BIOLOGY 2E
2nd Edition
ISBN: 9781506699851
Author: OpenStax
Publisher: XANEDU PUBLISHING
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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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Is the dependent variable the reaction time? And what is the controlled variables in this experiment and are there any controls that are used in this experiment?
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
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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/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_forwardIn 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_forward
- On 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_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_forwardFor an experiment where you use different concentrations of catalase to determine how that affects rate of the reaction with its substrate, hydrogen peroxide, what effect does enzyme concentration have on reaction activity? Would it be possible to have too much catalase in the tube? What would happen?arrow_forward
- Hello can someone please help me graph 1&2 and help find the vmax and kmarrow_forwardchoices for first blank (protonater,deprotonated) 2nd blank (higher,lower,same) 3rd blank (10,50,90,100) 4th blank (allowed from, excluded in)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_forwardWhich model for enzyme-substrate chemical complementarity is described by the following: Before substrate binding, some enzyme molecules have active sites complementary to substrates and other enzyme molecules have non-complementary active sites. Substrate molecules preferentially bind to the enzyme molecules with complementary active sites. Non-complementary enzyme molecules undergo a structural change to become complementary to maintain conformational equilibrium. a) conformational selection b) induced fit c) lock and key...arrow_forwardDescribe the two models that explain the behavior of allosteric enzymes. Include thelimitation or advantage of each. Give also an example of each.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License