Principles of Biology
2nd Edition
ISBN: 9781259875120
Author: Robert Brooker, Eric P. Widmaier Dr., Linda Graham Dr. Ph.D., Peter Stiling Dr. Ph.D.
Publisher: McGraw-Hill Education
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Chapter 6, Problem 4TY
Summary Introduction
Introduction:
The ATP (adenosine triphosphate) production is vital for the functioning of the various systems and biochemical processes in the cell. The ATP can be generated through aerobic and anaerobic respiration. Several
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An inhibitor was added to an enzyme and the expected rate of the reaction was not detected and the substrate was not utilized at all. This inhibitor is (choose one answer only):
Is un-competitive, meaning the inhibitor binds to a site near the active site.
Is competitive, meaning the inhibitor binds directly to the same active site as the subtrate.
Is non-competitive, meaning the inhibitor binds to site other than the active site as the subtrate.
Is irreversible, meaning the inhibitor binds covalently to the enzyme keeping the enzyme inactive permanently.
Classify the inhibitor characteristics according to one of three types of inhibition: reversible competitive, reversible
noncompetitive, or irreversible.
Reversible competitive
inhibitor binds noncovalently at site other than
active site
0°
Reversible noncompetitive
inhibitor structure resembles
substrate structure
inhibitor does not alter the maximum reaction
rate
Irreversible
inhibitor binds.covalently and permanently at
site other than active site
Which effect of which enzyme inhibitor is shown in the graph?
Select one:
Irreversible mixed
Reversible mixed
Reversible uncompetitve
Reversible competitive
Irreversible
Chapter 6 Solutions
Principles of Biology
Ch. 6.1 - Which do you think has more entropy, an NaCl...Ch. 6.1 - Prob. 1TYKCh. 6.1 - Prob. 2TYKCh. 6.2 - Prob. 1CCCh. 6.2 - Prob. 2CCCh. 6.2 - Prob. 3CCCh. 6.2 - Prob. 1TYKCh. 6.2 - An inhibitor raises the Km for an enzyme but has...Ch. 6.3 - Prob. 1CCCh. 6.3 - Prob. 1TYK
Ch. 6.3 - Prob. 2TYKCh. 6.3 - Prob. 3TYKCh. 6.4 - Prob. 1CCCh. 6.4 - Prob. 1BCCh. 6.4 - Prob. 1TYKCh. 6.4 - Prob. 2TYKCh. 6.4 - Prob. 2CCCh. 6.5 - Prob. 1TYKCh. 6.6 - During the citric acid cycle, what happens to...Ch. 6.7 - Prob. 1CCCh. 6.7 - Prob. 2CCCh. 6.7 - Prob. 3CCCh. 6.7 - Prob. 1TYKCh. 6.7 - Prob. 2TYKCh. 6.7 - Prob. 3TYKCh. 6.8 - Prob. 1CCCh. 6.8 - Prob. 1TYKCh. 6 - According to the second law of thermodynamics....Ch. 6 - Reactions that release free energy are exergonic....Ch. 6 - Prob. 3TYCh. 6 - Prob. 4TYCh. 6 - Prob. 5TYCh. 6 - Prob. 6TYCh. 6 - Prob. 7TYCh. 6 - Prob. 8TYCh. 6 - Prob. 9TYCh. 6 - Prob. 10TYCh. 6 - Describe the mechanism and purpose of feedback...Ch. 6 - What causes the rotation of the y subunit of ATP...Ch. 6 - PRINCIPLES A principle of biology is that living...Ch. 6 - Discuss how life can maintain its order in spite...Ch. 6 - Prob. 2CBQ
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Which of the following are characteristics of catabolic metabolic pathways? (Choose all correct answers). Overall oxidation of initial substrates so redox reactions involve use of NAD+ as oxidizing agent, converted to NADH. Large initial substrates are broken down to smaller final products. Overall reduction of intial substrates so redox reactions involve use of NADPH as reducing agent, converted to NADP+. The pathways are overall exergonic (negative delta G). Net production of ATP as a result of the pathway. Essentially irreversiblearrow_forwardPlease select all of the following statements that are true. Cofactors involve the use of vitamins to assist enzymes Competitive inhibitors bind to the same active site as the substrate. When the substrate binds to the enzyme the reaction rate increases. Non-competitive inhibitors can act as both inhibitors and activators.arrow_forwardWhich mechanism does NOT regulate the activity of an enzyme? a competitive inhibitor binding to the active site a competitive inhibitor binding to the ES complex an uncompetitive inhibitor binding to the ES complex All three mechanisms regulate enzyme activity.arrow_forward
- Which statement is false of a competitive inhibitor? It irreversibly inhibits the enzyme by chemically modifying a group at the active site. It competes with substrate for binding to the active site. Its effects can be overcome by increasing the substrate concentration. It often resembles the substrate for the enzyme it inhibits.arrow_forwardDetermine whether the following statements describe a reversible competitive inhibitor, a reversible noncompetitive inhibitor, or an irreversible inhibitor. Both the inhibitor and the substrate cannot bind to the enzyme at the same time. The structure of the inhibitor is similar to that of the substrate. The addition of more substrate can reverse the inhibitor effect It forms a covalent bond with the active site.arrow_forwardClassify the items as competitive or noncompetitive inhibitors for control of enzyme action. Bind to the allosteric site on the enzyme Not influenced by the concentration of substrate Resemble the substrate Do not resemble thhe substrate Bind to active site of the enzymearrow_forward
- A transition-state analog— resembles the active site of general acid-base enzymes. is less stable when binding to an enzyme than the normal substrate. stabilizes the transition state for the normal enzyme-substrate complex. reacts more rapidly with an enzyme than the normal transition state intermediate. resembles the transition-state structure of the normal substrate in the enzyme-substrate complex.arrow_forwardMark any/all that apply to uncompetitive inhibition: Group of answer choices: None of these is correct. The inhibitor does not resemble the substrate. The inhibitor can bind to both enzyme alone AND enzyme that is bound by substrate. Inhibition can be overcome by the addition of more substrate. KM/Vmax are equal for both the inhibited and the uninhibited reaction.arrow_forwardThe image shows the rate of an enzyme reaction under conditions of no inhibition, competitive inhibition, and noncompetitive inhibition as reactions labeled uninhibited, A, and B. Which of the following best explains what has occurred in the enzyme reactions? Reaction B shows competitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows noncompetitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows competitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor. Reaction B shows noncompetitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor.arrow_forward
- Many drugs are competitive inhibitors of specific enzymes. For drugs that act as competitive inhibitors, the enzymes must be allosterically regulated. the amount of drug needed to achieve the same effect is increased as the substrate concentration increases. the substrate must be bound to the enzyme before the drug can bind. the amount of drug needed to achieve the same effect is increased as the substrate concentration decreases.arrow_forwardAn enzyme facilitate catalysis by formation of ester bond with an alcoholic substrate. Which amino acid residues can facilitate such mechanism of catalysis? Select the correct response: Cys and Met Lys and Arg Ser and Tyr Glu and Asparrow_forwardWhen the enzyme hexokinase binds to glucose and ATP it undergoes a conformational change. All of the following are true about this enzyme-substrate binding EXCEPT: The active site changes shape so that it binds more tightly to the substrates The substrates are optimally positioned for the reaction to occur The substrates become contorted or strained, which increases their reactivity The activation energy of the reaction increasesarrow_forward
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