Enzyme Kinetics and Equilibrium Constants
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Questions and Answers

What is the steady state assumption in enzyme kinetics?

  • The rate of ES formation is zero
  • The rate of ES formation equals the rate of ES dissociation (correct)
  • The rate of ES formation is less than the rate of ES dissociation
  • The rate of ES formation is greater than the rate of ES dissociation

    • What is the expression for the rate of the reaction in Michaelis-Menten kinetics?

  • ν = k2 [Eo][S] / KM
  • ν = k2 [Eo][S]^2 / KM
  • ν = k2 [Eo][S] / [S]+ KM (correct)
  • ν = k2 [Eo][S]^2

    • What is the significance of Km in Michaelis-Menten kinetics?

  • It is the maximum rate of the reaction
  • It is the substrate concentration at half Vmax
  • It is the enzyme-substrate dissociation constant (correct)
  • It is the substrate concentration at saturation

    • What is the relationship between Vmax and Km?

    <p>Vmax is independent of Km</p> Signup and view all the answers

    What is the expression for Vmax in Michaelis-Menten kinetics?

    <p>Vmax = k2 [Eo]</p> Signup and view all the answers

    What is the term for the substrate concentration at which the rate of the reaction is half of Vmax?

    <p>KM</p> Signup and view all the answers

    What is the effect of a non-competitive inhibitor on the kinetics of an enzyme?

    <p>Decreases Vmax and Km remains the same</p> Signup and view all the answers

    What happens to the inhibition by an uncompetitive inhibitor when the substrate concentration is increased?

    <p>Inhibition is enhanced</p> Signup and view all the answers

    What is the characteristic of a competitive inhibitor?

    <p>Binds to the active site and increases Km</p> Signup and view all the answers

    What is the effect of a non-competitive inhibitor on the double reciprocal plot?

    <p>Two parallel lines intersecting at the Y-axis</p> Signup and view all the answers

    What type of inhibitor binds to the free enzyme and the enzyme-substrate complex?

    <p>Non-competitive inhibitor</p> Signup and view all the answers

    What is the purpose of the Eadie-Hofstee plot?

    <p>To determine Km and Vmax</p> Signup and view all the answers

    What types of attractions are involved in the binding of substrates to enzymes?

    <p>Electrostatic interactions, hydrogen bonds, Van der Waals forces, and hydrophobic interactions</p> Signup and view all the answers

    What is the main factor that determines the specificity of enzyme-substrate binding?

    <p>The precisely defined arrangement of atoms at the active site</p> Signup and view all the answers

    What is the primary function of the enzyme ribonuclease?

    <p>To cleave RNA</p> Signup and view all the answers

    What is the name of the endoribonuclease enzyme from SARS-CoV?

    <p>Nsp15</p> Signup and view all the answers

    How many domains are present in the structure of nsp15?

    <p>3</p> Signup and view all the answers

    What is the quaternary structure of nsp15?

    <p>Hexamer</p> Signup and view all the answers

    What is the basis of the specificity of an enzyme?

    <p>The precise interaction of substrate with the enzyme</p> Signup and view all the answers

    What type of inhibition occurs when DIPF reacts with the R groups of amino acids?

    <p>Group-specific inhibition</p> Signup and view all the answers

    What is the name of the enzyme that cleaves any peptide bond?

    <p>Subtilisin</p> Signup and view all the answers

    What is the name of the nerve gas that reacts with Ser in acetylcholinesterase?

    <p>DIPF</p> Signup and view all the answers

    What is the name of the kinetics that describes the relationship between enzyme-substrate binding and reaction rate?

    <p>Michaelis-Menten kinetics</p> Signup and view all the answers

    What does the equilibrium constant k in the equation k[A][B] = k-1[C] represent?

    <p>The extent of the reaction</p> Signup and view all the answers

    Why does the reaction rate not increase linearly with an increase in [S]?

    <p>Because the enzyme concentration is limiting</p> Signup and view all the answers

    What is the overall mechanism of the enzyme catalysis reaction?

    <p>Two consecutive reversible reactions</p> Signup and view all the answers

    Why can we ignore the reverse reaction in our analysis?

    <p>Because we are only measuring the initial rate</p> Signup and view all the answers

    What is the significance of the assumption [S] >> [E]o?

    <p>The enzyme will be mostly present as the intermediate ES</p> Signup and view all the answers

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