Enzymes and Catalysis
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Questions and Answers

What is the primary function of an enzyme?

  • To decrease the rate of a chemical reaction
  • To be consumed by the reactants
  • To alter the reactants in a chemical reaction
  • To increase the rate of a chemical reaction (correct)

What is the characteristic of enzyme-substrate binding according to the induced fit model?

  • The enzyme binds to multiple substrates simultaneously
  • The substrate induces a change in the enzyme's conformation (correct)
  • The enzyme-substrate complex is highly unstable
  • The enzyme's shape is complementary to the substrate's shape

What is the purpose of the active site in an enzyme-catalyzed reaction?

  • To increase the activation energy
  • To bind to the substrate by noncovalent interactions (correct)
  • To bind to the products
  • To bind to the reactants

Why is the lock-and-key model less likely to be an effective catalyst?

<p>The ES complex may be too stable, reducing the thermodynamic benefit (B)</p> Signup and view all the answers

What is the term for the energy required to reach the transition state from the ground state of the reactants?

<p>Activation energy (A)</p> Signup and view all the answers

What is the characteristic of enzyme-catalyzed reactions?

<p>They are 103-1020 times faster than uncatalyzed reactions (D)</p> Signup and view all the answers

What is the primary function of the transition state?

<p>To represent an unstable arrangement of atoms in which chemical bonds are being formed or broken (A)</p> Signup and view all the answers

What is the advantage of inducing a fit in the induced fit model?

<p>It reduces the distance to the transition state (A)</p> Signup and view all the answers

What is the characteristic of most enzymes?

<p>They are proteins (D)</p> Signup and view all the answers

What is the term for the reactant in an enzyme-catalyzed reaction?

<p>Substrate (C)</p> Signup and view all the answers

What is the characteristic of competitive inhibition?

<p>Km increases (A)</p> Signup and view all the answers

What is the effect of uncompetitive inhibition on Vmax?

<p>Decreases (A)</p> Signup and view all the answers

What is the characteristic of non-competitive inhibition?

<p>Vmax decreases, Km remains the same (A)</p> Signup and view all the answers

What is the effect of adding more substrate in competitive inhibition?

<p>Overcomes the inhibition (D)</p> Signup and view all the answers

What type of inhibition occurs when the inhibitor binds only to the ES complex?

<p>Uncompetitive (D)</p> Signup and view all the answers

What is the effect of non-competitive inhibition on Km?

<p>Remains the same (B)</p> Signup and view all the answers

What is the characteristic of irreversible inhibition?

<p>Forms a stable covalent bond with the enzyme (C)</p> Signup and view all the answers

What is the effect of uncompetitive inhibition on the ES complex?

<p>Decreases the formation of ES (C)</p> Signup and view all the answers

What is the result of irreversible inhibition of acetylcholinesterase (AChE)?

<p>Death by paralysis (B)</p> Signup and view all the answers

What is the difference between reversible and irreversible inhibition?

<p>Reversible inhibition can be overcome by adding more substrate, while irreversible inhibition cannot (B)</p> Signup and view all the answers

What is the primary purpose of studying Enzyme Kinetics?

<p>To understand various properties of enzymes such as substrate specificity and affinity (A)</p> Signup and view all the answers

What is the unit of measurement for Turnover Number (Kcat)?

<p>sec-1 (B)</p> Signup and view all the answers

What does a small KM value indicate?

<p>The enzyme requires only a small amount of substrate to become saturated (C)</p> Signup and view all the answers

What is the purpose of Lineweaver-Burk plots?

<p>To accurately determine Vmax and KM from experimental data (A)</p> Signup and view all the answers

What is the result of excessive heat on enzyme function?

<p>Enzyme becomes completely nonfunctional (A)</p> Signup and view all the answers

What type of inhibitor binds to the active site of E, competing with S?

<p>Competitive inhibitor (D)</p> Signup and view all the answers

What is the definition of Vmax?

<p>The maximum reaction rate reached when the enzyme is completely saturated with substrate (A)</p> Signup and view all the answers

What is the significance of Km in enzyme kinetics?

<p>It gives us information on enzyme affinity for the substrate (A)</p> Signup and view all the answers

What is the definition of catalytic efficiency?

<p>The ratio of Kcat to Km (C)</p> Signup and view all the answers

What is the effect of pH on enzyme function?

<p>Enzymes work best within a particular range of pH (A)</p> Signup and view all the answers

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