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Michaelis-Menten Assumptions quiz #1 Flashcards

Michaelis-Menten Assumptions quiz #1
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  • What are the three key assumptions underlying the Michaelis-Menten equation in enzyme kinetics, and why are they important?
    The three key assumptions are: (1) Substrate concentration assumption: the total substrate concentration is approximately equal to the free substrate concentration because substrate is much more abundant than enzyme; (2) Initial velocity assumption: only the initial reaction velocity is measured, so reverse reactions are negligible early on; (3) Steady state assumption: the concentration of the enzyme-substrate complex remains constant during the reaction. These assumptions are crucial for deriving and applying the Michaelis-Menten equation.
  • Who were Michaelis and Menten, and what was their major contribution to biochemistry?
    Michaelis and Menten were enzymologists who proposed a fundamental model for enzyme kinetics in 1913, emphasizing the formation of an enzyme-substrate complex during enzyme-catalyzed reactions.
  • What is the substrate concentration assumption in the Michaelis-Menten model?
    It assumes that the total substrate concentration is approximately equal to the free substrate concentration because substrate is much more abundant than enzyme.
  • Why can the free substrate concentration be used to represent the total substrate concentration in the Michaelis-Menten equation?
    Because the free substrate concentration is much greater than the enzyme concentration, making the amount of substrate bound to enzyme negligible.
  • What does the initial velocity assumption state in Michaelis-Menten kinetics?
    It states that only the initial reaction velocity is measured, so reverse reactions are negligible early in the reaction.
  • Why do biochemists focus on the initial velocity of enzyme-catalyzed reactions?
    Because at the start of the reaction, there is little product, making the reverse reaction from product to enzyme-substrate complex negligible.
  • What is the steady state assumption in the context of Michaelis-Menten kinetics?
    It assumes that the concentration of the enzyme-substrate complex remains constant during the reaction.
  • How does the steady state assumption affect the rates of formation and dissociation of the enzyme-substrate complex?
    It means the rate of formation of the enzyme-substrate complex equals the rate of its dissociation.
  • Why are the three Michaelis-Menten assumptions important for the equation's application?
    They are crucial for deriving and correctly applying the Michaelis-Menten equation to enzyme kinetics.
  • What historical context makes Maud Menten’s contributions to enzyme kinetics particularly notable?
    Maud Menten made significant scientific contributions at a time when women in Canada were not even legally considered 'persons' and could not vote.