Enzyme Conservation Law Formula:
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The Enzyme Conservation Law states that the total enzyme concentration remains constant throughout a reaction. In the presence of inhibitors, the free enzyme concentration can be calculated by subtracting the concentrations of enzyme-substrate and enzyme-inhibitor complexes from the initial enzyme concentration.
The calculator uses the enzyme conservation law formula:
Where:
Explanation: This formula accounts for the distribution of enzyme molecules between free form, substrate-bound form, and inhibitor-bound form in enzymatic reactions with competitive inhibition.
Details: Accurate determination of free enzyme concentration is crucial for understanding enzyme kinetics, calculating reaction rates, and studying inhibition mechanisms in biochemical systems.
Tips: Enter initial enzyme concentration, enzyme-substrate complex concentration, and enzyme-inhibitor complex concentration in mol/m³. All values must be non-negative and the sum of ES and EI should not exceed the initial enzyme concentration.
Q1: What types of inhibition does this formula apply to?
A: This formula applies to competitive inhibition where the inhibitor binds to the same site as the substrate, forming an enzyme-inhibitor complex.
Q2: Can this formula be used for non-competitive inhibition?
A: For non-competitive inhibition, additional terms may be needed as inhibitors can bind to both free enzyme and enzyme-substrate complex.
Q3: What are typical units for enzyme concentrations?
A: Enzyme concentrations are typically measured in mol/m³ (SI units) or mol/L. The calculator uses mol/m³ for consistency.
Q4: What if the calculated catalyst concentration is negative?
A: A negative result indicates invalid input where the sum of ES and EI exceeds the initial enzyme concentration, which violates the conservation law.
Q5: How is this related to Michaelis-Menten kinetics?
A: This conservation law forms the basis for deriving the modified Michaelis-Menten equation for competitive inhibition scenarios.