Homework Answers
Ans.3. Allosteric enzyme is more sensitive to substrate concemtration because of that if the substrate bound to the active aite and inhibitor will bind to the allosteric site then all substrate site will occupy and it does not change the michalis mentan constant but Vmax will decreses because of that of irreversible reaction and non formation of product in this case,so these enzyme are most sensitive to substate,if all substrate occupy active site then no changes in the rate of reaction although we increase the substrate concentration.
Ans.4 low or hogh pH both will cause decrease in the rate of enzymatic reaction because of that the enzyme will work best on their optimum pH.
Same in the case of temperature,if we increase the temperature then enzyme original structure will destroyed hence its activity decreases.
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3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a...
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...
Write the equations that describe the Michaelis-Menten and the Lineweaver-Burk double-reciprocal plots. Draw examples of each...
Write the equations that describe the Michaelis-Menten and the Lineweaver-Burk double-reciprocal plots. Draw examples of each plot, demonstrating how Km and Vmax can be determined. On the same graphs, draw another plot where the same enzyme-catalyzed reaction is subjected to inhibition by a competitive inhibitor.
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is: a) a competitive inhibitor b) an allosteric inhibitor c) a noncompetitive inhibitor d) a suicide inhibitor 3. Competitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c) bind outside the active site and decrease substrate binding d) bind outside the active site and decrease rate of catalysis.
Please show how to calculate Km and Vmax for no inhibitor/low inhibitor given graph. Show how to ...
Please show how to calculate Km and Vmax for no inhibitor/low
inhibitor given graph. Show how to solve for a.,a/a etc.
Lineweaver Burk #4: No inhibitor, Low inhibitor 0.2 ▲ No inhibitor Low inhibitor 0.15 0.05 0.2 0.15 0.1 0.05 0.05 0.1 0.15 02 5 1/IS] in units of 1/mM Fill in the blanks. Show your work. No inhibitor Kmno Vmax,o- Vmax,w = ๙ Vmax,o Solve for ๙ inhibitor Krmkw =픕Km,o Solve for 픕 Hint treat, as a single number....
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as...
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as a function of substrate concentration; label both axes. Write the associated Michaelis-Menton equation and show the location of Km and Vmax on your graph. b. Draw a second graph showing the classic Lineweaver-Burk plot; label both axes. Show the location of Km and Vmax on your graph. Discuss which plot is the most useful to determine Vmax. Draw a second line on each graph...
1. Graphic depictions of enzyme kinetic data can aid in evaluation of reversible enzyme inhibition. Please...
1. Graphic depictions of enzyme kinetic data can aid in evaluation of reversible enzyme inhibition. Please use the data below to determine type of inhibition for using two different concentrations (in blue and purple). Be sure to include graphical representation (Michaelis-Menton, Lineweaver-Burk plots), type of inhibition, appropriate kinetic schemes and rate equations. The enzyme concentration at its initial state E, was kept constant. All data points are given in arbitrary units. Completely justify your answer. Use Excel or graphing paper...
D-Lactose is the substrate for B-galactosidase. Given Vo = kcat [Et] [S]/km + [S], calculate [S],...
D-Lactose is the substrate for B-galactosidase. Given Vo = kcat [Et] [S]/km + [S], calculate [S], when Km = 4.0 nM, V. = 10.5 M s', kcat = 500 s, and [Et] = 40 uM Calculate the catalytic efficiency. Below is a double-reciprocal plot for an enzyme reaction in the absence and presence of of inhibitor. Give the equation for the line. Calculate Vmax and Km for the enzyme and enzyme plus inhibitor. Which type of inhibition is apparent. 0.10...
Problem 3: A) Draw the mechanistic modifications associated with chymotripsin enzyme and its substrate up to...
Problem 3: A) Draw the mechanistic modifications associated with chymotripsin enzyme and its substrate up to the formation of acyl enzyme intermediate. Specify the role of each of the amino acids in the catalytic triad. B) Provide a Michaelis-Menten rate-law equation. Subsequently, on the same graph draw Lineweaver-Burk plots for i) enzyme which is not inhibited: ii) enzyme inhibited by a non-competitive inhibitor, C) The Km and kcat for hexokinase with as a glucose substarte are 5-10 M and 8-10²...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is give...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
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...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is: a) a competitive inhibitor b) an allosteric inhibitor c) a noncompetitive inhibitor d) a suicide inhibitor 3. Competitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c) bind outside the active site and decrease substrate binding d) bind outside the active site and decrease rate of catalysis.
Please show how to calculate Km and Vmax for no inhibitor/low
inhibitor given graph. Show how to solve for a.,a/a etc.
Lineweaver Burk #4: No inhibitor, Low inhibitor 0.2 ▲ No inhibitor Low inhibitor 0.15 0.05 0.2 0.15 0.1 0.05 0.05 0.1 0.15 02 5 1/IS] in units of 1/mM Fill in the blanks. Show your work. No inhibitor Kmno Vmax,o- Vmax,w = ๙ Vmax,o Solve for ๙ inhibitor Krmkw =픕Km,o Solve for 픕 Hint treat, as a single number....
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as a function of substrate concentration; label both axes. Write the associated Michaelis-Menton equation and show the location of Km and Vmax on your graph. b. Draw a second graph showing the classic Lineweaver-Burk plot; label both axes. Show the location of Km and Vmax on your graph. Discuss which plot is the most useful to determine Vmax. Draw a second line on each graph...
1. Graphic depictions of enzyme kinetic data can aid in evaluation of reversible enzyme inhibition. Please use the data below to determine type of inhibition for using two different concentrations (in blue and purple). Be sure to include graphical representation (Michaelis-Menton, Lineweaver-Burk plots), type of inhibition, appropriate kinetic schemes and rate equations. The enzyme concentration at its initial state E, was kept constant. All data points are given in arbitrary units. Completely justify your answer. Use Excel or graphing paper...
D-Lactose is the substrate for B-galactosidase. Given Vo = kcat [Et] [S]/km + [S], calculate [S], when Km = 4.0 nM, V. = 10.5 M s', kcat = 500 s, and [Et] = 40 uM Calculate the catalytic efficiency. Below is a double-reciprocal plot for an enzyme reaction in the absence and presence of of inhibitor. Give the equation for the line. Calculate Vmax and Km for the enzyme and enzyme plus inhibitor. Which type of inhibition is apparent. 0.10...
Problem 3: A) Draw the mechanistic modifications associated with chymotripsin enzyme and its substrate up to the formation of acyl enzyme intermediate. Specify the role of each of the amino acids in the catalytic triad. B) Provide a Michaelis-Menten rate-law equation. Subsequently, on the same graph draw Lineweaver-Burk plots for i) enzyme which is not inhibited: ii) enzyme inhibited by a non-competitive inhibitor, C) The Km and kcat for hexokinase with as a glucose substarte are 5-10 M and 8-10²...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
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