Biology 2e
2nd Edition
ISBN: 9781947172517
Author: Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher: OpenStax
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Textbook Question
Chapter 6, Problem 15RQ
Which of the following analogies best describes the induced-fit model of enzyme-substrate binding?
- a hug between two people
- a key fitting into a lock
- a square peg fitting through the square bole and a round peg fitting through the round hole of a children’s toy
- the fitting together of two jigsaw puzzle pieces
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Students have asked these similar questions
In the following example an enzyme is being inhibited. This is an example of
Active site Inhibitor
Altered active site
O Non-competitive inhibition
O Competitive inhibition
MacBook Air
An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided.
Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots
Calculate the following:
Km of enzyme in the reaction without inhibitor
Km' of the enzyme in the reation with inhibitor
Vmax of the uninhibited reaction
Vmax of the inhibited reaction
What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.
Which of the following statements regarding enzymes and transition states is true?
stabilization of the transition state must be less than stabilization of ES for
catalysis to occur
binding of substrate to an enzyme often causes strain, thus promoting transition
state formation
the transition state conformation of an enzyme catalyzed reaction is identical to the
conformation seen in the uncatalyzed transition state
formation of the transition state always assures that the reaction will proceed to
product
none of the above are true
Chapter 6 Solutions
Biology 2e
Ch. 6 - Figure 6.8 Look at each of the processes shown,...Ch. 6 - Figure 6.10 If no activation energy were required...Ch. 6 - Figure 6.14 The hydrolysis of one ATP molecule...Ch. 6 - Energy is stored long-term in the bonds of and...Ch. 6 - DNA replication involves unwinding two strands of...Ch. 6 - Consider a pendulum swinging. Which type(s) of...Ch. 6 - Which of the following comparisons or contrasts...Ch. 6 - Which of the following is the best way to judge...Ch. 6 - Which of the following is not an example of an...Ch. 6 - In each of the three systems, determine the state...
Ch. 6 - The energy released by the hydrolysis of ATP is...Ch. 6 - Which of the following molecules is likely to have...Ch. 6 - Which of the following is not true about enzymes...Ch. 6 - An allosteric inhibitor does which of the...Ch. 6 - Which of the following analogies best describes...Ch. 6 - Does physical exercise involve anabolic and/or...Ch. 6 - Name two different cellular functions that require...Ch. 6 - Explain in your own words the difference between a...Ch. 6 - Describe the position of the transition state on a...Ch. 6 - Imagine an elaborate ant farm with tunnels and...Ch. 6 - Energy transfers take place constantly in everyday...Ch. 6 - Do you think that the Ea for ATP hydrolysis is...Ch. 6 - With regard to enzymes, why are vitamins necessary...Ch. 6 - Explain in your own words how enzyme feedback...
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- An experiment on enzyme-catalyzed reaction was conducted in the laboratory by a student. Results obtained are summarized in the table below. In all the experiments, the concentration of the enzyme is the same. Substrate Concentration Velocity (pmol) (pmol/min) 1.5 0.21 0.28 4 0.32 6 0.36 0.4 15 0.45 18 0.47 1. Plot or graph these results using the Lineweaver-Burk method. 2. Determine the Km and Vmax values. Show all equations and calculations.arrow_forwardAn experiment on enzyme-catalyzed reaction was conducted in the laboratory by a student. Results obtained are summarized in the table below. In all the experiments, the concentration of the enzyme is the same. Substrate Concentration Velocity (pmol/min) (pmol) 1.5 0.21 3 0.28 4 0.32 0.36 8 0.4 15 0.45 18 0.47 1. Plot or graph these results using the Lineweaver-Burk method. 2. Determine the KM and Vmax values. Show all equations and calculations.arrow_forwardThe figure displays the relationship between initial rate of product formation and reactant concentration in an enzyme-catalyzed reaction with a fixed amount of enzyme. Which of the following statements best explains the shape of the rate curve at high reactant concentration?arrow_forward
