EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
7th Edition
ISBN: 8220100853180
Author: STOKER
Publisher: CENGAGE L
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Chapter 21, Problem 21.32EP
(a)
Interpretation Introduction
Interpretation: The meaning of the notation “S” in the given equation has to be stated.
Concept introduction: The binding of the substrate to the active site of the enzyme results in the formation of enzyme-substrate complex. The catalysis of enzyme-substrate complex produces enzyme-product complex. It dissociates to give free enzyme and product.
(b)
Interpretation Introduction
Interpretation: The meaning of the notation “EP” in the given equation has to be stated.
Concept introduction: The binding of the substrate to the active site of the enzyme results in the formation of enzyme-substrate complex. The catalysis of enzyme-substrate complex produces enzyme-product complex. It dissociates to give free enzyme and product.
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Although graphical methods are available for accurate determination of the Vmax and Km of an enzyme-catalyzed reaction, sometimes these quantities can be quickly estimated by inspecting values of V0 at increasing [S]. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the following data were obtained:
You have obtained experimental kinetic data for two versions of the same enzyme, a wild‑type and a mutant differing from the wild‑type at a single amino acid. The data are given in the table.
Compare the kinetic parameters of the two versions using the data in the table.
Assuming a two-step reaction scheme in which ?−1 is much larger than ?2, which of the following statements are correct?
The mutant version has a higher affinity for the substrate.
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The wild‑type version has a higher affinity for the substrate.
The mutant version requires a greater concentration of substrate to achieve ?maxVmax.
Calculate the initial velocity of the reaction catalyzed by the wild‑type enzyme when the substrate concentration is 10 mM.
The reaction equilibrium is reached once there is no net change in the concentration of the substrate or the product.
Based on the data table and your initial…
In enzyme kinetics, for the reversible with two central complexes mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicate forward direction while the variables denoted with b indicate backward direction.
Chapter 21 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
Ch. 21.1 - Which of the following statements concerning the...Ch. 21.1 - Prob. 2QQCh. 21.2 - Which of the following statements about a...Ch. 21.2 - Which of the following statements about cofactors...Ch. 21.2 - Prob. 3QQCh. 21.3 - Which of the following statements concerning an...Ch. 21.3 - Prob. 2QQCh. 21.3 - Which of the following pairings of enzyme type and...Ch. 21.3 - Which of the following pairings of enzyme type and...Ch. 21.4 - Prob. 1QQ
Ch. 21.4 - Which of the following statements concerning the...Ch. 21.4 - Prob. 3QQCh. 21.5 - The specificity of an enzyme that catalyzes the...Ch. 21.5 - Prob. 2QQCh. 21.6 - The number of substrate molecules converted to...Ch. 21.6 - Prob. 2QQCh. 21.6 - Prob. 3QQCh. 21.7 - Extremozyme presence is not possible in which of...Ch. 21.7 - Prob. 2QQCh. 21.8 - Prob. 1QQCh. 21.8 - Prob. 2QQCh. 21.8 - Prob. 3QQCh. 21.9 - Prob. 1QQCh. 21.9 - Prob. 2QQCh. 21.9 - Prob. 3QQCh. 21.10 - Prob. 1QQCh. 21.10 - Prob. 2QQCh. 21.11 - Prob. 1QQCh. 21.11 - Prob. 2QQCh. 21.12 - Prob. 1QQCh. 21.12 - Prob. 2QQCh. 21.12 - Prob. 3QQCh. 21.13 - Prob. 1QQCh. 21.13 - Prob. 2QQCh. 21.13 - In the recharging of a metal-containing enzyme by...Ch. 21.14 - Prob. 1QQCh. 21.14 - Prob. 2QQCh. 21.14 - Prob. 3QQCh. 21.14 - Which of the B vitamins has a name that draws...Ch. 21.14 - Prob. 5QQCh. 21.14 - Prob. 6QQCh. 21.15 - Prob. 1QQCh. 21.15 - Prob. 2QQCh. 21.15 - Prob. 3QQCh. 21.15 - For which of the following vitamins is blood...Ch. 21.15 - Prob. 5QQCh. 21 - What is the general role of enzymes in the human...Ch. 21 - Why does the body need so many different enzymes?Ch. 21 - Prob. 21.3EPCh. 21 - Prob. 21.4EPCh. 21 - Indicate whether each of the following phrases...Ch. 21 - Indicate whether each of the following phrases...Ch. 21 - Explain why a metal ion can function as a cofactor...Ch. 21 - Prob. 21.8EPCh. 21 - Prob. 21.9EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Prob. 21.11EPCh. 21 - Based on its name, indicate whether each of the...Ch. 21 - Predict the function of each of the following...Ch. 21 - Predict the function of each of the following...Ch. 21 - Prob. 21.15EPCh. 21 - Prob. 21.16EPCh. 21 - Prob. 21.17EPCh. 21 - Suggest a name for an enzyme that catalyzes each...Ch. 21 - Prob. 21.19EPCh. 21 - Prob. 21.20EPCh. 21 - To which of the six major classes of enzymes does...Ch. 21 - To which of the six major classes of enzymes does...Ch. 21 - Identify the enzyme needed in each of the...Ch. 21 - Identify the enzyme needed in each of the...Ch. 21 - Prob. 21.25EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Indicate whether each of the statements in Problem...Ch. 21 - Indicate whether each of the statements in Problem...Ch. 21 - Prob. 21.29EPCh. 21 - Prob. 21.30EPCh. 21 - Prob. 21.31EPCh. 21 - Prob. 21.32EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Indicate whether each of the following statements...Ch. 21 - Prob. 21.35EPCh. 21 - Prob. 21.36EPCh. 21 - Prob. 21.37EPCh. 21 - Prob. 21.38EPCh. 21 - What type of specificity (absolute, group,...Ch. 21 - What type of specificity (absolute, group,...Ch. 21 - The following graph shows the relationship between...Ch. 21 - Based on the graphical information in Problem...Ch. 21 - Prob. 21.43EPCh. 21 - Based on the graphical information in Problem...Ch. 21 - Prob. 21.45EPCh. 21 - Prob. 21.46EPCh. 21 - Draw a graph that shows the effect of increasing...Ch. 21 - Prob. 21.48EPCh. 21 - Prob. 21.49EPCh. 21 - What is an enzyme turnover number?Ch. 21 - Describe the effect that each of the following...Ch. 21 - Describe the effect that each of the following...Ch. 21 - What is an extremophile?Ch. 21 - What are two common environmental settings where...Ch. 21 - Indicate whether each of the following pairings of...Ch. 21 - Indicate whether each of the following pairings of...Ch. 21 - Prob. 21.57EPCh. 21 - What type(s) of extremophiles are used in oil well...Ch. 21 - Prob. 21.59EPCh. 21 - Prob. 21.60EPCh. 21 - Prob. 21.61EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Prob. 21.63EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Prob. 21.65EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Prob. 21.67EPCh. 21 - Prob. 21.68EPCh. 21 - Prob. 21.69EPCh. 21 - Prob. 21.70EPCh. 21 - Prob. 21.71EPCh. 21 - Prob. 21.72EPCh. 21 - Prob. 21.73EPCh. 21 - Prob. 21.74EPCh. 21 - Prob. 21.75EPCh. 21 - Prob. 21.76EPCh. 21 - Prob. 21.77EPCh. 21 - Prob. 21.78EPCh. 21 - Prob. 21.79EPCh. 21 - Prob. 21.80EPCh. 21 - Prob. 21.81EPCh. 21 - Prob. 21.82EPCh. 21 - What is the medical diagnostic value associated...Ch. 21 - Prob. 21.84EPCh. 21 - Indicate whether each of the following is a...Ch. 21 - Indicate whether each of the following is a...Ch. 21 - Prob. 21.87EPCh. 21 - Prob. 21.88EPCh. 21 - Prob. 21.89EPCh. 21 - Prob. 21.90EPCh. 21 - Prob. 21.91EPCh. 21 - What are the structural differences between the...Ch. 21 - Prob. 21.93EPCh. 21 - Prob. 21.94EPCh. 21 - Vitamin C is biosynthesized in a two-step process....Ch. 21 - Prob. 21.96EPCh. 21 - Prob. 21.97EPCh. 21 - Prob. 21.98EPCh. 21 - Prob. 21.99EPCh. 21 - Prob. 21.100EPCh. 21 - Which of the B vitamins has a structure that fits...Ch. 21 - Which of the B vitamins has a structure that fits...Ch. 21 - Prob. 21.103EPCh. 21 - Prob. 21.104EPCh. 21 - Prob. 21.105EPCh. 21 - Prob. 21.106EPCh. 21 - The coenzyme forms of B vitamins are involved in...Ch. 21 - The coenzyme form of B vitamins are involved in...Ch. 21 - Prob. 21.109EPCh. 21 - What is the relationship between the plant pigment...Ch. 21 - Prob. 21.111EPCh. 21 - List four major functions of vitamin A in the...Ch. 21 - Prob. 21.113EPCh. 21 - Prob. 21.114EPCh. 21 - Prob. 21.115EPCh. 21 - Prob. 21.116EPCh. 21 - Prob. 21.117EPCh. 21 - Prob. 21.118EPCh. 21 - Prob. 21.119EPCh. 21 - Prob. 21.120EPCh. 21 - Which structural form of vitamin E exhibits the...Ch. 21 - Prob. 21.122EPCh. 21 - Prob. 21.123EPCh. 21 - Prob. 21.124EPCh. 21 - Prob. 21.125EPCh. 21 - Prob. 21.126EPCh. 21 - Prob. 21.127EPCh. 21 - Prob. 21.128EPCh. 21 - Prob. 21.129EPCh. 21 - Prob. 21.130EPCh. 21 - Prob. 21.131EPCh. 21 - Which vitamin or vitamins has (have) each of the...Ch. 21 - Which of the 13 vitamins has a structure that fits...Ch. 21 - Prob. 21.134EP
