4.2 14. The Km of a steady-state equation was experimentally derived to be equal to 6.5 mM. If the rate constant for thedisappearance of the enzyme-substrate complex were both equal to 4.0 mM, which statement is TRUE about thisreaction?A. The enzyme-substrate complex is permanent.B. In principle, k2 has higher magnitude than k-1.C. The reaction is kinetically possible but unstable.D. The magnitude of ki is lower compared to k2.15. Template/lock and key theory of enzyme action is supported by which of the following?A. Enzymes speed up a reactionB. Enzymes determine the direction of a reactionC. Compounds similar to substrate inhibit enzyme activityD. Enzymes have absolute specificity to a certain substrate onlyE. Enzymes occur in living beings and speed up certain reactions

The formation of an enzyme-substrate complex is the first step in enzymatic catalysis. The enzyme…

15. Template/lock and key theory of enzyme action is supported by which of the following? A. Enzymes speed up a reaction B. Enzymes determine the direction of a reaction C. Compounds similar to substrate inhibit enzyme activity D. Enzymes have absolute specificity to a certain substrate only E. Enzymes occur in living beings and speed up certain reactions

15. Template/lock and key theory of enzyme action is supported by which of the following? A. Enzymes speed up a reaction B. Enzymes determine the direction of a reaction C. Compounds similar to substrate inhibit enzyme activity D. Enzymes have absolute specificity to a certain substrate only E. Enzymes occur in living beings and speed up certain reactions

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 6TYK: Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent...

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Similar questions

In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.
Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent bonding with the substrate at their active site b. bringing reacting molecules into close prosimity c. orienting reactants into positions to favor transition states d. changing charges on reactants to hasten their reactivity e. increasing fit of enzyme and substrate that reduces the energy of activation
Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
1. Can you describe how electrostatic and steric considerations may lead to preferential stabilization of the transition state at an enzyme active site? 2. What factors are involved in “transition-state complementarity”?
4 In a reaction system, the concentrations of Enzyme-Substrate complex (ES), free enzyme [E] and free substrate [S] are 5mM, 2mM and 45 mM respectively. If the enzyme has 5 identical binding sites for this substrate, then calculate the value of Equilibrium Association constant (Ka)
1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?
1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? Explain
1. What is the difference between the lock and key model in the induced fit model enzyme-substrate binding? 1a. What factors affect an enzymes catalytic function?
1. A. Estimate from the graph what the Vmax is for the enzyme without inhibitor present (black circles) and in the presence of the inhibitor (green squares). B. Estimate the Km from the graph without inhibitor present (black circles) and in the presence of the inhibitor (green squares). C. Based on the data, what type of reversible inhibitor do you think was used? Explain your answer.
5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop a
1 what is does the induced -fit model account for? 2 why are most enzyme inactive at higher temperature ( greater than 37degree Celsius) 3 Does this happen to all enzymes in all species? 4 What are the formulas for the reduced form of the coenzymes?
1) Is the ratio of the forward rate constant and reverse rate constant changed by the presence of an enzyme catalyst? 2) 4) What is the simplest mathematical relationship between substrate concentrations [S], initial velocity (Vo) of an enzyme catalyzed reaction, the maximal velocity of the reaction (Vmax), and the ½ maximal Vo (i.e. Km) ? (Hint: what is the Michaelis-Menten Equation? 3) Graphically illustrate the most useful derivation of the Michaelis-Menton equation (that darn linearized, double-reciprocal)