Enzymes are important molecules in biochemistry that catalyze reactions. The energy diagram illustrates the difference between a catalyzed reaction and an uncatalyzed reaction. Label the energy diagram. activation energy reactants (substrate) free energy reaction progress transition state uncatalyzed reaction catalyzed reaction AG for reaction products

Enzymes are important molecules in biochemistry that catalyze reactions. The energy diagram illustrates the difference between a catalyzed reaction and an uncatalyzed reaction. Label the energy diagram. activation energy reactants (substrate) free energy reaction progress transition state uncatalyzed reaction catalyzed reaction AG for reaction products

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter7: Energy And Metabolism

Section: Chapter Questions

Problem 11TYU: PREDICT In the following reaction series, which enzyme(s) is/are most likely to have an allosteric...

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state a optimum temperature of enzyme E
The reason for the increase in the rate of an enzyme reaction when the temperature is increased isa. decrease in kinetic energy of reactantb. increase in kinetic energy of reactantc. increase in activation energy of reactiond. decrease in activation energy of reaction
In enzyme kinetics, why are measurements made at the start of a reaction?
A student in lab is trying to use an enzyme to obtain a reaction product . After several attempts , the enzyme reaction continually fails . Using what you know about some factors that affect enzyme function , you ask the student questions to determine what has gone wrong . List three questions you would ask , and why these questions ( and their potential answers ) are important to determine why the reaction is not happening.
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
Some enzymes have catalytic activity only limited by diffusion. Which rate constants of an enzyme- catalyzed reaction is/are rate limiting for the enzyme? How does this line up/compare to the rate limiting step of Michaelis-Menten Enzyme Kinetics? (Please show work and correct answer)
Suicide substrates are substances that resemble the substrate,but when incorporated into the active site they form a covalent bond with the enzyme, permanently inhibiting it. Thesemolecules have been used to label the amino-acid side chainsthat are involved in the catalytic reaction occurring withinthe active site. This is usually accomplished by hydrolyzingthe inhibited enzyme. How could an investigator identify theamino acid bound to the suicide substrate molecule?
Alkaline phosphatase had an optimal temperature of 37°C. If you tested the enzyme at 37°C, 50°C, and 80°C, what would be your expected reaction rates? Graph your expected results (label your axes and lines)
Suggest the possible class of enzyme (or name of enzyme) for each of the enzyme-catalyzed reactions below. Briefly explain your answer.
A student determined the Km, Vmax and turnover number (kcat) for an enzyme by performing reactions with varying amounts of substrate and a concentration of enzyme at 10nm The student then decided to repeat the reaction with the same substrate concentration but with increased enzyme concentration to 20nm. Would the following increase, decrease or stay the same? Km Vmax Kcat
Given: Your professor gives you a vial of enzyme and a vial of substrate. The product of this reaction is fluorescent and you can measure the concentration of the product as a function of time. (answer a, b, and c)a) Your professor tells you to quantify how much product is being produced per minute at thebeginning of the experiment. What exactly are you measuring?b) On the same plot, show the kinetic curve for an increased quantity of enzyme. Assume a 2x concentration. Indicate Km and Vmax.c) You don’t have a computer hand. Sad. How can you plot the data such that you can get important Michaelis-Menten values?
When calculating the order of a reaction, the enzyme doesnot appear in the equation. Explain.