Can you help me Determine whether each of the inhibitors (or inhibitor characteristics) are involved in reversible inhibition orirreversible inhibition.a) inhibitor structure often resembles the substrate structureb) inhibitor forms a new and permanent covalent bond to the enzyme's active sitec) sulfanilamided) aspirine) inhibitor binds weakly and noncovalently to an enzyme's active site and decreases its activityf) penicillin Vg) inhibitor binds weakly and noncovalently to the enzyme at a region other than the active siteh) inhibitors repeatedly attach to and detach from enzymei) inhibitor is used in a pathway that is regulated by feedback inhibition

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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A mixed inhibitor of an enzyme (sometimes called a mixed non-competitive inhibitor) can decrease the rate of a reaction by any of the following EXCEPT by: a) binding to a site other than the active site of the enzyme. b) binding to the active site of the enzyme, preventing substrate binding. c) decreasing kcat. d) Increasing KM.
Which of the following statements about non-competitive inhibitors is true? A) They bind at the active site of the enzyme and block access to the substrate. B) They bind at a location away from the active site. C) They function by changing the shape of the enzyme's active site. D) B and C
the type of enzyme inhibition in which covalent bulky adduct prevents catalysis is ? a) uncompetitive b) reversible c) noncompetitive d) competitive e) Irreversible
A competitive inhibitor diminishes the rate of catalysis: A) By reducing the proportion of enzyme molecules bound to a substrate. OB) By altering the shape of the active site of the enzyme C) By binding to a regulatory subunit D) By enhancing the interaction between enzyme and reaction product
In a Lineweaver-Burk graph, the lines representing the uninhibited and inhibited enzyme catalyzed reaction meet each other on the x-axis. The type of inhibition which is occurring is: a) competitive b) noncompetitive c) uncompetitive d) allosteric CO2 exerts direct activity upon hemoglobin by: a) blocking oxygen from binding to the heme group b) displacing BPG from the central cavity c) oxidizing Fe+2 to Fe+3 which does not bind oxygen d) forming an N-terminal carbamate which favors the T-state The dominant motif found in hemoglobin and myoglobin is: a) helix-turn-helix b) twisted beta sheet c) beta barrel d) random coil Which of these is an ketohexose? a) fructose b) glucose c) ribose d) erythrose Which of these is a constitutional isomer of d-glucose? a) fructose b) galactose c) l-glucose d) ribose Which of these is an enantiomer of d-glucose? a) d-fructose b) d- galactose c) l-glucose d) d-ribose Which of these is a diastereomer of…
. Based on what you know about enzyme inhibition, classify the following examples as irreversible, competitive, or noncompetitive enzyme inhibition. A) competitive B) noncompetitive C) irreversible 1) Diisopropyl fluorophosphate binds to acetylcholinesterase and permanently inactivates the enzyme. Paralysis results. 2) A drug binds to the active site of an enzyme but disassociates and leaves the enzyme active. 3) A toxin binds to the surface of an enzyme. The enzyme then binds the substrate, but no product is produced. The toxin may disassociate and the enzyme will become active again. 4) Vitamin K is a coenzyme involved in blood clotting. An anticoagulant drug binds at the site of vitamin K bonding, blocking vitamin K binding and preventing clotting. Clotting resumes after the patient stops taking the drug. 5) Aspirin binds to prostaglandin synthetase and permanently stops its ability to produce prostaglandin.
One of the hallmarks of competitive inhibition is that there is constant competition betweenthe substrate and the inhibitor for binding to the enzyme active site.a) If [inhibitor] >> [substrate], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?b) If [substrate] >> [inhibitor], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?
Which model for enzyme-substrate chemical complementarity is described by the following: Before substrate binding, some enzyme molecules have active sites complementary to substrates and other enzyme molecules have non-complementary active sites. Substrate molecules preferentially bind to the enzyme molecules with complementary active sites. Non-complementary enzyme molecules undergo a structural change to become complementary to maintain conformational equilibrium. a) conformational selection b) induced fit c) lock and key...
Vmax for an enzyme-catalyzed reaction: A) generally increases when pH increases. B) is limited only by the amount of substrate supplied. C) is twice the rate observed when the concentration of substrate is equal to the Km. D) is unchanged in the presence of a uncompetitive inhibitor. E) increases in the presence of a competitive inhibitor.
The activity of an enzyme can be regulated by a: A) competitive inhibitor binding to the active site. B) competitive inhibitor binding to the ES complex. C) noncompetitive inhibitor binding to the ES complex. D) Only A and C are correct. E) Only A and B are correct.
Vmax for an enzyme-catalyzed reaction: A)is twice the rate observed when the concentration of substrate is equal to Km. B)is unchanged in the presence of a noncompetitive inhibitor. C)generally increases when pH increases. D)increases in the presence of a competitive inhibitor. E)is limited only by the amount of substrate supplied.
All of the following statements about competitive and non-competitive inhibitors are true EXCEPT:(a) Competitive inhibitors are structurally similar to anenzyme’s substrate and bind to the enzyme’s allostericsite.(b) Competitive inhibitors work by competing with a sub-strate for binding to an enzyme’s active site.(c) Noncompetitive inhibitors can bind at sites other thanthe active site of an enzyme, distorting the tertiary pro-tein structure, which alters the shape of the active site,rendering it ineffective for substrate binding.(d) Some noncompetitive inhibitors bind reversibly whilesome bind irreversibly to their enzyme.(e) b and d.

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Determine whether each of the inhibitors (or inhibitor characteristics) are involved in reversible inhibition or irreversible inhibition. a) inhibitor structure often resembles the substrate structure b) inhibitor forms a new and permanent covalent bond to the enzyme's active site c) sulfanilamide