Formula Used:
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The Enzyme Substrate Dissociation Constant (Ki') represents the equilibrium constant for the dissociation of an enzyme-substrate complex in the presence of an inhibitor. It quantifies the affinity between the enzyme and substrate when modified by an inhibitor.
The calculator uses the formula:
Where:
Explanation: This formula calculates the modified dissociation constant when an inhibitor affects the enzyme-substrate interaction, where α' represents the factor by which the inhibitor modifies the substrate binding.
Details: Accurate determination of the dissociation constant is crucial for understanding enzyme kinetics, inhibitor effects, and designing effective enzyme inhibition studies in biochemical research and drug development.
Tips: Enter inhibitor concentration in mol/m³ and the enzyme substrate modifying factor. The modifying factor must be greater than 0 and not equal to 1 for valid calculation.
Q1: What does the Enzyme Substrate Modifying Factor represent?
A: The modifying factor (α') quantifies how much an inhibitor affects the binding affinity between the enzyme and substrate.
Q2: Why can't the modifying factor be equal to 1?
A: When α' = 1, the denominator becomes zero, making the equation undefined as the inhibitor would have no effect on the dissociation constant.
Q3: What are typical values for the dissociation constant?
A: Values vary widely depending on the specific enzyme-substrate-inhibitor system, ranging from nanomolar to millimolar concentrations.
Q4: How is this different from the standard dissociation constant?
A: Ki' represents the modified dissociation constant in the presence of an inhibitor, while Kd typically refers to the dissociation constant without inhibitors.
Q5: What units should be used for concentration values?
A: While mol/m³ is used here, consistent units must be maintained throughout the calculation. Conversions may be needed for different unit systems.