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Questions and Answers
According to Michaelis-Menten kinetics, what is the purpose of using the kinetics equation?
Which type of reactions can Michaelis-Menten kinetics be applied to?
In a pseudo first order reaction involving two substrates, what happens to the rate when more of substrate A is added?
Which equation represents the Michaelis-Menten kinetics?
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What does a small KM value indicate in enzyme kinetics?
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Which plot creates a straight line graph for Michaelis-Menten kinetics?
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Study Notes
Michaelis-Menten Kinetics
- The purpose of using the Michaelis-Menten kinetics equation is to analyze the rates of enzyme-catalyzed reactions.
Applicability of Michaelis-Menten Kinetics
- Michaelis-Menten kinetics can be applied to reactions involving a single substrate and a single active site on the enzyme.
Pseudo First Order Reaction
- In a pseudo first order reaction involving two substrates, when more of substrate A is added, the rate remains constant, indicating that the reaction is saturated with respect to substrate A.
Michaelis-Menten Equation
- The Michaelis-Menten equation is V = Vmax * [S] / (KM + [S]), where V is the initial reaction rate, Vmax is the maximum reaction rate, [S] is the substrate concentration, and KM is the Michaelis-Menten constant.
Michaelis-Menten Constant (KM)
- A small KM value indicates that the enzyme has a high affinity for the substrate, meaning that it can bind easily to the active site.
Lineweaver-Burk Plot
- The Lineweaver-Burk plot creates a straight line graph for Michaelis-Menten kinetics, which is a double reciprocal plot of 1/V vs 1/[S].
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Description
Test your knowledge of enzyme kinetics with this quiz! Explore the principles behind Michaelis-Menten kinetics and learn how to determine the maximum rate and substrate affinity of enzymes. Discover the reactions to which this kinetics equation can be applied.
