The image below shows the Lineweaver-Burke plot for Enzyme catalysed reaction. Units for the Y- axis is (s/mmol) and X-axis is (1/mM). Use the data on the plot to calculate Vmax and Km for this reaction. Type your answers in the text box below clearly indicating which value is Vmax and which one is Km. You do not need to show your workings but don't forget your units. -0.4 Download -0.2 0.4 0.3 0.2 0.1 ..0.0. -0.1 0.0 ENZYME CATALYSED REACTION 0.2 0.4 y = 0.3086x + 0.0276 R² = 0.9967 0.6 0.8 1.0 1.2

The image below shows the Lineweaver-Burke plot for Enzyme catalysed reaction. Units for the Y- axis is (s/mmol) and X-axis is (1/mM). Use the data on the plot to calculate Vmax and Km for this reaction. Type your answers in the text box below clearly indicating which value is Vmax and which one is Km. You do not need to show your workings but don't forget your units. -0.4 Download -0.2 0.4 0.3 0.2 0.1 ..0.0. -0.1 0.0 ENZYME CATALYSED REACTION 0.2 0.4 y = 0.3086x + 0.0276 R² = 0.9967 0.6 0.8 1.0 1.2

Chemistry & Chemical Reactivity

10th Edition

ISBN:9781337399074

Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Chapter14: Chemical Kinetics: The Rates Of Chemical Reactions

Section14.7: Reaction Mechanisms

Problem 1.2ACP

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10. Applying the Michaelis-Menten Equation III A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction HAPPY = SAD. The researchers begin to characterize the enzyme. a. In the first experiment, with [E:] at 4 nm, they find that the Vmax is 1.6 µM s1. Based on this experiment, what is the kcat for happyase*? (Include appropriate units.) b. In the second experiment, with [E:] at 1 nm and [HAPPY] at 30 µM, the researchers find that Vo = 300 nMs. What is the measured Km of S %3D happyase* for its substrate HAPPY? (Include appropriate units.) c. Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation and the two experiments are repeated, the measured Vmax in (a) is increased to 4.8 µM s, and the measured Km in (b) is now 15 µM. Calculate the values of a and a' for ANGER.…
4. Suppose the data shown below are obtained for an enzyme catalyzed reaction. [S] (MM) v (mmol/ml/min) 0.1 3.33 0.2 5.0 0.5 7.14 0.8 8.0 1.0 8.3 2.0 9.09 a) Plot the data and determine Km and Vmax (please include the plot). b) Assuming the enzyme was used in these reactions at a concentration of 10-6 M, then calculate the turnover number for the enzyme.
A research group discovers a neW version oI happyasee, which they nappyase", that catalyzes the chemical reaction HAPPY = SAD The researchers begin to characterize the enzyme. In the first experiment, with [E] at 4 nM, they find that the Vmax is 1.6 µM s-1. Based on this experiment, what is the kcat for happyase*? kcat 400 S In another experiment, with [E,] at 1 nM and [HAPPY] at 30 µM, the researchers find that Vo is equal to 300 nM s-1. What i the measured Km of happyase* for its substrate HAPPY? Km 10 x10–6 Incorrect Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two experiments repeated, the measured Vmax increases to 4.8 µM s-, and the measured Km is now 15 µM. S For the inhibitor ANGER, calculate the values of a' and a. a' 2 Incorrect 2
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Question 14 of 58 Click to see additional instructions The rate of an enzyme-catalyzed reaction (in mM/min) was determined at different concentrations of substrate On a double-reciprocal Ginewnaver-Burk) plot of the data, the intercept wi -0.01 mM and the slope was 0.05 min. Determine the two values below and give your answer as a whole number (no decimals). Acceptable Characters Only numbers, decimal point markers, or sign indicators preceding a number Vmax mM/min Km mM
What should be taken in consideration when designing an enzyme kinetics experiment so that the reaction will not be too slow or too fast? M - amount of substrate B - amount of enzyme |- temperature O - pH
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