Question 5Select all statements that are correct.Competitive inhibitors bind to the allosteric site on the enzymeUncompetitive inhibitors bind to the substrate binding siteCompetitive inhibitors bind to the substrate binding siteCompetitive inhibitors are usually of similar size and shape than the substrate of the enzymeNon-competitive inhibitors can bind to the free enzyme but not to the enzyme-substratecomplex

Enzymes catalyze biochemical reactions. Enzyme activity can be inhibited by competitive inhibitors,…

Answered: Question 5 Select all statements that…

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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QUESTION 6 If a drug is built to bind to the active site of the enzyme, it will prevent substrate binding. This drug would be classified as a(n) allosteric activator. O allosteric inhibitor. noncompetitive inhibitor. competitive inhibitor.
QUESTION 10 Select a property that does not belong to allosteric enzymes. They conform to hyperbolic Michaelis-Menten kinetics They may have binding sites for regulatory molecules that are separate from active sites They tend to have a signmoidal curve of rate versus [S] They undergo conformation changes as a result of modulator binding.
Question 13 of 13 Fill in the blanks: Write C if only statement A is correct, Hif only statement B is correct, E if both statements are correct, M if both statements are incorrect. A.An inhibitor that binds somewhere in the enzyme other than the active site is an uncompetitive inhibitor. B. With this mode of inhibitor binding, the substrate's affinity to the enzyme is affected and it decreases the maximum reaction velocity.
Time 3/33 answered Ở Show Hewtty, Carlos Remaining Please save all answers. Questions that you save can still be edi pu have 1 UNSAVED ANSWER- SAVE ALL ANSWERS Question 32 The initial rate for an enzyme-catalyzed reaction has been determined at several substrate concentrations. Data are as follows: The Km value (µM) is: TT [S] umol/L v[(umol/L) min-1] 22 10 39 20 65 50 102 100 120 200 135 Select an answer and submit. For keyboard navigation, use the up/down arrow kéys to select an answer. a 800 100 1200 2000 e 90 10
QUESTION 40 An inhibitor that binds noncovalently to the active site is noncovalently to a different site is while an inhibitor that binds Both types of inhibition are O a. competitive, noncompetitive, reversible. b. uncompetitive, competitive, reversible. O c. noncompetitive, uncompetitive, reversible. O d. competitive, noncompetitive, irreversible. O e. uncompetitive, competitive, irreversible. Click Save and Submit to save and submit. Click Save All Answers to save all answers. MacBo
A purely competitive inhibitor of an enzyme has which of the following kinetic effects? decrease in Km increase in Vmax decrease in Vmax increase in Km Question 60 The Michaelis-Menten constant (KM) has the following characteristics, EXCEPT: The dimension for KM is concentration, such as molarity It is equal to ½ of Vmax It is the substrate concentration necessary to reach ½ of Vmax
Select all statements that are correct. Enzyme inhibitors more than 1 correct statement. reduce the activation energy of a reaction 1 prevent the formation of the enzyme-substrate complex and no product can be formed reduce the rate at which products are formed by making it harder for the enzyme-substrate complex or the product to be formed prevent the product from being released from the enzyme reduce the activity of the enzyme Note there might
Question 6 Review Concept 8.4 Enzymes. Match the term and its description. Each term can only be used once. These are nonprotein enzyme helpers. [ Choose) These inhibitors bind to the active site of an enzyme, [ Choose ) competing with the substrate to decrease reaction > >
QUESTION 34 Bonus: In the graph shown below which of the following statements is TRUE concerning the "plateau" region of the curve? Reaction welocity v Substrate concentration. IS) O both (a) and (c) All the available substrate has been converted to product The enzyme is in the stressed state O The enzymes active site is saturated with enzyme O The enzyme becomes less active Click Save and Submit to save and submit. Click Save All Answers to save all answers.
Question 8 Review Concept 8.5. Match the term and its description. Each term can only be used once. A regulatory molecule binds to a protein at one site and (Choose ) affects the protein's function at another site is termed as A form of allosteric regulation that can amplify enzyme [ Choose ) activity is called The end product of a metabolic pathway shuts down the [ Choose ) pathway > > >
Incorrect Question 2 0/ How does an enzyme affect a chemical reaction? Select all that apply. V Increases the activation energy Decreases the rate of the reaction Lowers the activation energy Increases the rate of the reaction
QUESTION 4 What TYPE of inhibition is observed in the following: S E Competitive Non-competitive Uncompetitive Allosteric

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