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 willend up covalently bound to the enzyme.the inhibitor can bind only AFTER the substrate has bound (i.e. it binds only tothe 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.

Inhibitors can be broadly classified into reversible and irreversible inhibitors. Reversible…

Answered: Which of the following is…

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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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
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 of the following statements regarding competitive enzyme inhibition is correct? O The substrate and the inhibitor compete for the active site on the enzyme. The substrate competes with an enzyme for binding to an inhibitor O The inhibition effect is always irreversible. The inhibitor binds to site other than the active site.
In noncompetitive inhibition, can both the substrate and the inhibitor bind at the same time? I know the inhibitor changes the enzyme's conformation so it would lower the product formation, but what if the substrate were to bind first, and then the inhibitor binded afterwards?
Determine 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.
A medicinal chemist is trying to determine the mechanism of action of inhibitors she has synthesized. The relative change in KM and Vmax upon incubation of the targeted enzyme with each inhibitor is shown in the table below. Inhibitor A Inhibitor B Inhibitor C Using this data, the mechanism of action of Inhibitor C is: Uncompetitive TS‡ analog Mixed Inhibition Competitive Кмарр- Км 0 Non-competitive app - Vmax <0 <0 0 Vmax
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.
Mark any/all that apply to uncompetitive inhibition: Group of answer choices -KM/Vmax are equal for both the inhibited and the uninhibited reaction. -The inhibitor does not resemble the substrate. -Inhibition can be overcome by the addition of more substrate. -The inhibitor can bind to both enzyme alone AND enzyme that is bound by substrate. -None of these is correct.
An 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 Asp
Why can we say that having a pure non- competitive inhibitor present is similar to just having less enzyme present?
PMSF is a protease inhibitor that binds to enzyme active site. What is the possible mode of inhibition? Competitive O Irreversible O Non-competitive O Mixed
In the following example an enzyme is being inhibited. This is an example of Active site Inhibitor Altered active site O Non-competitive inhibition O Competitive inhibition MacBook Air

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