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Definition: This calculator determines the initial concentration of enzyme based on the enzyme-substrate complex concentration, dissociation rate constant, and substrate concentration.
Purpose: It helps biochemists and researchers understand enzyme kinetics and quantify enzyme concentrations in reaction systems.
The calculator uses the formula:
Where:
Explanation: The formula calculates the total enzyme concentration by accounting for both free enzyme and enzyme bound in the ES complex.
Details: Knowing the initial enzyme concentration is crucial for determining reaction rates, enzyme efficiency (kcat/Km), and understanding enzyme inhibition mechanisms.
Tips: Enter the enzyme-substrate complex concentration, dissociation rate constant, and substrate concentration. All values must be positive (except KD which can be zero).
Q1: What is the dissociation rate constant (KD)?
A: KD is the equilibrium constant for the dissociation of the enzyme-substrate complex into free enzyme and substrate.
Q2: How do I measure enzyme-substrate complex concentration?
A: ES complex can be measured using spectroscopic methods, rapid-quench techniques, or other kinetic assays.
Q3: What units should I use for the inputs?
A: The calculator uses mol/m³ for all concentrations, but you can convert from other units (e.g., mM to mol/m³ by multiplying by 1000).
Q4: Can KD be zero?
A: Yes, if the enzyme-substrate complex doesn't dissociate, KD would be zero (irreversible binding).
Q5: How does this relate to Michaelis-Menten kinetics?
A: This calculation is fundamental to understanding the relationship between enzyme, substrate, and ES complex in Michaelis-Menten kinetics.