Homework Answers
kcat - (f) Rate constant for substrate conversion to product in an enzyme active site
Allostery - (b) Changes in active site properties through ligand binding to another site.
Vmax - (d) Maximum rate for an enzyme under a given set of conditions.
Ki - (e) The dissociation constant for inhibitor binding to an enzyme.
Hill coefficient - (h) Describes the curvature of V vs [S] plots for cooperative enzymes.
Km - (i) Substrate concentration at which the velocity is 1/2 the maximum under a given set of conditions.
Velocity - (c) Rate of an enzyme reaction under a given set of conditions.
Ki (apparent) - (a) Concentration of inhibitor where the velocity is 1/2 the maximum under a given set of conditions.
Cooperativity - (g) Results from substrate affinity changes induced by substrate binding to oligomeric enzymes.
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Vmax II. Enzyme Kinetics 1. Vocabulary - match the term on the left with the definition...
56. In the lock and key model of substrate binding to enzymes Pprat wnich they work...
56. In the lock and key model of substrate binding to enzymes Pprat wnich they work best a the substrate changes its conformation to fit the active site b. the active site changes its conformation to fit the substrate c. the active site is rigid and the substrate must fit exactly d. the substrate binds only to part of the active site In the induced-fit model of substrate binding a. 57. the substrate changes its conformation to fit the active...
a. An enzyme has a Vmax of 100 umol/min and a Km of 40 uM. When...
a. An enzyme has a Vmax of 100 umol/min and a Km of 40 uM. When substrate concentration is 40 uM what is the initial reaction rate? b. An enzyme with a Vmax of 100 umol/minute and a Km of 10 uM was reacted with a irreversible active site specific inhibitor. After reaction with the inhibitor, the enzyme was assayed using a 2 mM concentration of substrate, and it gave a reaction rate of 20 umol/min. What percentage of the...
enzyme has a molar mass of 30 kilodatons. From this information, calculate Keat for this enzyme-catalyzed...
enzyme has a molar mass of 30 kilodatons. From this information, calculate Keat for this enzyme-catalyzed reaction both with and without inhibitor. Also explain from the data given on the graph which type of enzyme inhibition any is curring Series 1 - no inhibitor. Series 2 inhibitor present • Seriesi Series2 Linear (Series1) Linear (Series2) 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:...
Homework # 16: Enzymes Late assignment will be given a grade of "0. Due Date 1. An enzyme is primarily made out of a (hint what food group). catechol+ oxygen (0a) Catecholasepolyphenol 2. Loo...
Homework # 16: Enzymes Late assignment will be given a grade of "0. Due Date 1. An enzyme is primarily made out of a (hint what food group). catechol+ oxygen (0a) Catecholasepolyphenol 2. Looking at the equation above, the enzyme in this reaction is: 2. A. Catechol B. Oxygen C. Catecholase D. Polyphenol 3. Looking at the same equation as question 2, what is the substrate? A. Catechol B. Oxygen C. Catecholase D. Polyphenol What is the name of the...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point where the enzyme is working at its maximum rate (Vmax/2), and amount of substrate needed to bind half of the active sites (Km). Label these points on the graph. Vmax represents: Vm Vmax/2 represents: Reaction velocity v Vmax 2 Km represents: Kim Substrate concentration (5)
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but...
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but eventually reaches a maximum value, even though the concentration of substrate continues to increase. Which of the following best explains why? O As substrate concentration increases, the substrates preferentially bind with each other instead of the active site of the enzyme, and no additional catalysis occurs. As substrate concentration increases, the active sites of all the enzyme molecules become occupied with substrate molecules, and...
Km is: A. the concentration of an inhibitor needed to give 1/2 Vmax B. a measure...
Km is: A. the concentration of an inhibitor needed to give 1/2 Vmax B. a measure of the rate of product formation C. related to the affinity of the enzyme for its substrate D. a measure of the activation energy of the enzyme-catalyzed reaction E. the velocity equal to one-half of the maximum velocity
1 2 3 4 5 6 7 8 9 Part A Which of the following is/are...
