Michaelis-Menten Equation:
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Definition: This calculator determines the initial reaction rate (V0) using the Michaelis-Menten equation, which is fundamental in enzyme kinetics.
Purpose: It helps biochemists and researchers understand enzyme kinetics by calculating reaction rates at different substrate concentrations.
The calculator uses the Michaelis-Menten equation:
Where:
Explanation: The equation describes how the reaction rate depends on substrate concentration, with Vmax being the maximum achievable rate and KM being the substrate concentration at half of Vmax.
Details: Understanding enzyme kinetics is crucial for drug development, metabolic pathway analysis, and industrial enzyme applications.
Tips: Enter the maximum reaction rate (Vmax), substrate concentration ([S]), and Michaelis constant (KM). All values must be > 0.
Q1: What is the significance of KM?
A: KM represents the substrate concentration at which the reaction rate is half of Vmax and indicates enzyme-substrate affinity.
Q2: How is this related to Lineweaver-Burk plots?
A: The Lineweaver-Burk plot is a double reciprocal plot (1/V0 vs 1/[S]) that linearizes the Michaelis-Menten equation for easier analysis.
Q3: What are typical units for these measurements?
A: Vmax and V0 are typically in mol/m³·s, [S] in kg/m³, and KM in mol/m³.
Q4: When would reaction rate equal Vmax?
A: When substrate concentration [S] is much greater than KM, the reaction rate approaches Vmax.
Q5: What affects KM values?
A: KM depends on temperature, pH, enzyme and substrate identity, and can be affected by inhibitors.