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Questions and Answers
What is the rate law for the reaction A + B -> AB?
What is the rate law for the reaction A + B -> AB?
In Michaelis-Menten kinetics experiments, which of the following is assumed to be true?
In Michaelis-Menten kinetics experiments, which of the following is assumed to be true?
What can be assumed about reaction conditions in Michaelis-Menten kinetics experiments?
What can be assumed about reaction conditions in Michaelis-Menten kinetics experiments?
How can the rate of a reaction be increased assuming the rate constant (k) is constant?
How can the rate of a reaction be increased assuming the rate constant (k) is constant?
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Adding more catalyst after a catalytic amount has already been added will increase the rate of reaction.
Adding more catalyst after a catalytic amount has already been added will increase the rate of reaction.
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What does it mean if the rate of reaction has reached maximum velocity (Vmax)?
What does it mean if the rate of reaction has reached maximum velocity (Vmax)?
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If a reaction has reached Vmax, what would happen to the rate of reaction if we increase the substrate concentration?
If a reaction has reached Vmax, what would happen to the rate of reaction if we increase the substrate concentration?
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What is one way to increase the Vmax of a reaction?
What is one way to increase the Vmax of a reaction?
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What are the respective reaction rate formulas for the enzyme catalysis steps E + S => ES => E + P?
What are the respective reaction rate formulas for the enzyme catalysis steps E + S => ES => E + P?
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What is the steady-state assumption when talking about enzyme kinetics?
What is the steady-state assumption when talking about enzyme kinetics?
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Study Notes
Enzyme Kinetics Overview
- Enzyme kinetics studies the rates of enzyme-catalyzed reactions and factors influencing these rates.
- Key parameters include substrate and enzyme concentrations, rate constants, and Vmax.
Rate Law Equation
- For the reaction A + B → AB, the rate law is expressed as Rate = k [A][B].
- Rate (change in concentration per unit time) depends on reactant concentrations and the rate constant (k).
Michaelis-Menten Kinetics Assumptions
- Constant substrate concentration and saturation of enzymes at Vmax are key assumptions.
- Increasing enzyme concentration will elevate Vmax; however, at Vmax, enzymes are saturated.
Ideal Behavior and Constant Factors
- Solutions are assumed to behave ideally, and constants ([E] and k) are stable throughout the experiment.
- Enzymes are essential for substrate conversion to product.
Reaction Rate Enhancement
- Reaction rates can be increased by raising substrate or enzyme concentrations.
- Adding inhibitors, regardless of type, does not enhance the reaction rate.
Catalyst Usage
- A catalyst performs its function with a small amount known as a "catalytic amount"—adding more will not further influence the reaction rate.
Vmax and Active Sites
- Vmax indicates saturation of enzymes; no increase in reaction rate occurs when substrate concentration rises because active sites are occupied.
- To increase Vmax, one must raise the enzyme concentration.
Enzyme Catalysis Steps
- Enzyme catalysis involves two key steps: formation of the enzyme-substrate complex (E + S → ES) and conversion to product (ES → E + P).
- The respective reaction rates for these steps are: Rate1 = k1 [E][S] for the first step and Rate2 = k2 [ES] for the second step.
Steady-State Assumption
- The steady-state assumption in enzyme kinetics posits that the concentration of the enzyme-substrate complex ([ES]) remains constant throughout the reaction.
Studying That Suits You
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Description
Test your knowledge on enzyme kinetics with this flashcard quiz from Biochemistry I Module of the MCAT Self Prep eCourse. Review key concepts such as rate laws and the factors affecting enzyme activity to prepare for your exam.