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- what is the purpose of staggering the start and stop of the reactions? With reference to your experimental protocol, what is the purpose of staggering the start and stop of the reactions? A.To ensure that the reaction occurs with different amounts of enzyme in each tube so as to ensure comparability between reaction tubes. B.To ensure that the reaction occurs at exactly the same pH in each tube so as to ensure comparability between reaction tubes. C.To ensure that the reaction occurs for exactly the same time interval (30 minutes) in each tube so as to ensure comparability between reaction tubes. D.To ensure that the reaction occurs with exactly the same amount of substrate in each tube so as to ensure comparability between reaction tubes.arrow_forwardMost of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: (a) Lineweaver-Burk equation is a manipulation of the Michaelis-Menten equation. Give the equation and state why it is necessary. (b) Is high or low Vmax preferable for an enzyme reaction? Give reason.arrow_forwardThe enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose 6-phosphate. After the reactants and products were mixed and allowed to reach equilibrium at 25°C, the concentration of glucose 1-phosphate was 4.5 mM and that of glucose 6-phosphate was 86 mM. Calculate Keq' and AG for this reaction. The reaction coordinate diagram for an enzyme-catalyzed reaction is shown below. How many transition states and intermediates are in the reaction? Is the reaction thermodynamically favorable? Which step is the rate-determining step of the reaction? G Reaction coordinatearrow_forward
- Given the following data in enzyme-catalyzed reaction, what are the Vm, Km of with DEDS (presence of inhibitor) and without DEDS ( absence of inhibitor) and its type of inhibition.arrow_forwardMost of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: Give the Michaelis-Menten equation of an enzyme reaction and draw the Michaelis-Menten plot of [S] versus V0.arrow_forwardIn enzyme kinetics, for the reversible with one complex mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicates forward direction while the variables denoted with b indicate backward direction.arrow_forward
- An enzyme has a single active site at which it can bind and hydrolyze either X or Y; however, the enzyme cannot bind X and Y at the same time. Answer the following questions regarding the Km and Vmax of this enzyme. (a) Will the Km for X be affected if Y is present in the reaction mixture? Explain. (b) Will Vmax for X be affected if Y is present in the reaction mixture? Explain. (a) No, X competes with Y for binding, so the apparent Km for X will stay the same. (b) Yes, the Vmax for X will decrease in the presence of Y. (a) No, Y does not compete with X for binding, so the apparent Km for X will stay the same. (b) No, the Vmax for X will be unaffected by the presence of Y.arrow_forwardThe total concentration of enzyme in a reaction, [E], is made up of the concentration of enzyme bound to substrate, [ES], and the concentration of enzyme still free in solution, [Ef]. Similarly, the total amount of substrate is made up of [Sf] and [ES]. We can assume that the concentration of enzyme is much less than that of the substrate, [E] << [S]. Assuming the steady state condition and the relationships between [E], [Ef] and [ES], and similar ones for S, given in lectures, derive an expression for the saturation factor, , in terms of [S] and . (Note that [E] and [S] denote the total amounts of enzyme and substrate added to the reaction, respectively. You may assume that [S]>>[E].)arrow_forwardKM is determined by measuring the reaction velocity of two enzymes (X and Y) at different concentrations. The curves for X and Y were sigmoid and hyperbolic, respectively. How are these graphs different, and why?arrow_forward
- The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] Km + [S] where v is the velocity, or rate, Vmax is the maximum velocity. K is the Michaelis-Menten constant, and [S] is the substrate concentration. A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (ro) at different substrate concentrations ([S]). First, move the line labeled Vmax to a position that represents the maximum velocity of the enzyme. Next, move the line labeled 1/2 Vmax to its correct position. Then, move the line labeled Km to its correct position. Estimate the values for Vmax and Km- Vmax= µM/min v (µM/min) 300 275 250 225 200 175 150 125 100 75 50 Km = 25 K 0 10 20 30 V max 40 50 [S] (M) 1/2 V max Michaelis-Menten curve 60 70 80 90 100 HMarrow_forwardIn a bisubstrate reaction, a small amount of the fi rst product P is isotopicallylabeled (P*) and added to the enzyme and the fi rst substrate A. No B or Q is present. Will A (= P—X) become isotopically labeled (A*) if the reaction follows a Ping Pong mechanism?arrow_forwardThe following reactions were catalyzed by an enzyme that follows the Michaelis-Menten mechanism in the absence and presence of inhibitor (10mM). Assume [E]T is the same for each reaction. Determine K, and/or K'. [S] (mM) Uninhibited v (um/s) Inhibited v. (um/s) 1 3 1.67 2 4.5 2.6 6.8 4.5 10 8.1 6.2 20 9.5 7.7arrow_forward
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