Question is in image. ### Enzyme Kinetics Study: α-Chymotrypsin**Introduction:**The enzyme α-chymotrypsin is secreted in the pancreas of mammals and cleaves peptide bonds made between certain amino acids. For this experiment, several solutions containing the small peptide N-glutaryl-L-phenylalanine-p-nitroanilide at different concentrations were prepared. The same small amount of α-chymotrypsin was added to each solution, and the initial rates of product formation were recorded.**Data:**The table below shows the concentration of the substrate ([S] in mmol dm⁻³) and the initial rate of product formation (v in mmol dm⁻³ s⁻¹).| [S] (mmol dm⁻³) | 0.334 | 0.450 | 0.667 | 1.00 | 1.33 | 1.67 ||--------------------------|------------|-------------|-------------|------------|------------|------------|| v (mmol dm⁻³ s⁻¹) | 0.152 | 0.201 | 0.269 | 0.417 | 0.505 | 0.667 |**Objective:**Determine the maximum velocity \( V_{max} \) and the Michaelis constant \( K_m \) for the reaction catalyzed by α-chymotrypsin.**Understanding the Data:**The goal is to find \( V_{max} \), the maximum rate of the reaction when the enzyme is saturated with the substrate, and \( K_m \), the substrate concentration at which the reaction rate is half of \( V_{max} \). This information is vital in understanding the efficiency and affinity of the enzyme for the substrate.**Analysis:**To analyze this data, you can plot [S] against v and fit the data to the Michaelis-Menten equation:\[ v = \frac{V_{max}[S]}{K_m + [S]} \]Alternatively, a Lineweaver-Burk plot (double reciprocal plot) can be used, plotting \( \frac{1}{v} \) versus \( \frac{1}{[S]} \), which linearizes the Michaelis-Menten equation:\[ \frac{1}{v

We have to find the Michaelis constant Km adn maximum velocity for given data, by plotting Michaelis…

I The enzyme a-chymotrypsin is secreted in the pancreas of mamma and cleaves peptide bonds made between certain amino acids. Several solution containing the small peptide N-glutaryl-L-phenylalanine-p-nitroanilide at diffe ent concentrations were prepared and the same small amount of a-chymotryps was added to each one. The following data were obtained on the initial rates of th formation of product: [S]/(mmol dm-3) 0.334 0.450 0.667 1.00 1.33 1.67 v/(mmol dm-³s-1) 0.152 0.201 0.269 0.417 0.505 0.66 Determine the maximum velocity and the Michaelis constant for the reaction.

I The enzyme a-chymotrypsin is secreted in the pancreas of mamma and cleaves peptide bonds made between certain amino acids. Several solution containing the small peptide N-glutaryl-L-phenylalanine-p-nitroanilide at diffe ent concentrations were prepared and the same small amount of a-chymotryps was added to each one. The following data were obtained on the initial rates of th formation of product: [S]/(mmol dm-3) 0.334 0.450 0.667 1.00 1.33 1.67 v/(mmol dm-³s-1) 0.152 0.201 0.269 0.417 0.505 0.66 Determine the maximum velocity and the Michaelis constant for the reaction.

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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