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Questions and Answers
What does the Michaelis-Menten equation primarily describe?
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?
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?
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?
What is the significance of the Lineweaver-Burk plot in enzyme kinetics?
If the rate-limiting step in the enzymatic reaction is from ES to EP, how is Vmax defined in this context?
If the rate-limiting step in the enzymatic reaction is from ES to EP, how is Vmax defined in this context?
Flashcards
Michaelis-Menten Equation
Michaelis-Menten Equation
A mathematical model that describes the relationship between the substrate concentration and the rate of an enzyme-catalyzed reaction.
Vmax
Vmax
The maximum rate of an enzyme-catalyzed reaction, reached when all enzyme active sites are saturated with substrate.
Km
Km
The substrate concentration at which the reaction rate is half of Vmax.
Lineweaver-Burk plot
Lineweaver-Burk plot
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Enzyme Kinetics
Enzyme Kinetics
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Substrate Saturation
Substrate Saturation
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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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