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Definition: This calculator determines the initial reaction rate (V₀) of an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor.
Purpose: It helps biochemists and researchers understand how uncompetitive inhibitors affect enzyme kinetics and reaction rates.
The calculator uses the formula:
Where:
Explanation: The formula describes how an uncompetitive inhibitor binds to the enzyme-substrate complex, affecting both Vmax and KM.
Details: Understanding inhibition kinetics is crucial for drug development, metabolic pathway analysis, and enzyme engineering.
Tips: Enter Vmax, substrate concentration, KM, and α' (default 1 for no inhibition). All values must be > 0.
Q1: What is an uncompetitive inhibitor?
A: An inhibitor that binds only to the enzyme-substrate complex, not to the free enzyme.
Q2: How does α' affect the reaction rate?
A: Higher α' values indicate stronger inhibition, decreasing both Vmax and KM.
Q3: What are typical KM values?
A: KM varies widely but is typically in the mM (10-3 mol/L) range for many enzymes.
Q4: How do I determine α' experimentally?
A: Measure reaction rates at different inhibitor concentrations and analyze with Lineweaver-Burk plots.
Q5: What's the difference between competitive and uncompetitive inhibition?
A: Competitive inhibitors bind only to free enzyme, while uncompetitive inhibitors bind only to ES complex.