Biological Science (7th Edition)
7th Edition
ISBN: 9780134678320
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Greg Podgorski, Emily Taylor, Jeff Carmichael
Publisher: PEARSON
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Textbook Question
Chapter 8, Problem 2TYK
What is a transition state?
a. the shape adopted by an enzyme that has an inhibitory molecule bound at its active site
b. the amount of kinetic energy required for a reaction to proceed
c. the intermediate complex formed as covalent bonds in the reactants are being broken and re-formed during a reaction
d. the structure of an enzyme when an allosteric regulatory molecule binds to it
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Students have asked these similar questions
What is the reason why the transition state of a catalyzed reaction is lower has lower energy compared to an uncatalyzed reaction?
A. because enzymes only work at low temperatures
B. because of favorable interactions with the substrate
C. because of enthalpic interactions between the enzyme and the transition state
D. A and B
Which statement best summarizes the structure of an enzyme before and after it catalyzes a reaction?
a.) Its structure is the same.
b.) It gains a water molecule in the reaction.
c.) It loses a carbon atom in the reaction.
d.) It loses a hydrogen atom in the reaction,
When you heat a solution past the optimum for an enzyme?
A. the active site permanently binds substrate via covalent bonding
B. the enzyme stiffens and slows down
C. the enzyme starts to denature
Chapter 8 Solutions
Biological Science (7th Edition)
Ch. 8 - 2. What is a transition state?
a. the shape...Ch. 8 - 3. How does pH affect enzyme-catalyzed...Ch. 8 - Explain how feedback inhibition regulates...Ch. 8 - 5. Explain the lock-and-key model of enzyme...Ch. 8 - If you were to expose glucose to oxygen on your...Ch. 8 - Using what you have learned about changes in Gibbs...Ch. 8 - Prob. 10TYPSSCh. 8 - 15. The functional form of PAH contains four...
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- What is activation energy? a. The thermal energy associated with random movements of molecules b. The energy released through breaking chemical bonds c. The difference in free energy between reactants and products d. The energy required to initiate a chemical reactionarrow_forward_____________ are molecules used in enzyme studies that resemble the structure of a substrate’s transition state.arrow_forwardWhat is the function of the active site of an enzyme? a. Involved in the catalytic reaction of the enzyme b. Inhibit the enzymatic activity c. Binding of regulators d. Binding of products after the reactionarrow_forward
- In the lab, a group of students is carrying out the reaction described and graphed in the previous question, but it is not proceeding. One student suggests heating it up to make it proceed more rapidly. Another student suggests adding an enzyme to the reaction instead. They try both and find that heating speeds up the reaction, and adding an enzyme also speeds up the reaction. A) How does heating the reaction in a test tube cause the reaction to occur at a higher rate? B) How does adding an enzyme enable the reaction to occur at a faster rate?arrow_forwardWhich statement defines a coenzyme? a. An enzyme precursor b. A unit consisting of an enzyme bound to reactants plus ATP c. An inactive enzyme that becomes functional upon contact with specific cofactors d. The active part of an enzyme e. An organic molecule closely associated with enzymesarrow_forwardSubstance A is converted to substance B in a metabolic reaction. Which statement best describes the role of enzyme during this reaction? A. It dissolves substance A in the reaction medium. B. It speeds up the reaction without it being consumed in the process. C. It provides energy to the reaction system D. It adjusts the pH of the reaction medium.arrow_forward
- In terms of functions of proteins in cells; how does enzymes function as catalysts ?arrow_forwardGroup amino acids according to those that have polar side chains vs those that have non-polar side chains vs those that have charged side chains and explain how the different chemical properties of those side chains could affect enzyme function.arrow_forwardIn a highly high-temperature environment, you placed an enzyme and some substrates. You've seen that there hasn't been any reaction. Applying what you have learned on enzyme activity, how would you explain what occurred? A. The enzyme was not placed at a pH level that would allow it to react at its maximum rate. B. There are not enough enzymes for the reaction to occur. C. The enzyme may have denatured or broken down due to the high temperature of the environment, resulting in no reaction. D. There are not enough substrates for reaction to occur. Substrate concentration affects enzyme activity. Determine what would occur when there are too many substrates and fewer enzymes? A. No enzyme activity would occur. B. The reaction rate would continuously increase. C. The reaction would speed up tremendously. D. Maximal rate of reaction would occur. Enzyme activity mainly involves the active site and the substrate. How would you compare the active site from the substrate? A. The substrate…arrow_forward
- draw the enzyme binding pocket and active site draw the curved arrows showing the reaction proceeding toward the products show how the enzyme facilitates the reaction write a description of how the enzyme works Propose a name for the enzyme based on the rules from classarrow_forwardName and describe three ways discussed in class that enzymes lower the activation energy of a reaction A. B. C.arrow_forwardEnzymes increase the rate of biochemical reactions by which process? A) donating electrons to substrates b) removing electrons from substrates c) facilitating the formation of transition states d) Changing single bonds to double bonds Substrates usually bind to enzymes by the following process: a) substrate fits tightly into active site like a lock and key b) substrate binds loosely to the active site at first. Then enzyme molds itself around the substrate to produce a tighter fit c) substrate binds tightly to the active site at first. Then the enzyme relaxes producing a looser fit. D) the substrate binds to a chaperone protein which directs it to the active site Proline racemase catalyzes the conversion of L-Proline to D-proline. It would be classed as: a) a ligase b) a hydrolase c) an isomerase d) an oxidoreductasearrow_forward
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