5. The following kinetic data are recorded for equal amounts of the enzyme, proline racemase,in the absence and presence of an inhibitor, I. Based on the Lineweaver-Burk plots:a. What type of inhibitor is I?b. Calculate the Km and Vmax in the presence and absence of the inhibitor?c. Calculate Ki of the inhibitor when 0.4mM inhibitor is used.0.50.40.30.20.1-0.2-0.10.10.20.30.4-0.11/[S] (1/mM)1/V (min/mM)

Competitive inhibitors bind to the free enzyme and show changes in the slope of the plot whereas…

5. The following kinetic data are recorded for equal amounts of the enzyme, proline racemase in the absence and presence of an inhibitor, I. Based on the Lineweaver-Burk plots: a. What type of inhibitor is 1? b. Calculate the Km and Vmax in the presence and absence of the inhibitor? c. Calculate Ki of the inhibitor when 0.4mM inhibitor is used. 0.5 0.4 0.3 0.2 30.1 -0.2 -0.1 -0.1 0.1 0.2 0.3 0.4 1/[S] (1/mM) 1/V (min/mM)

5. The following kinetic data are recorded for equal amounts of the enzyme, proline racemase in the absence and presence of an inhibitor, I. Based on the Lineweaver-Burk plots: a. What type of inhibitor is 1? b. Calculate the Km and Vmax in the presence and absence of the inhibitor? c. Calculate Ki of the inhibitor when 0.4mM inhibitor is used. 0.5 0.4 0.3 0.2 30.1 -0.2 -0.1 -0.1 0.1 0.2 0.3 0.4 1/[S] (1/mM) 1/V (min/mM)

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...

See similar textbooks

Similar questions

Indicate the mechanism of enzyme inhibition represented in each plot, and justify your answer with respect to inhibitor effect on Km and Vmax.
1
4. Graphing the results from kinetics experiments with enzyme inhibitors The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of two different inhibitors (2) and (3) at 5 mM concentration. Assume [Er] is the same in each experiment. [S] (mM) 1 2 4 8 12 1 2 4 8 12 [S] (mm) a. Determine Vmax and Km for the enzyme. b. Determine the type of inhibition and the Kıfor each inhibitor. 1/[S] M-1 Plot these data as double-reciprocal Lineweaver-Burk plots and use your graph to answers a. and b. 1000 500 250 125 83.3 Answer: The data may be analyzed using double-reciprocal variables. For each [S] and corresponding u, we will calculate 1/[S] and 1/v. sed to get mo Helmien (1) v (μmol/mL sec 12 20 29 35 40 1/v (1) v (1) μmol/mL se mL-sec/umol C 12 20 29 35 40 Please explain how to get K 1/v 20 × 104 10 × 104 -400 8.33x104 5.00x104 3.45x104 2.86x104 2.50x104 Condition No inhibitor 0 5 mM inhibitor (2) 5 mM inhibitor (3) Plots of 1/v vs. 1/[S]…
Give me detailed Solution with explanation needed..don't give Handwritten answer
Please answer C and D.
Enz-SH + Ag* - Enz-S-Ag + H* The affinity of Ag* for sulfhydryl groups is so great that Ag* can be used to titrate -SH groups quantitatively. To 10.0 mL of a solution containing 3.5 mg/mL of a pure enzyme, an investigator added just enough AGNO, to completely inactivate the enzyme. A total of 0.536 umol AGNO, was required. Calculate the minimum molecular weight (M,) of the enzyme. minimum M, = The determined M, is not exact, but it is a minimum value for the M, of the enzyme. Why does the M, value obtained this way give only the minimum molecular weight? There is only one polypeptide chain. There are no disulfide bonds in the protein. There is only one titratable -SH group per protein molecule. The Ag* would also react with the terminal carboxyl group.
What conclusion can be drawn concerning an inhibitor if Vmax is the same in the presence and absence of the inhibitor? a. KM is smaller in the presence of the inhibitor. Ob. The inhibitor binds to the same active site as the substrate. Oc. The inhibitor binds to the substrate. Od. The inhibitor reacts with a critical residue of the enzyme. Je. The inhibitor can be overcome with sufficiently high concentrations of the substrate.
29. In chymotrypsin both histidine and serine are important amino acids in the catalytic reaction. Below is an image showing one step of the reaction. Describe what is happening and the roles histidine and serine are playing. In your answer be sure to use correct terms in describing the type of enzyme mechanism being done each amino acid. His Asp 102 H₂C CH₂ Ser (195) CH₂ 4 Asp 102 H₂C CH₂ His 57 New N-terminus of cleaved polypeptide R chain Ser 195 CH₂
4 1. Use the Michaelis-Menten equation to explain relationship between the amount of product produced and the concentration of enzyme in each reaction. 2. Briefly explain how you would modify the experiment performed in part C to determine the Km and Vmax of the lactase enzyme ANSWER BOTH
help please answer in text form with proper workings and explanation for each and every part and steps with concept and introduction no AI no copy paste remember answer must be in proper format with all working
The Km value of an enzyme is affected in the presence of a competitive inhibitor because it requires less substrate to achieve the same Vmax as without the inhibitor. True False
Allosteric regulators alter the equilibrium between the: A. ES state B. R and T forms of an enzyme. C. forward and reverse reaction rate. D. formation of the product and its reverse reaction. E. concentration thresholds.