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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Which of the following is characteristic of competitive inhibitors?
the inhibitor could bind to the active site or to an allosteric site on the enzyme.
the enzyme will mistake the inhibitor for its substrate, so that the inhibitor will
end up covalently bound to the enzyme.
the inhibitor can bind only AFTER the substrate has bound (i.e. it binds only to
the ES complex).
the inhibitor can bind reversibly at the substrate-binding site (the active site).
the inhibitor will lower the characteristic Vmax of the enzyme.
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 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 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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- Please 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_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_forward
- Classify 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_forwardWhich of the following accurately characterizes enzyme active sites? (Pick two.) Active sites form the greatest number of favorable electrostatic interactions with a reaction's substrates. Active sites form the greatest number of favorable electrostatic interactions with a reaction's transition state. Competitive inhibitors that resemble an enzyme's substrate bind more tightly to the active site than those that resemble products or transition states. Competitive inhibitors that resemble an enzyme's transition state bind more tightly to the active site than those that resemble products or substrates.arrow_forwardClassify each specific inhibitor or inhibitor characteristic according to one of two types of inhibition: competitive or noncompetitive.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_forwardA 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_forward
- The 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_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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