5. Explain a competitive inhibitorIn the induced-fit model, what happens tothe shape of the enzyme when the substratebinds?A. stays the sameB. adapts to the shape of thesubstrate35) An irreversible inhibitor is one thatA) forms hydrogen bonds with the substrate.B) binds to the enzyme with hydrophobicinteractions.C) reacts covalently with the substrate.D) binds covalently to the enzyme active site.E) reacts covalently with a cofactor.47) Metal ions such as Zn2+ and Fe3+ are oftenneeded by enzymes asA) isozymes.B) allosteres.C) inhibitors.D) cofactors.E) substrates.3) An enzyme that converts a functional group toanother between two structuresA) oxidoreductaseB) transferaseC) hydrolaseD) lyaseE) isomeraseWhat is the function of these enzymes:OxidoreductaseTransferaseDecarboxylase32) When an end product from an enzyme-mediatedsequence is also an inhibitor for an earlier step in thereaction sequence, the process is referred to asA) feedback control.B) competitive inhibition.C) irreversible inhibition.D) negative catalysis.E) concentration control.

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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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Which of the following is NOT true of a competitive inhibitor? A) Its effects can be overcome by increasing the concentration of substrate. B) It competes with substrate for binding to the active site. C) It irreversibly inhibits the enzyme by chemically modifying a group at the active site. D) It often resembles the substrate for the enzyme it inhibits.
7. Identify the type of inhibition in each description. A) competitive B) noncompetitive C) Irreversible 1) an inhibitor that resembles the structure of the substrate 2) an inhibitor that forms a covalent bond with a side chain in the active site 3) Adding more substrate does not reverse the effect of this inhibitor. 4) The inhibition can be reversed by increasing the concentration of substrate. 5) The inhibitor does not resemble the substrate.
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.
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
Indicate i) the class of enzymes to which it belongs to, ii) name the kind of bond that is modified due to its activity, iii) indicate the substrate that is recognised by the enzyme using the amino acid three letter code and iv) whether the enzyme displays high or low substrate specificity. Must be less than 50 words total.
6. Which of the following is true of the binding energy derived from enzyme-substrate interactions? A) It cannot provide enough energy to explain the large rate accelerations brought about by enzymes. B) It is sometimes used to hold two substrates in the optimal orientation for reaction. C) It is the result of covalent bonds formed between enzyme and substrate. D) Most of it is derived from covalent bonds between enzyme and substrate. E) Most of it is used up simply binding the substrate to the enzyme. B
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)?
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.
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.
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...
Which of the following is a type of irreversible enzyme inhibitor A) Mechanism-based (suicide) inhibitor B) Non-competitive inhibitor C) Uncompetitive inhibitor OD) Competitive inhibitor 8
In competitive inhibition A) a molecule competes for the allosteric site on an enzyme B) two proteins combine C) a molecule completes for the active site on an enzyme D) activation energy is reduced

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3) An enzyme that converts a functional group to another between two structures, A) oxidoreductase B) transferase C) hydrolase D) lyase E) isomerase