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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Chapter 8, Problem 10TYPSS
Summary Introduction
Introduction:
Allosteric molecules are those molecules that bind to the allosteric site of an enzyme and induce conformational change in the enzyme.
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If the environmental temperature gets too high, what will happen to an enzyme and the chemical reaction it catalyzes?
Group of answer choices
A. It will not encounter its substrates often, and the reaction will slow down.
B. It will crystallize, the active site will become inflexible and slow down the reaction.
C. It will denature, lose its shape, and the reaction will not occur.
D. It will become less fluid, and be unable to transport substances easily.
E. It will become more fluid, and speed up the reaction.
Which of the following is true about allosteric enzymes?
A. Allosteric enzymes are always multimeric.
B. Regulatory sites (allosteric sites) on an allosteric enzyme are always different from the catalytic site.
C. Allosteric enzymes always change the conformation of the active site in response to binding of an allosteric modulator.
D. Suicide inactivators are examples of allosteric modulators.
Choose only the letter, no explanation needed.
Enzyme activity is affected by a variety of factors. What factor causes the enzyme to denature if it becomes extremely high? *
Choices:
A. Water's Effect
B. pH
C. Temperature
D. Activator's Effect
An inhibitor binds to the enzyme's active site, preventing the substrate from binding to it. What conclusions can you make from this situation? *
A. No reaction occurred
B. Non-competitive inhibition occurred
C. Enzyme activity occurred
D. Competitive inhibition occurred
Each enzyme is very selective when it comes to its substrate. What can you conclude from this statement? *
A. Any substrate can bind to the active site.
B. Enzymes are used up in the reaction.
C. Only a specific substrate can bind to the active site.
D. Enzymes break down when not used.
Lock : Key :: Active Site : _____________________________ *
A. Substrate
B. Active Site
C. Coenzyme
D. Cofactor
Enzymes only speed up biological functions, so they are NOT used up in the…
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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- Enzymes can be regulated in a many different ways. Covalent modification is one way. Here, the functional groups are attached to or removed from the enzyme. A phosphate group is an example of a functional group that can be added to an enzyme. Depending on the enzyme, addition of a phosphate group can either increase or decrease an enzyme's activity. Evaluate the following names and identify the general name of an enzyme that functions to add phosphate groups to its substrate? A. isomerase B. phosphatase C. kinase D. ligasearrow_forwardWhich of the following statements about allosteric enzyme regulation are true. A. Allosteric regulation is always used to negatively regulate enzyme activity. B. Allosteric regulators are often end products of a biochemical pathway. C. Different allosteric regulators turn enzyme activity on or off by binding the same site. D. Binding of allosteric regulators alters the conformation of an enzyme.arrow_forwardYou are studying Protein X, which is a tetramer whose function is to bind glucose. You have found a molecule that is an allosteric effector of the protein’s activity. This means that: a. The molecule causes Protein X to bind O2 very tightly b. The molecule does not bind in the active site but affects the function of the protein c. The molecule is highly negatively charged d. The molecule binds in the same site as glucosearrow_forward
- Which of the following is true about the phosphorylation of proteins? A. Proteins are usually phosphorylated at amino acids that have hydroxyl group-containing side chains. B. Phosphorylation of proteins is catalyzed by phosphatases. C. Phosphoryation always activates enzymes. D. The specificity in phosphorylation is conferred solely by the amino acid to be phosphorylated.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_forwardA mother in the kitchen squeezes a small lemon onto a fruit mix to avoid browning. Explain the kitchen technique that the mother used in terms of the Polyphenoloxidase enzyme chemistry you learned from the experiment.arrow_forward
- Which one of the following statements is true of enzyme catalysts? a. Their catalytic activity is independent of pH. b. They are generally equally active on D and L isomers of a given substrate. c. They can increase the equilibrium constant for a given reaction by a thousand fold or more. d. They can increase the reaction rate for a given reaction by a thousand fold or more. e. To be effective, they must be present at the same concentration as their substrate.arrow_forwardSuppose an enzyme and its substrate obey the lock and key model of enzyme catalysis. Which of the following would be true of the enzyme?Select all that apply A.the active site of the enzyme must be rigid B.the active site of the enzyme must be flexible C.only one substrate could be converted to product by the enzyme D.the enzyme could bind different substrates if the substrates shared a common motif somewhere in their structures E.the entire enzyme must be rigidarrow_forwardThe concept of “induced fit” refers to the fact that: a. enzyme specificity is induced by enzyme-substrate binding. b. enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. c. enzyme-substrate binding induces movement along the reaction coordinate to the transition state. d. substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. e. when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate.arrow_forward
- Most synthetic reactions in which carbon dioxide is used require vitamin biotin. The biotin becomes covalently bound to a lysine molecule that is part of an enzyme, and the biotin can then attach to and carry the carbon dioxide molecule. Biotin is best referred to as: a. Prosthetic group b. Enzyme inhibitor c. Competitive inhibitor d. Organic acid e. Non-competitive inhibitorarrow_forwardA histidine was determined to be the critical residue involved in an enzyme-catalyzed reaction. If the pKa of the histidine is known to be 6.5 in the active site and the pH of maximum catalytic activity is 7.2, what is likely the primary role of histidine in the catalytic reaction? A. forms a covalent bond with the substrate B. reduces the entropy of the substrate C. stabilizes a charged intermediate D. acts as a proton donor Aspartate and lysine are in the active site of an enzyme. They are both known to participate directly in catalysis. The pKa's of the residues are found to be 3.2 and 9.6, respectively for aspartate and lysine. The optimum pH for the enzyme is 6.4. Which forms of these two residues will predominate when the enzyme is most active? A. aspartate is protonated; lysine is deprotonated B. both residues are deprotonated C. aspartate is deprotonated; lysine is protonated D. both residues are protonatedarrow_forwardEnzymes are catalytic proteins or RNA molecules that accelerate chemical reactions. Substrates are the molecules that are acted upon by enzymes and are converted into products through the binding of substrates to an enzyme’s active site. Figure 1 below shows a protein enzyme’s active site and four potential protein substrates. Table 1 indicates the different chemical properties at several locations in a hypothetical enzyme’s active site, and Table 2 indicates the different chemical properties at several locations in the potential substrates. Locations labeled “A” in the enzyme’s active site and on the substrate will attempt to interact, as will locations that are labeled “B” and “C. Describe, in terms of energy, how enzymes catalyze chemical reactions.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License