Which of the following are effects of catalyst that cause an increase in the rate ofreaction? (This is a multi-select question. Select all that apply).a decrease in DG‡.an increase in DG.an increase in temperature.an increase in the energy of the molecules/ions of reactant.an increase in the number of molecules/ions of reactant with enough energy toovercome the activation energy barrier.

The 'D' in DG and DG+ stands for delta ().DG () is the change in free energy. For a general reaction…

Answered: Which of the following are effects of…

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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Which of the following aspects of catalysis by enzymes can NOT be explained by the Fischer Lock and Key Hypothesis? Enzymes will lower the activation energy barrier for reaction. Enzymes will specifically recognize their substrates. Appropriate substrates will bind to the enzyme to form a Michaelis complex. Enzymes have an "active site" where appropriate substrates will be bound. Two of the above cannot be explained by the Fischer "Lock and Key" Hypothesis.
Which of the statement is true regarding equilibrium? The rate of the forward reaction exceeds the rate of the reverse reaction The concentration of the reactants and the concentration of the products remains constant The value of equilibrium constant will change if a catalyst is present O Increasing the concentration of reactants increase the equilibrium constant
Which of the following is not an assumption made when evaluating Michaelis Menton kinetics? the reaction is happening at body temperature the substrate is in great excess of the catalyst measurement of initial velocity of the reaction reaction conditions are occurring under steady state
. To catalyze a biochemical reaction, an enzyme typically dissociates into additional reactant molecules, thereby increasing the геaction ratе decomposes and releases energy to increase the number of successful collisions between reactant molecules binds temporarily to reactant molecules to lower the activation energy of the reaction drives the reaction to completion by consuming byproducts of the reaction CLEAR ALL
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.
The transition state of a reaction is easily isolated using column chromatography. by definition higher in free energy than the product. equal to the AG‡ of the uncatalyzed reaction minus the G‡ of the catalyzed reaction. Olower in free energy than the ground state of the substrate.
Which of the following statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.
this one represents an endothermic reaction. Things are similar: the flat line on the left (beginning of the reaction) is the total energy possessed by the reactant molecules; once again, kJ stands for energy in kiloJoules, thousands of Joules. The flat line on the right (reaction complete) is the total energy of the products. Since an endothermic reaction has a net absorption of energy (taking this extra energy from the surroundings), the products have higher energy than the reactants. Question: the energy of the reactant molecules is kJ. [to answer, simply identify the correct y-axis coordinate.] 250 200 PE (kJ) 150 100 50 Reaction pathway
In order for the reaction rate to rise the activation energy should be Select one: O O O O a. decreased b. increased c. decreased or increased d. not changed Riboflavin gives rise to cofactors:
Mark any/all statements that are TRUE regarding reactions and enzyme catalysis. Group of answer choices -The role of an enzyme in catalysis is to increase the difference in free-energy between the products and reactants (increase the G for the reaction). -None of these is correct. -The free-energy of a reaction (G) determines the rate of reaction. -In thermodynamics, the term "spontaneous" means that a reaction requires energy to proceed. -The transition state of an enzyme-catalyzed reaction is destabilized in comparison to the transition state of the uncatalyzed reaction.
Amylase is an enzyme found in saliva that breaks down starch. The enzyme is currently functioning at its optimal pH of 7 and optimal temperature of 32oC. Which of the following could result in an increase in the reaction rate? Providing an environment with a pH of 9. Decreasing enzyme concentration. Placing the reactants in an environment at 10oC. Increasing substrate concentration.
Which of the following statements is false regarding an enzyme's ability to catalyse a reaction? an enzyme provides a reaction surface and a hydrophilic environment for the reaction to take place an enzyme binds reactants such that they are positioned correctly and can attain their transition-state configurations an enzyme allows the reaction to go through a more stable transition state than would normally be the case an enzyme can weaken bonds in reactants through the binding process

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