Questions and Answers
What happens to kcat and Km when an allosteric effector increases the catalytic efficiency of an enzyme?
kcat increases, Km decreases
What is catalytic efficiency?
A measure of how well an enzyme facilitates reactions at low substrate concentrations
When enzyme concentration is held constant, what is catalytic efficiency proportional to?
The initial slope of a Michaelis-Menten curve
Study Notes
Allosteric Effectors
- Allosteric effectors can enhance enzyme action if they increase kcat (turnover number) and decrease Km (Michaelis constant).
- Increased kcat indicates a higher rate of product formation, while decreased Km suggests a stronger enzyme-substrate affinity.
Catalytic Efficiency
- Catalytic efficiency assesses how effectively an enzyme converts substrates into products, particularly in conditions of low substrate availability.
- It is calculated as the ratio of kcat to Km, providing insight into enzyme performance.
Enzyme Concentration Impact
- When enzyme concentration remains constant, catalytic efficiency relates directly to the initial slope of the Michaelis-Menten curve.
- A steeper slope signifies better catalytic efficiency, reflecting a more significant response to substrate concentration at low levels.
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Description
This quiz focuses on key concepts related to enzymes in biochemistry, including allosteric effectors and catalytic efficiency. Learn how factors such as kcat and Km affect enzyme efficiency at low substrate concentrations. Perfect for students looking to reinforce their understanding of enzymatic functions.
