Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all thestatements that are true.WithoutenzymeWithenzymeA+BTimeABOa. The reaction is now spontaneous due to the addition of enzymeb. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reactionO C. The reaction is exergonicO d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to theuncatalyzed reactione. The enzyme stabilizes the transition state for the reactionReleased Energypes

Those proteins or biological catalysts which help to speed up the chemical reaction are termed…

Answered: Consider the following free energy…

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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Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB O a. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O b. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction O c. The enzyme stabilizes the transition state for the reaction Od. The reaction is exergonic е. The reaction is now spontaneous due to the addition of enzyme Released Energy
A biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme B
Which of the following is TRUE concerning the induced fit model of enzyme catalysis? * (One correct answer only) A. The active site can be influenced by molecules binding elsewhere on an enzyme B. The initial binding of enzyme and substrate is the most tightly bound conformation C. The induced fit must occur prior to the initial binding of enzyme and substrate in order for the reaction to proceed D. The binding of enzyme and substrate is weakest in the transition state
If a competitive inhibitor of an enzyme is added to the mixture of the enzyme and its substrate, the inhibitor will: O a. decrease the value of Vmax for the chemical reaction catalyzed by this enzyme O b. decrease the value of KM for the chemical reaction catalyzed by this enzyme O c. increase the value of KM for the chemical reaction catalyzed by this enzyme O d. increase the value of Vmax for the chemical reaction catalyzed by this enzyme
What is the expected and logical result that you anticipate after you boil the extracted enzyme? Select one: O a. The boiled enzyme will not affect the reaction at all O b. The boiled enzyme will cause an increase in the reaction speed O c. The boiled enzyme will cause a decrease in the reaction speed d. The reaction will not proceed
pse A red blood cell is placed in a solution that is .85% solute. O a It depends upon the temperature b. Salt will leave the cell c. The cell crenates Od. There is no net change in the cell e The cell lyses QUESTION 4 If a reaction has a Delta G of -61: a. The reaction is non-spontaneous b The reaction is energy requiring Oc The reaction is spontaneous C. Od The reaction is exergonic Ge The reaction is endergonic
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).
An enzyme catalyzes the reaction A --> B. The enzyme is present at a concentration of 2 nM, and the Vmax is 10 uM/s. The Km for substrate A is 10mM Calculate the catalytic efficiency of this enzyme
An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.
An enzyme catalyzes the reaction A ⇌ B. The enzyme is present at a concentration of 2 nM, and the Vmax is 1.2 μM s-1 . The Km for substrate A is 10 μM. Calculate the initial velocity of the reaction, V0, when the substrate concentration is 2 μM.
Which of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that apply
Choose the False statement about the parameters that quantitate enzyme catalysis A. V max is the velocity of enzymetic traction at high substrate concentration. B. V max is attained when all enzyme moleculesare present in the form of complex with substrate C. Rate of the reaction is different from the rate constant D. under the certain conditions, michaelis constant Km charatertizes potency of substrate binding. E rate constant is higher at larger substrate concentration

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Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme pes