Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN: 9781305389892
Author: Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher: Cengage Learning
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Textbook Question
Chapter 6, Problem 8TYK
Which of the following statements about the allosteric site is true?
a. The allosteric site is a second active site on a substrate in a
b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway.
c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again.
d. An allosteric activator prevents binding at the active site.
e. An enzyme that possesses allosteric sites does not possess an active site.
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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.
Indicate whether each of the following statements about an enzyme active site is true or false.
a. It is the location where substrate molecules are produced.
b. It always has a fixed, rigid geometry.
c. It always has a geometrical shape exactly complementary to that of substrate.
d. It always accomodates several structurally related substrates.
e. It is the location where substrate molecules are converted to product molecules.
f. It always has a shape that has a degree of flexibility to it.
g. it always accomodates only one specific substrate.
Which of the following statements regarding protein phosphorylation is FALSE?
Select one:
A. Phosphorylation is catalyzed by enzymes called protein kinases.
B. Phosphorylation inhibits the activity of enzymes
C. Aspartate residues can be phosphorylated.
D. Phosphorylation is a reversible covalent modification of enzymes.
Which is usually the slowest way to regulate a reaction in a metabolic pathway?
Select one:
A. Allosteric modulation
B. Covalent modification
C. Changing the enzyme concentration
D. All of the above are usually equally as fast
Chapter 6 Solutions
Biology: The Dynamic Science (MindTap Course List)
Ch. 6.1 - Prob. 1SBCh. 6.1 - In thermodynamics, what is meant by an isolated...Ch. 6.2 - Prob. 1SBCh. 6.2 - Prob. 2SBCh. 6.2 - Distinguish between exergonic and endergonic...Ch. 6.3 - Prob. 1SBCh. 6.3 - How are coupled reactions important to cell...Ch. 6.4 - How do enzymes increase the rates of the reaction...Ch. 6.4 - Can enzymes alter the G of a reaction?Ch. 6.5 - Prob. 1SB
Ch. 6.5 - What is the difference between competitive and...Ch. 6.5 - Prob. 3SBCh. 6.6 - Prob. 1SBCh. 6 - The capacity to do work best defines: a metabolic...Ch. 6 - The assembly of proteins from amino acids is best...Ch. 6 - When two glucose molecules react to form maltose:...Ch. 6 - When glucose reacts with ATP to form...Ch. 6 - In the following graph: A represents the product....Ch. 6 - Which of the following methods is not used by...Ch. 6 - In an enzymatic reaction: a. the enzyme leaves the...Ch. 6 - Which of the following statements about the...Ch. 6 - Which of the following statements about inhibition...Ch. 6 - Which of the following statements is incorrect? a....Ch. 6 - Prob. 11TYKCh. 6 - Discuss Concepts Trace the flow of energy through...Ch. 6 - Prob. 13TYKCh. 6 - Prob. 14TYKCh. 6 - Prob. 15TYKCh. 6 - Prob. 16TYKCh. 6 - Prob. 17TYKCh. 6 - Prob. 1ITDCh. 6 - Prob. 2ITDCh. 6 - Prob. 3ITD
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- The 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_forwardWhich 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 statearrow_forwardChoose 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…arrow_forward
- A hypothetical three-step metabolic pathway consists of intermediates W, X, Y, and Z and enzymes A, B, and C. Deduce the order of the enzymatic steps in the pathway from the following information: 1. Compound Q, a metabolic inhibitor of enzyme B, causes Z to build up. 2. A mutant in enzyme C requires Y for growth. 3. An inhibitor of enzyme A causes W, Y, and Z to accumulate. 4. Compound P, a metabolic inhibitor of enzyme C, causes W and Z to build up.arrow_forwardWhich of the following is true for the induced-fit model of enzyme-substrate binding? A. The conformation of the enzyme’s active site changes when the enzyme binds to its substrate B. Stronger interactions between the enzyme and its substrate are formed as compared to the lock-and-key model of enzyme-substrate binding C. Both A and B D. Neither A nor B Which statement does not apply to transition states? A. only exist transiently (have lifetimes on the order of 10^-14 to 10^-13 seconds) B. differ in energy from the substrate by the activation energy C. Chemical bonds are in the process of being formed and broken. D. Many have been detected and purified experimentally.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_forward
- 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 will happen if the concentration of an enzyme increases for a given substrate?? a. the reaction rate increases similarly b. the rate of the reaction decreases to a point. c. there is no change in the reaction. d. the turnover number decreases at the same rate that the enzyme concentration increases. e. the reaction stops.arrow_forwardWhich of the following statements about the Michaelis Menten constant (Km) is correct......A. can be determined by plotting the data v/[S] against 1/[S] B. A large Km indicates a low affinity between the enzyme and the substrate C. A large Km means that a large concentration of substrate is needed for the enzyme to work D. is a measure of the affinity of enzymes for proteins, minerals and vitamins E. Small Km means that a large concentration of substrate is needed for the enzyme to workarrow_forward
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