Which of the following aspects of catalysis by enzymes can NOT be explained by theFischer 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.

Enzymes are proteins that catalyze biochemical reactions. Enzymes catalyse the reaction by reducing…

Answered: Which of the following aspects 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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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.
Consider an enzyme (P) that gets activated by forming a dimer (P2): 2P = P2 At 25 °C, we have AH- 19 kJ/mol and AS-65 kJ/mol, for this dimerization reaction. Identify the correct statement. O The enzyme is activated when kept at temp = +37 °C. O The enzyme is activated at all temperatures. O The enzyme is activated when kept in the fridge with temp = 4 "C. O The enzyme can never be activated, no matter what the temperature is. O None of the above statements is true.
The following reaction coordinate diagram charts the energy of a substrate molecule (S) as it passes through a transition state (X‡) on its way to becoming a stable product (P) alone or in the presence of one of two different enzymes (E1 and E2). How does the addition of either enzyme affect the change in Gibbs free energy (ΔG) for the reaction? Which of the two enzymes binds with greater affinity to the substrate? Which enzyme better stabilizes the transition state? Which enzyme functions as a better catalyst?
Consider a reaction in which reactants X and Y combine to form the product Z. The diagram below compares the reaction coordinates for the catalyzed and uncatalyzed pathways of this reaction. B. X+Y Reaction Coordinate What does letter B represent? O Letter B represents the activation energy of the uncatalyzed reaction pathway. Letter B represents the energy difference between the reactants and products for the uncatalyzed pathway. O Letter B represents the activation energy of the catalyzed reaction pathway. Letter B represents the energy difference between the reactants and products for the catalyzed pathway. Energy
Give a complete and well descriptive definition of the following:1.1 Enzyme catalysis1.2 Co-enzyme1.3 Negative heterotropic co-cooperativit
Enzymes are biological catalysts that fulfill the following general reaction mechanism: E+S [ES] [EP] E + P Where E is enzyme, S is substrate, and P is product. Briefly describe how an enzyme is able to speed of the rate of a reaction:
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
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 Michaelis–Menten kinetics Lineweaver–Burk plot 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.
The 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 coordinate
The decomposition reaction of hydrogen peroxide (H₂O₂) proceeds as follows: 2 H₂0₂ → 2 H₂O + 0₂ 2 This reaction can occur without a catalyst, in the presence of a chemical catalyst (platinum) or of a biological catalyst (catalase). 1- From the values given in the table below, determine the catalytic power of each catalyst (ratio of the catalyzed rate of reaction to the uncatalyzed rate). 2- Which catalyst is the most efficient? Reaction conditions No catalyst Platinum Catalase Ea (kJ.mol¹) at 20 °C 75 49 8
Which of the following statements is TRUE of enzyme catalysts? for heads up question 2 and 3 are false 1) To be effective, they must be present at the same concentration as their substrate. 2) They can increase the equilibrium constant for a given reaction by a thousand-fold or more. 3) They lower the free energy for conversion of substrate to product. 4) Their catalytic activity is dependent on pH. 5) They are generally equally active on D and L isomers of a given substrate.
One enzyme-catalyzed reaction in a biochemical cycle has an equilibrium constant that is 10 times the equilibrium constant of a second reaction. If the standard Gibbs energy of the former reaction is -300 kJ/mol, what is the standard Gibbs energy of the second reaction? Ans: -294 kJ/mol

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