Enzyme Homework 1. The initial rate of an enzymatic reaction was determined at different substrate concentrations. The data is below: [S] (µmoles/L) v [(µmol/L) min -¹] 0.05 0.24 0.5 2.3 5 22 10 39 20 65 50 102 100 120 200 135 a. Try to calculate more or less what the Km of the enzyme is. b. Quickly calculate what the velocity would be when [S] = 1µmol / L c. Now make the Michaelis and Menten graph and use it to estimate Vmax and Km. d. Make the Lineweaver-Burk graph and use it to estimate Vmax and Km. e. What would you expect to find in the Vmax and Km values if you do the same experiment but with twice the amount of enzyme used here. Draw your answer on the MM graph (question c)
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An enzyme catalyzes the reaction A → B. The initial rate of the reaction was measured as a function of the concentration of A. The following data were obtained. Use a Lineweaver-Burke analysis to derive your answers. [A], micromolar V0, nmoles/min 0.05 0.08 0.1 0.16 0.5 0.79 1 1.6 5 7.3 10 13 50 40 100 53 500 73 1,000 76 5,000 79 10,000 80 20,000 80 a. What is the Km of the enzyme for the substrate A? b. What is the value of V0 when [A] = 43 uΜ? c. What is the value of Vmax? d. Using the competitive inhibitor I (concentration 2 uΜ, Ki = 200 uΜ), how is Km and Vmax changing?
Adi S.
Consider enzyme-catalyzed reactions that have typical Michaelis-Menten kinetics. Answer the following questions. a. What percentage of Vmax is obtained when the substrate is present at 25% of the Km? Show your work. b. What is the kcat for a reaction in which Vmax is 0.4 mmol/min and the reaction mixture contains 5 x 10^-6 micromoles of enzyme? Show your work and show units. c. If an enzyme-catalyzed reaction has a Km of 3.5 mM and the velocity of the reaction is 5 mM/min at a substrate concentration of 0.5 mM, what is the Vmax? Show your work and show units.
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Table $11^{*}$ lists data for the enzyme invertase treated with the substrate sucrose. We want to model these data with a Michaelis-Menten function. (A) Plot the points in Table 11 on graph paper and estimate $V_{\max }$ to the nearest integer. To estimate $K_{M},$ add the horizontal line $v=\frac{V_{\max }}{2}$ to your graph, connect successive points on the graph with straight-line segments, and estimate the value of $s$ (to the nearest integer) that satisfies $v(s)=\frac{V_{\max }}{2}$ (B) Use the constants $V_{\max }$ and $K_{M}$ from part (A) to form a Michaelis-Menten function for the data in Table $11 .$ (C) Use the function from part (B) to estimate the velocity of the enzyme reaction when the sucrose is 9 and to estimate the sucrose when the velocity is 32
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