1. The allosteric inhibitor of an enzyme a) Causes the enzyme to work faster b) Binds to the active site c) Participates in feedback regulation d) Denatures the enzyme
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- 1. Allosteric regulation is an important part of feedback regulation. All of the functions listed below can be performed by an allosteric molecule EXCEPT: A) catalysis of a reaction. B) activation of an enzyme. C) inhibition of an enzyme. D) conformational change of an enzyme.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 productThe active site of an enzyme is usually a groove or pocket on the surface that A) binds allosteric regulators of the enzyme. B) is involved in the catalytic reaction of the enzyme. C) is inhibited by the presence of a coenzyme or a cofactor.
- 1. A substance that is able to interact with an enzyme, reducing its ability to process a substrate, is called an inhibitor. If the inhibitor acts by temporarily attaching to an area other than the binding site, causing a change in the shape of the enzyme's active site, it would be a(n) a. Irreversible inhibitor b. Competitive inhibitor c. Reversible inhibitor d. Noncompetitive inhibitor 2. Several factors can affect the rate of an enzyme-catalyzed reaction. The following four diagrams show how reaction rates are affected by pH, temperature, substrate concentration and the amount of enzyme. Which diagram best represents how changes in the substrate concentration affect the rate? a b C d. While there are several theories used to explain how enzymes function, one popular one is call the induced-fit theory. Which of the following is the basis of that theory? 3. а. Different cofactors can be used by the same apoenzyme, allowing it to interact with an entire class of substrates. b.…2. Enzymes A) have highest affinity for the substrate B) have highest affinity for the product C) have highest affinity for the transition state D) None of the above Briefly explain:1. Shown below is a metabolic pathway: Es E E4 E1 E2 A - B - C - D E3 E6 Q- R – S E7 Es Suppose we have too much of "S" in the cell, please answer the following questions, with regards to feedback inhibition: a) Which enzyme is most likely to be regulated? b) Which substance will act as the 'regulator'? c) Name the "site" where this 'regulator' will bind to the enzyme: d) Is this substance (from #b), a homotropic or heterotropic modulator?
- . 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.Which of the following statements is/are correct?a) Enzyme quantities depend on the rate of their synthesis and degradationb) Enzyme quantity is decreased if an amino-acid involved in the catalytic activity is modifiedc) Protein kinase A activity is regulated through protein interaction.d) Kinases control the activity of other enzymes by covalent modification; irreversiblephosphorylation explain each of the following optionThe 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.
- 3) Read the situations below and indicate which of the four methods of enzyme regulation is occurring for each. a) The energy-carrying molecule ATP is made by the enzyme ATP synthase. Muscle cells use a lot of energy and also have higher amounts of the ATP synthase enzyme than many other cell types. General mechanism of enzyme regulation: S b) Prostaglandins are messenger molecules involved in the inflammatory response, as well as the perception of pain. They are synthesized from polyunsaturated fatty acid substrates by an enzym called cyclo-oxygenase. "Ibuprofen" is the active ingredient in a variety of anti-inflammatory medications such as Motrin® and Advil®. It reduces pain and swelling by binding to a hydrophobic channel in the active site of cyclo-oxygenase, blocking the polyunsaturated fatty acids from binding to the enzyme, and therefore stopping production of prostaglandins. General mechanism of enzyme regulation: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 C4. An enzyme-substrate complex has a Kd = 100 nM. A competitive inhibitor with which of the following Ki values will be most effective at inhibiting this enzyme? A) K₁ = 10 nM B) K₁ = 100 nM C) K₁ = 1000 nM D) None of the above - only the KM is important Briefly explain: