9 The G° of the reaction of reactant X to product Y is the same in its catalytic reaction and the uncatalyzed reaction. Which ofthe following is false?Catalysts does not affect the concentrations of X and Y at equilibrium.O The time it takes for both reactions to reach equilibrium is the sameA small difference in GO means a small difference in relative amounts of X and Y at equilibrium.A large difference in G° means a large difference in relative amounts of X and Y at equilibrium.

Enzymes are protein molecules that catalyze the biological reactions inside the cell. Enzymes do not…

Answered: The G° of the reaction of reactant X to…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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For the reaction B A at standard conditions with [B] =1 M and [A] =1 M, AG is initially a large negative number. As the reaction proceeds, [B] decreases and [A] increases until the system reaches equilibrium. How do the values of AG and AG" change as the reaction moves toward equilibrium? both AG and AG stay the same O AG reaches zero and AG" becomes more negative AG becomes less negative and AG" stays the same AG stays the same and AG becomes less negative AG becomes positive and AG" becomes positive
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).
Which one of the following statements is completely TRUE? O When AG > 0, the reaction is BOTH product-favored (spontaneous) AND endergonic. When AG 0, the reaction is BOTH reactant-favored (nonspontaneous) AND endergonic. When AG > 0, the reaction is BOTH product-favored (spontaneous) AND exergonic. When AG > 0, the reaction is BOTH reactant-favored (nonspontaneous) AND exergonic. When AG < 0, the reaction is BOTH reactant-favored (nonspontaneous) AND exergonic.
For 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 b
if 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 constant
Based 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 surely
The enzyme -catalyzed reaction ratewill be increased if the energy level of ES can be increased by all EXCEPT: destabilization of ES by strain loss of entropy due to binding of E and S. destabilization of ES by distortion destabilization of ES by solvation destabilization of ES by electrostatic effects a. b. с. d. е.
Which of the following statements are true for BOTH the "transition state" and an "intermediate" of reaction? (This is a multi-select question, select all that apply.). Both are only observed in enzyme-catalyzed reactions. Both can be converted to product(s) or might decompose back to the reactant(s). Neither are part of the "net equation" for the reaction. Both contain covalent bonds are in the process of breaking and/or forming. Both are part of every chemical reaction. (i.e. the mechanisms of all chemical reactions, whether enzyme catalyzed or not, will have involve both a transition state and an intermediate).
For a given reaction, CH3CHO+1/202 --> CH3COOH; the oxidizing agent is 002 O None of the above Осн сно OCH3COOH
An enzyme catalyzes a reaction with a K of 7.50 mM and a Vmax of 4.15 mMs. Calculate the reaction velocity, o, for each substrate concentration. [S] = 1.75 mM MM-s-1 [S] = 7.50 mM [S] = 11.0 mM DO mM-s mM-s
Which of the following statements regarding Michaelis-Menten kinetics is TRUE? The ES complex can move toward product or toward substrate. As Vmax is approached, KM approaches 1. Vmax is reached when [S] is low. When Vmax is reached, the concentration of the E is high.
A particular reaction has a ΔG‡ of 37.0 kJ mol-1. In the presence of an enzyme, the same reaction has a ΔG‡ of 5.70 kJ mol-1. Calculate the value of ΔΔG‡ in kJ mol-1.

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