Michaelis-Menten Equation Overview

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Questions and Answers

What does the Michaelis-Menten equation primarily describe?

  • The effect of temperature on enzyme activity.
  • The influence of pH on enzyme stability.
  • The impact of enzyme inhibitors on reaction velocity.
  • The relationship between substrate concentration and reaction rate. (correct)

In the context of enzyme kinetics, what happens when substrate concentration, S, is greater than the Michaelis constant, Km?

  • The substrate begins to denature.
  • The enzyme undergoes allosteric regulation.
  • The enzyme is inhibited.
  • The reaction rate approaches Vmax. (correct)

Which statement correctly describes the significance of the Michaelis-Menten model in biochemistry?

  • It is only applicable for irreversible reactions.
  • It provides a complete model of all enzyme activities.
  • It emphasizes the role of product inhibition in enzyme kinetics.
  • It allows for the prediction of enzyme activity under various conditions. (correct)

What is the significance of the Lineweaver-Burk plot in enzyme kinetics?

<p>It simplifies the calculation of Km and Vmax. (C)</p> Signup and view all the answers

If the rate-limiting step in the enzymatic reaction is from ES to EP, how is Vmax defined in this context?

<p>Vmax = k3[Et] (D)</p> Signup and view all the answers

Flashcards

Michaelis-Menten Equation

A mathematical model that describes the relationship between the substrate concentration and the rate of an enzyme-catalyzed reaction.

Vmax

The maximum rate of an enzyme-catalyzed reaction, reached when all enzyme active sites are saturated with substrate.

Km

The substrate concentration at which the reaction rate is half of Vmax.

Lineweaver-Burk plot

A double reciprocal plot of the Michaelis-Menten equation, used to determine kinetic parameters (Km and Vmax).

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Enzyme Kinetics

The study of how enzymes catalyze biochemical reactions.

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Substrate Saturation

The point where all enzyme active sites are occupied by substrate, leading to maximum reaction rate.

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Study Notes

Michaelis-Menten Equation

  • The Michaelis-Menten equation describes the rate equation for a one-substrate enzyme-catalyzed reaction.
  • It's expressed as: V₀ = (Vmax [S]) / (Km + [S])
  • V₀ represents the initial velocity.
  • Vmax represents the maximum velocity.
  • [S] represents the initial substrate concentration.
  • Km represents the Michaelis constant.
  • V₀, Vmax, [S], and Km can be measured experimentally.

Enzyme Action (Michaelis-Menten)

  • Enzyme and substrate combine to form a complex (ES) in a fast, reversible step.
    • This is described by the reaction E + S ⇌ ES
  • The ES complex then breaks down to yield the free enzyme and the reaction product (E + P) in a slower step.
    • This is represented by the reaction ES ⇌ E + P
  • The second step limits the overall reaction rate.
  • The overall reaction rate is proportional to [ES].

Lineweaver-Burk Equation

  • Simplifying the Michaelis-Menten equation leads to the Lineweaver-Burk equation.
  • The Lineweaver-Burk equation is useful for graphically determining the kinetic parameters for an enzyme.
  • The equation is expressed as 1/V₀ = (Km/Vmax) (1/[S]) + 1/Vmax.

Interpreting Km

  • Km can vary for different substrates of the same enzyme.
  • Km values for different enzymes and substrates are in a table.

Interpreting Vmax

  • The number of reaction steps and the rate-limiting step(s) differ among enzymes.
  • For a two-step Michaelis-Menten mechanism:
    • If the rate-limiting step is ES → EP, then Vmax = k₂[Et].
    • If the rate-limiting step is EP → E + P, then Vmax = k₃[Et].

kcat (Turnover Number)

  • kcat is the turnover number.
  • It's the number of substrate molecules converted to product per enzyme molecule per unit of time when the enzyme is saturated.
  • kcat values for different enzymes and substrates are in a table.

Comparing Catalytic Mechanisms and Efficiencies

  • Comparing the ratio kcat/Km for two reactions is important to compare catalytic efficiencies or turnover.
  • The specificity constant is the rate constant for the conversion of E + S to E + P.

kcat/Km

  • kcat/Km has units of M⁻¹s⁻¹.
  • The upper limit for kcat/Km is 10⁸ to 10⁹ M⁻¹s⁻¹.
  • A table lists enzymes with kcat/Km close to the diffusion-controlled limit (10⁸ to 10⁹ M⁻¹s⁻¹).

Reactions with Multiple Substrates

  • Enzymes catalyzing reactions involving two or more substrates account for nearly 2/3 of all enzymatic reactions.
    • Often they have two substrates and two products.
  • Examples
    • Group transfer reactions
    • Oxidation-reduction reactions

Ternary Complex

  • Substrates can bind in a random sequence or in a specific order.
  • Some reactions involve a ternary complex (enzyme-substrate-substrate).
    • These reactions have a different reaction mechanism compared to simpler reactions
  • Some enzyme reactions do not form a ternary complex.
    • Ping-Pong, or double-displacement reactions

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