Homework Answers
Question
Answer - (A) negative regulator
Explain - The allosteric enzyme ATCase is regulated by CTP, which binds to the T-state of ATCase. CTP is a negative regulator because, CTP binds to the regulatory chains and stabilizes the structure of the T-state by decreasing its energy.
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The allosteric enzyme ATCase is regulated by CTP, which binds to the T-state of ATCase. CTP...
BIOCHEMISTRY PALA (shown below) binds to the active site of ATCase and is an important probe...
BIOCHEMISTRY
PALA (shown below) binds to the active site of ATCase and is an
important probe molecule to study ATCase regulation. PALA acts as
_______________ type of inhibitor and acts to stabilize the
__________-state of the enzyme.
PALA{N-(phosphonasetyl)-L-aspartate.
A) uncompetitive/T
B) competitive/T
C) Uncompetitive/R
D) Competitive/R
E) Noncompetitive/R
HN Cooc Jacooo
3. Which of the following is true for a concerted mechanism of allosteric regulation? (a) All of ...
3. Which of the following is true for a concerted mechanism of allosteric regulation? (a) All of the subunits are in either T state or R state. (b) Binding of ligand to one site can affect neighboring sites without causing all of the subunits to undergo the T to R transition (c) The regulation of ATCase cannot be explained using a concerted model. (d) Binding of CTP to the enzyme shifts the equilibrium of all subunits simultaneously to the R...
The rate-limiting enzyme of the pyrimidine nucleotide synthesis pathway is controlled by many different allosteric regulator...
The rate-limiting enzyme of the pyrimidine nucleotide synthesis pathway is controlled by many different allosteric regulator molecules. Which is involved in this regulation? Select one: a. UTP b. ATP c. CTP d. All of these e. None of these
What indicates that an enzyme inhibitor binds at an allosteric site?
What indicates that an enzyme inhibitor binds at an allosteric site?a.) The inhibitor has no effect on kcat.b.) The inhibitor increases kcat.c.) The inhibitor decreases kcat.
41. An enzyme-substrate complex forms when substrate binds to an enzyme at the enzyme's site. 42....
41. An enzyme-substrate complex forms when substrate binds to an enzyme at the enzyme's site. 42. An inorganic ion such as zinc or manganese that is needed for an enzyme to function is acting as a 43. Competitive inhibition of enzymes occurs when: site A) catalytic B) allosterie C) operative B) cofactor C) apoenzyme D) holoenzyme A) coenzyme A) the inhibitor binds to the active site of the enzyme B) the inhibitor binds to the allosteric site of the enzyme...
A) List, in order, the three enzymes that catalyze the highly regulated steps in glycolysis. (Don't...
A) List, in order, the three enzymes that catalyze the highly regulated steps in glycolysis. (Don't just enter 1, 2, 3 for reaction numbers - give the reaction number based on the 10 steps of glycolysis.) Reaction # Enzyme Reaction # Enzyme Reaction # Enzyme B) For each of these reactions, name ONE allosteric regulator of the enzyme and whether that regulator inhibits or activates the enzyme. Reaction # allosteric regulator Inhibitor or activator? Reaction # allosteric regulator Inhibitor or...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is: a) a competitive inhibitor b) an allosteric inhibitor c) a noncompetitive inhibitor d) a suicide inhibitor 3. Competitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c) bind outside the active site and decrease substrate binding d) bind outside the active site and decrease rate of catalysis.
12. Which of the following statements is true of enzyme catalysts? A B C To be...
12. Which of the following statements is true of enzyme catalysts? A B C To be effective, they must be present at the same concentration as their substrate. They can increase the equilibrium constant for a given reaction by a thousand-fold or more. They lower the activation energy for conversion of substrate to product. Their catalytic activity is independent of pH. They are generally equally active on D and L isomers of a given substrate. D E 13. In competitive...
Which of the following statements about the MWC model is false? a. it involves the enzyme...
Which of the following statements about the MWC model is false? a. it involves the enzyme occurring in the two distinct conformations when the allosteric regulator is absent b. it involves the enzyme occurring in an R state (performs catalysis well) and a T state (performs catalysis poorly) c. it involves a conformational shift in the prescence of allosteric regulator d. it involves a higher population of the T state than the R state when allosteric regulator is not present...
Which answer best describes a drug which is an allosteric inhibitor? Select one: a. binds to...
Which answer best describes a drug which is an allosteric inhibitor? Select one: a. binds to the binding site for the endogenous ligand and have no physiological response b. increases the binding of the endogenous ligand C. competes with the endogenous ligand on the receptor binding site d. decreases the binding of the endogenous ligand
BIOCHEMISTRY
PALA (shown below) binds to the active site of ATCase and is an
important probe molecule to study ATCase regulation. PALA acts as
_______________ type of inhibitor and acts to stabilize the
__________-state of the enzyme.
PALA{N-(phosphonasetyl)-L-aspartate.
A) uncompetitive/T
B) competitive/T
C) Uncompetitive/R
D) Competitive/R
E) Noncompetitive/R
HN Cooc Jacooo
3. Which of the following is true for a concerted mechanism of allosteric regulation? (a) All of the subunits are in either T state or R state. (b) Binding of ligand to one site can affect neighboring sites without causing all of the subunits to undergo the T to R transition (c) The regulation of ATCase cannot be explained using a concerted model. (d) Binding of CTP to the enzyme shifts the equilibrium of all subunits simultaneously to the R...
41. An enzyme-substrate complex forms when substrate binds to an enzyme at the enzyme's site. 42. An inorganic ion such as zinc or manganese that is needed for an enzyme to function is acting as a 43. Competitive inhibition of enzymes occurs when: site A) catalytic B) allosterie C) operative B) cofactor C) apoenzyme D) holoenzyme A) coenzyme A) the inhibitor binds to the active site of the enzyme B) the inhibitor binds to the allosteric site of the enzyme...
A) List, in order, the three enzymes that catalyze the highly regulated steps in glycolysis. (Don't just enter 1, 2, 3 for reaction numbers - give the reaction number based on the 10 steps of glycolysis.) Reaction # Enzyme Reaction # Enzyme Reaction # Enzyme B) For each of these reactions, name ONE allosteric regulator of the enzyme and whether that regulator inhibits or activates the enzyme. Reaction # allosteric regulator Inhibitor or activator? Reaction # allosteric regulator Inhibitor or...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is: a) a competitive inhibitor b) an allosteric inhibitor c) a noncompetitive inhibitor d) a suicide inhibitor 3. Competitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c) bind outside the active site and decrease substrate binding d) bind outside the active site and decrease rate of catalysis.
12. Which of the following statements is true of enzyme catalysts? A B C To be effective, they must be present at the same concentration as their substrate. They can increase the equilibrium constant for a given reaction by a thousand-fold or more. They lower the activation energy for conversion of substrate to product. Their catalytic activity is independent of pH. They are generally equally active on D and L isomers of a given substrate. D E 13. In competitive...
Which answer best describes a drug which is an allosteric inhibitor? Select one: a. binds to the binding site for the endogenous ligand and have no physiological response b. increases the binding of the endogenous ligand C. competes with the endogenous ligand on the receptor binding site d. decreases the binding of the endogenous ligand
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