Biology
5th Edition
ISBN: 9781260487947
Author: BROOKER
Publisher: MCG
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Chapter 6, Problem 3TY
Summary Introduction
Introduction: The equilibrium constant of a particular
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Question 23
An enzyme has a single active site at which it can bind and hydrolyze either X or
Y but the enzyme cannot bind X and Y at the same time. Which of the following
statements are TRUE?
Multiple answers: Multiple answers are accepted for this question
Select one or more answers and submit. For keyboard navigation... SHOW MORE V
The Km for X will be affected if Y is present in the reaction mixture.
a
Y is a competitive inhibitor of X.
The Km for X will increase.
d.
The V for X will be affected if Y is present in the reaction mixture.
max
pH dependence of Vmax reflects the ionization state of catalytic site
e
residues.
Consider the following: X and Y are methanol (poisonous) and ethanol
respectively. If the Km for X = 0.01 M and the Km for Y = 0.001 M then
0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax.
Addition of an enzyme to a chemical reaction increases the ratio of
g
products to reactants (Keg).
What terms would best describe the above coupled reaction?A. it is non-spontaneous and endothermic (because the overall Go is positive)B. it is spontaneous and exothermic (because the overall Go is positive)C. it is non-spontaneous and exothermic (because the overall Go is positive)D. it is spontaneous and exothermic (because the overall Go is negative)E. it is non-spontaneous and endothermic (because the overall Go is negative)
For the following first-order liquid-phase reversible reaction, where initially only
reactant A is present:
k₁
AR,
k2
Equilibrium constant: K
1) Express the equilibrium conversion rate, Xe, using K, and demonstrate that Xe can
be determined using thermodynamic data.
2) Show how the rate constants kl and k2 can be determined experimentally.
Chapter 6 Solutions
Biology
Ch. 6.1 - Which do you think has more entropy, a NaCl...Ch. 6.1 - Prob. 2CCCh. 6.2 - Prob. 1CCCh. 6.2 - Prob. 2CCCh. 6.2 - Prob. 1CSCh. 6.2 - Prob. 1EQCh. 6.2 - Prob. 2EQCh. 6.2 - Prob. 3EQCh. 6.3 - Prob. 1CSCh. 6.3 - Prob. 2CS
Ch. 6.4 - What are advantages of protein degradation?Ch. 6 - Reactions that release free energy are a....Ch. 6 - Enzymes speed up reactions by a. providing...Ch. 6 - Prob. 3TYCh. 6 - Researchers analyzed a cell extracta mixture of...Ch. 6 - In biological systems, ATP functions by a....Ch. 6 - In a chemical reaction, NADH is converted to NAD+...Ch. 6 - Prob. 7TYCh. 6 - Prob. 8TYCh. 6 - Prob. 9TYCh. 6 - Autophagy provides a way for cells to a. degrade...Ch. 6 - Prob. 1CQCh. 6 - Prob. 2CQCh. 6 - Prob. 3CQCh. 6 - Prob. 1COQCh. 6 - Prob. 2COQ
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- Fill in the blanks: Write Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct, Mif both statements are incorrect. A. The Michaelis-Menten plot shows that initially, the increase in the reaction velocity is relatively fast. B. Then after sometime, the change in the reaction velocity slows down and tapers off to a certain limit.arrow_forwardWhat are the benefits of measuring the initial rate of a reaction Vå for use in kinetic studies? (This is a multi-select question). [ES] can be measured accurately. changes in [S] are negligible, so the value of [S] is known. changes in Km are negligible, so Km can be treated as a constant. V₁ = Vmax. --> A negligible amount of product has formed, so that the back reaction P -- need not be considered. ESarrow_forwardWhich of the following statements about a plot of V0 vs. [S] for an enzyme that follows Michaelis-Menten kinetics is false? a. As [S] increases, the initial velocity of reaction V0 also increases. b. At very high [S], the velocity curve becomes a horizontal line that intersects the y-axis at Km. c. Km is the [S] at which V0 = 1/2 Vmax. d. The shape of the curve is a hyperbola. e. The y-axis is a rate term with units of μm/min.arrow_forward
