. The table below indicates the rate at which a substrate reacts as catalyzed by an enzyme that follows Michaelis-Menten kinetics: 1) in the absence of inhibitor; 2) and 3) in the presence of 10 mM concentration, respectively, of each of two inhibitors. Assume [E]T is the same for all reactions. [S] (mM) | (1) v0 (ÎĽM/s) | (2) v0 (ÎĽM/s) | (3) v0 (ÎĽM/s) 1 | 2.5 | 1.17 | 0.77 2 | 4.0 | 2.10 | 1.25 5 | 6.3 | 4.00 | 2.00 10 | 7.6 | 5.7 | 2.50 20 | 9.0 | 7.2 | 2.86 Make a Lineweaver-Burke plot (and show it) to determine: a) Vmax in the absence & presence of each inhibitor b) Km in the absence & presence of each inhibitor c) Type of inhibition for each inhibitor
Sri K.
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