Homework Answers
Highest value of V° is the correct answer
Here option C is correct answer
Option E is not correct because at 3000 mmol/l , this V is obtained
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(3 of 5) The following data were obtained in a study of an enzyme known to...
26. The serine 195 sidechain forms acyl-enzyme intermediate following the sessile bond cleavage. To regenerate the...
26. The serine 195 sidechain forms acyl-enzyme intermediate following the sessile bond cleavage. To regenerate the serine sidechain, the hydroxide of 27. True or False. Imadazole of His is a strong electrophile for attacking carbonyl carbon atom. nucleophilic attacks the carbonyl carbonyl carbon of the acyl-enzyme intermediate to form tetrahedral intermediate. 28. Write down Michaelis-Menten equation. 29. The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: Vo (umol/min) Substrate (umol/L) 117 225 324...
Please show all your work and the thought process i.e why you did what you did,...
Please show all your work and the thought process i.e why you did what you did, also I have to do this by hand with a calculator, so please DON'T use graphs or plot anything. Thank you. The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: V0 (μmol/min) ————————————— 217 325 433 488 647 ————————————— Substrate added (mmol/L): 0.8 2 4 6 1,000 The Km for this enzyme is approximately: A) 1 mM...
112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the...
112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the enzyme- catalized reactions are explained by Michaelis-Menten equation. IMPORTANT: Show the calculations and indicate the units for all your answers. a. For an enzyme which follows the Michaelis-Menten enzyme kinetics, Km is 50 mmol L. Calculate the substrate concentration required to obtain the initial velocity (V.) equivalent to 90% of the maximum velocity (Vmax). b. The Vmax of the above reaction is 250 mmol...
20.8 2) Consider the following data for an enzyme-catalyzed hydrolysis reaction in the presence and absence...
20.8 2) Consider the following data for an enzyme-catalyzed hydrolysis reaction in the presence and absence of inhibitor I using a Michaelis-Menten plot, determine Kn for both inhibited and uninhibited reactions. What kind of inhibition is this? [Substrate)(M) vo (umol/min) Vos (moles/min) 6x106 4.2 1x105 29 5.8 2x105 6x109 13.6 1.8x10* 16.2
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a...
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine, by inspection of the graph, the values for Km and Vmax. ISI (M) V (nmol/min) 0.20 0.26 0.33 1.00 1.43 1.67 2.08 3.33 5. You measured the kinetics of an enzyme activity as a function of substrate concentration (see Table). The enzyme concentration was maintained constant at a level of 1 M. [S] AM Vopmol/min 2.9 3.8 4.4 Plot the...
The following data were obtained in an enzyme study: Use these data to construct a Michaelis-Menten...
The following data were obtained in an enzyme study: Use these data to construct a Michaelis-Menten plot, a Lineweaver-Burk plot, and an Eadie-Hofstee plot. Fit the data in the L-B and E-H plots and use the fit parameters to determine K_M and v_s in each case. Comment on how well the K_Ms and v_ss agree with each other.
1. The turnover number for an enzyme is known to be 5000 min. From the following set of data, calculate the Km, Vma...
1. The turnover number for an enzyme is known to be 5000 min. From the following set of data, calculate the Km, Vmax and the amount of enzyme present in this experiment. Use excel to obtain the lineweaver burk plot. Substrate concentration (MM) 1 Initial velocity (umol/min) 167 250 334 376 498 499 100 1,000
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
9. The following data were obtained from an enzyme kinetics experiment. Graph the data using a...
9. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine the values for Km and Vmax. [S] (UM) V(nmol/min) 0.20 0.26 1.43 1.67 2.08 3.33 0.33 1.00
1. Calculate the pKa of lactic acid, given that when the concentration of lactic acid is...
1. Calculate the pKa of lactic acid, given that when the concentration of lactic acid is 0.010 M and the concentration of lactate is 0.087 M, the pH is 4.80 B. Calculate the ratio of the concentrations of acetate and acetic acid required in a buffer system of pH 5.30 C The pH of a 0.20 M sodium acetate buffer is 5.1. The pKa of acetic acid is 4.76. Explain in details (showing all calculation) how to prepare the buffer...
26. The serine 195 sidechain forms acyl-enzyme intermediate following the sessile bond cleavage. To regenerate the serine sidechain, the hydroxide of 27. True or False. Imadazole of His is a strong electrophile for attacking carbonyl carbon atom. nucleophilic attacks the carbonyl carbonyl carbon of the acyl-enzyme intermediate to form tetrahedral intermediate. 28. Write down Michaelis-Menten equation. 29. The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: Vo (umol/min) Substrate (umol/L) 117 225 324...
112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the enzyme- catalized reactions are explained by Michaelis-Menten equation. IMPORTANT: Show the calculations and indicate the units for all your answers. a. For an enzyme which follows the Michaelis-Menten enzyme kinetics, Km is 50 mmol L. Calculate the substrate concentration required to obtain the initial velocity (V.) equivalent to 90% of the maximum velocity (Vmax). b. The Vmax of the above reaction is 250 mmol...
20.8 2) Consider the following data for an enzyme-catalyzed hydrolysis reaction in the presence and absence of inhibitor I using a Michaelis-Menten plot, determine Kn for both inhibited and uninhibited reactions. What kind of inhibition is this? [Substrate)(M) vo (umol/min) Vos (moles/min) 6x106 4.2 1x105 29 5.8 2x105 6x109 13.6 1.8x10* 16.2
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine, by inspection of the graph, the values for Km and Vmax. ISI (M) V (nmol/min) 0.20 0.26 0.33 1.00 1.43 1.67 2.08 3.33 5. You measured the kinetics of an enzyme activity as a function of substrate concentration (see Table). The enzyme concentration was maintained constant at a level of 1 M. [S] AM Vopmol/min 2.9 3.8 4.4 Plot the...
The following data were obtained in an enzyme study: Use these data to construct a Michaelis-Menten plot, a Lineweaver-Burk plot, and an Eadie-Hofstee plot. Fit the data in the L-B and E-H plots and use the fit parameters to determine K_M and v_s in each case. Comment on how well the K_Ms and v_ss agree with each other.
1. The turnover number for an enzyme is known to be 5000 min. From the following set of data, calculate the Km, Vmax and the amount of enzyme present in this experiment. Use excel to obtain the lineweaver burk plot. Substrate concentration (MM) 1 Initial velocity (umol/min) 167 250 334 376 498 499 100 1,000
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
9. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine the values for Km and Vmax. [S] (UM) V(nmol/min) 0.20 0.26 1.43 1.67 2.08 3.33 0.33 1.00
1. Calculate the pKa of lactic acid, given that when the concentration of lactic acid is 0.010 M and the concentration of lactate is 0.087 M, the pH is 4.80 B. Calculate the ratio of the concentrations of acetate and acetic acid required in a buffer system of pH 5.30 C The pH of a 0.20 M sodium acetate buffer is 5.1. The pKa of acetic acid is 4.76. Explain in details (showing all calculation) how to prepare the buffer...
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