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Part A Which of the following is/are means whereby a catalyst can lower the activation energy of a reaction? quantum tunneling decreasing the number of reactive molecules permanently binding substrates inefficient collisions altering the temperature within the cell to one appropriate for reactions to proceed Subrnit Request Answer Part A An enzyme Obinds substrates in a manner that facilitates the formation of product decreases the rate of a reaction. is always...
high and detecting one product at a time Question 77 The initial velocity of an enzyme...
high and detecting one product at a time Question 77 The initial velocity of an enzyme reaction (vo) describes A) The concentration of the enzyme at maximal velocity B) The concentration of substrate at maximal velocity C) The concentration of both at the start of the reaction D) The rate of the reaction when the substrate and enzyme are first med Question 78 What is the shape of a typical plot of initial rate vs substrate concentration tres kinetics? A)...
12. Which of the following statements is true of enzyme catalysts? A B C To be...
12. Which of the following statements is true of enzyme catalysts? A B C To be effective, they must be present at the same concentration as their substrate. They can increase the equilibrium constant for a given reaction by a thousand-fold or more. They lower the activation energy for conversion of substrate to product. Their catalytic activity is independent of pH. They are generally equally active on D and L isomers of a given substrate. D E 13. In competitive...
56. In the lock and key model of substrate binding to enzymes Pprat wnich they work best a the substrate changes its conformation to fit the active site b. the active site changes its conformation to fit the substrate c. the active site is rigid and the substrate must fit exactly d. the substrate binds only to part of the active site In the induced-fit model of substrate binding a. 57. the substrate changes its conformation to fit the active...
enzyme has a molar mass of 30 kilodatons. From this information, calculate Keat for this enzyme-catalyzed reaction both with and without inhibitor. Also explain from the data given on the graph which type of enzyme inhibition any is curring Series 1 - no inhibitor. Series 2 inhibitor present • Seriesi Series2 Linear (Series1) Linear (Series2) 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:...
Homework # 16: Enzymes Late assignment will be given a grade of "0. Due Date 1. An enzyme is primarily made out of a (hint what food group). catechol+ oxygen (0a) Catecholasepolyphenol 2. Looking at the equation above, the enzyme in this reaction is: 2. A. Catechol B. Oxygen C. Catecholase D. Polyphenol 3. Looking at the same equation as question 2, what is the substrate? A. Catechol B. Oxygen C. Catecholase D. Polyphenol What is the name of the...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point where the enzyme is working at its maximum rate (Vmax/2), and amount of substrate needed to bind half of the active sites (Km). Label these points on the graph. Vmax represents: Vm Vmax/2 represents: Reaction velocity v Vmax 2 Km represents: Kim Substrate concentration (5)
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but eventually reaches a maximum value, even though the concentration of substrate continues to increase. Which of the following best explains why? O As substrate concentration increases, the substrates preferentially bind with each other instead of the active site of the enzyme, and no additional catalysis occurs. As substrate concentration increases, the active sites of all the enzyme molecules become occupied with substrate molecules, and...
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Part A Which of the following is/are means whereby a catalyst can lower the activation energy of a reaction? quantum tunneling decreasing the number of reactive molecules permanently binding substrates inefficient collisions altering the temperature within the cell to one appropriate for reactions to proceed Subrnit Request Answer Part A An enzyme Obinds substrates in a manner that facilitates the formation of product decreases the rate of a reaction. is always...
high and detecting one product at a time Question 77 The initial velocity of an enzyme reaction (vo) describes A) The concentration of the enzyme at maximal velocity B) The concentration of substrate at maximal velocity C) The concentration of both at the start of the reaction D) The rate of the reaction when the substrate and enzyme are first med Question 78 What is the shape of a typical plot of initial rate vs substrate concentration tres kinetics? A)...
12. Which of the following statements is true of enzyme catalysts? A B C To be effective, they must be present at the same concentration as their substrate. They can increase the equilibrium constant for a given reaction by a thousand-fold or more. They lower the activation energy for conversion of substrate to product. Their catalytic activity is independent of pH. They are generally equally active on D and L isomers of a given substrate. D E 13. In competitive...
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