Formula Used:
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The Enzyme Inhibitor Dissociation Constant (Ki) is a measure of the affinity between an enzyme and its inhibitor. It represents the concentration of inhibitor required to form half of the enzyme-inhibitor complex under equilibrium conditions.
The calculator uses the formula for noncompetitive inhibition:
Where:
Explanation: This formula calculates the dissociation constant for noncompetitive inhibitors, where the inhibitor binds to both the enzyme and enzyme-substrate complex.
Details: The dissociation constant is crucial for understanding enzyme inhibition mechanisms, drug design, and determining the potency of enzyme inhibitors in biochemical and pharmacological studies.
Tips: Enter inhibitor concentration in mol/m³, maximum rate in mol/m³·s, and apparent maximum rate in mol/m³·s. All values must be positive and non-zero.
Q1: What is the difference between competitive and noncompetitive inhibition?
A: Competitive inhibitors bind only to the free enzyme, while noncompetitive inhibitors can bind to both the free enzyme and the enzyme-substrate complex.
Q2: How does Ki relate to inhibitor potency?
A: Lower Ki values indicate higher inhibitor potency, as less inhibitor is needed to achieve the same level of enzyme inhibition.
Q3: What are typical units for Ki?
A: Ki is typically expressed in concentration units such as mol/m³, M (molar), or mM (millimolar).
Q4: When is this formula applicable?
A: This formula is specifically for noncompetitive inhibition where the inhibitor reduces Vmax but doesn't affect Km.
Q5: How does temperature affect Ki values?
A: Temperature can affect Ki values as it influences both enzyme-inhibitor binding affinity and the stability of the enzyme-inhibitor complex.