- In the scheme below which represents the mechanism of action for a large number of enzymes: A+B⟺AB⟶C The steady state approximation is reached when: d[AB]/dt≈0 k2≫k1 k−1≫k1 k−1=k1arrow_forwardAn allosteric enzyme that follows the concerted mechanism has a T/R ratio of 500 in the absence of substrate. Suppose that a mutation reversed the ratio. How would this mutation affect the relation between the rate of the reaction and substrate concentration? The mutant enzyme would behave like an enzyme that obeys Michaelis Menton kinetics. The mutant enzyme would have a smaller vmax There would be no difference in the mutant enzyme in terms of substrate binding and catalysis. More than one answer is correct. The mutant enzyme would display cooperativity more than the wild type. MacBook Air 888 F5 F4 F3 F2 %23 2$ %arrow_forwardData from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these values with assays run without inhibitor are used to understand how the inhibition is occurring. This is useful for better understanding the active site as well as the practical aspect of pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of inhibitors. Comnetitive Uncomnetitive Mixed +Inh +Inh 4Inh Anh Inh Anh [S] [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed c. For each situation in Model 1, consider an inhibitor that is better than the one shown on the graph. Answer the following questions for each type of inhibition: i. How would the KmPP change? ii. How would the Vmax PP change?arrow_forward
- Which of the following statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.arrow_forwardOn the figure below are shown three Lineweaver-Burk plots for enzyme reactions that have been carried out in the presence, or absence, of an inhibi- tor. Indicate what type of inhibition is predicted based on each Lineweaver- Burk plot. For each plot indicate which line corresponds to the reaction without inhibitor and which line corresponds to the reaction with inhibitor present. 1 1 1 [S] [S] [S]arrow_forwardWhich of the following statements regarding enzyme catalysis is false? All options are false. Once formed, the transition state slowly proceeds to forming the product at a rate determined by cofactor binding The free energy of binding of the enzyme to the transition state is more favorable than the free energy of binding of the enzyme to the substrate The substrate and active site of the enzyme are solvated to promote enzyme-substrate interaction Once formed, the product dissociates from the enzyme after ATP hydrolysis in order to regenerate the active sitearrow_forward
- using the method for experiment below and the table conduct 1 graph of the different factors vs rate of enzyme activity. The experiment began by preparing a hot water bath by boiling water and an ice water bath using ice in a 400 mL beaker. In the control group, 2 mL of 3% H2O2 was placed in a test tube and a pinch of MnO2 was added. The rate of this reaction was assigned as 5, and the production of bubbles in millimeters (mm) was noted. The reaction was considered complete when no more bubbles were produced. Another control group was set up by placing 2 mL of 3% H2O2 in a test tube and adding a pinch of sand, with the rate of reaction assigned as 0. To investigate the difference between plant and animal catalase, 2 mL of H2O2 was added to a test tube and a small piece of fresh liver was added. The rate of reaction between 0-5 was noted, along with the production of bubbles in mm. The same procedure was repeated using a small piece of fresh potato. Next, the effect of…arrow_forwardThe line does not cross the X-axis when the Y-variable is equal to zero 1점 because * Why does this line not start exactly at (0,0)? Rate of Reaction Enzyme Concentration the low concentration of enzyme is still enough to catalyze some reaction some small amount of product can be formed even without the enzyme present some small amount of product can be formed even without any product the pH was changedarrow_forwardA multi-enzyme complex Is made up of three polypeptide chains, A, B and C. A is associated with decarboxylase activity; B is a transacetylase, while C is a dehydrogenase. When the protein was placed in a nonpolar solvent, then run in PAGE, two protein bands were observed. Enzyme assays showed that one protein band exhibited decarboxylase activity while the other has both transacetylase and dehydrogenase activities. When the protein was also placed in an aqueous solvent at pH 5.0, then run in electrophoresis, two protein bands were also detected. Further enzyme assays also showed that one protein band exhibits transacetytase activity while the other has both decarboxylase and dehydrogenase activities. a. What types of non-covalent interactions are possible between A, B and C? b. Addition of urea, a reducing agent gave 4 bands in the PAGE profile with a subsequent loss of decarboxylase activity. What could be the reason for the observed result? Explain briefly in terms of the structure…arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License