- ver is given. A +B C+ D 1) Calculate AG for the above react un and indicáte whether the reaction is favorable or unfavorable [A] = 0.9 M 20°C AG° = 4 KJ/mol %3D [B] = 15mM [C] = 4mM [D] = 3 M R= 8.314 J/moleK %3D %3D 4.7 and explain how you know.arrow_forwardConsider the analogy of the jiggling box containing coins that was described on page 85. The reaction, the flipping of coins that either face heads up (h) or tails up (T), is described by the equation h ↔ T, where the rate of the forward reaction equals the rate of the reverse reaction.a. What are ΔG and ΔG° in this analogy? b. What corresponds to the temperature at which the reaction proceeds? What corresponds to the activation energy of the reaction? assume you have an “enzyme,” called jigglase, which catalyzes this reaction. What would the effect of jigglase be and what, mechanically, might jigglase do in this analogy?arrow_forwardBased on the definition of kcat, substitute a value that can be measured and yet still represents the value associated with the original concentration of the R. What would the rate or velocity of the reaction be equal to under these circumstances? How can cells increase Vmax? What variable that we could change would directly impact Vmax? Would the value of KM be affected by the ways you determined that Vma,x could be increased? What does this indicate about KM? Thinking about how catalysts work, about the Michaelis-Menten Equation, and the definition of kcat, what specifically does the enzyme change in the reaction mechanism to increase the rate? If an enzyme follows the 2 step mechanism proposed by Michaelis-Menten, what do you know about this enzyme? Be very specific and comprehensive. Please answer very soon will give rating surelyarrow_forward
- During a test of kinetics of an enzyme-catalyzed reaction, the following data were recorded: a. Determine the Michaelis-Menten constant for the reaction with no inhibitor present at 30 °C and at 49.6 °C. b. Determine the maximum velocity of the uninhibited reaction at 30 °C and an enzyme concentration of 1.6 g/L. c. Determine the Ki for the inhibitor at 30 °C and decide what type of inhibitor is being used.arrow_forwardFor the following reaction X + YA + B at 300 K, it is found equilibrium constant equal to 10. Therefore, AG & AGⓇ of the reaction at 300 K respectively are - Answer barrow_forwardThe enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"arrow_forward
- Potassium nitrate is widely used in industries. The reaction for the industrial production of KNO3 is summarized in the equation below; 4KCl + 4 HNO3 + O2 → 4 KNO3 + 2 Cl2 + 2 H2O Which of the following statements below is correct about the production of KNO3? a. A redox reaction; KCl is a reducing agent and O2 is an oxidizing agent b. A redox reaction; HNO3 is a reducing agent and Cl is an oxidizing agent c. Not a redox reaction d. A redox reaction; KCl is a reducing agent and KNO3 is an oxidizing agent e. A redox reaction; HNO3 is a reducing agent and KNO3 is an oxidizing agentarrow_forwardch Select all statements that are correct. Note there might be more than 1 correct statement. From the Lineweaver-Burk plot the equilibrium constant (Keq) can be obtained The Lineweaver-Burk plot gives a more accurate prediction for Vmax than the Michaelis- Menten plot The Lineweaver-Burk plot assumes that products and reactants are present at equal concentrations during the entire time of the reaction The Lineweaver-Burk plot shows velocity of reaction vs substrate concentration The Lineweaver-Burk plot shows 1/velocity of reaction vs 1/substrate concentration O 20°C D) // Earrow_forwardif the reaction given below occurs and pure A and B were mixed, which of the following would take place as equilibrium was established A + B ⇌ C a. the concentration of C would increase for a time, then remain constant b. the concentration of A would increase for a time, then decrease c. the concentration of B would increase for a time, then remain constantarrow_forward
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