5 Questions
What is the Michaelis-Menten kinetics model based on?
Data from batch reactors with constant liquid volume
What is the active site of an enzyme responsible for?
Interaction with the substrate
What happens as reaction time progresses in enzymatic reactions?
More amounts of products are produced until the limiting reactants are consumed
What is the structure of the active site of an enzyme designed to fit?
The molecular shape of the substrate
What does a higher initial substrate concentration result in, according to the text?
More product produced
Study Notes
Enzymatic Reactions
- The Michaelis-Menten kinetics model is based on the rates of enzyme-catalyzed reactions.
- The active site of an enzyme is responsible for binding the substrate and facilitating the conversion of the substrate into product.
- As reaction time progresses in enzymatic reactions, the rate of reaction initially increases, but eventually reaches a maximum rate (Vmax) as the active sites of the enzyme become saturated with substrate.
- The structure of the active site of an enzyme is designed to fit the specific shape and chemical properties of the substrate, allowing for efficient binding and catalysis.
- A higher initial substrate concentration results in a faster initial rate of reaction, as there are more substrate molecules available to bind to the active site of the enzyme.
Test your understanding of enzyme kinetics with this quiz on Michaelis-Menten kinetics. Explore the mathematical model and concepts related to the rate of enzymatic reactions.
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