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 occupy half of the enzyme's active sites and is measured by titrating inhibitor into an enzyme solution while monitoring heat changes.
The calculator uses the formula:
Where:
Explanation: This formula calculates the dissociation constant for competitive inhibitors by comparing the apparent Michaelis constant in the presence of inhibitor with the true Michaelis constant.
Details: The dissociation constant is crucial for understanding enzyme-inhibitor interactions, determining inhibitor potency, and designing effective enzyme inhibitors for therapeutic applications.
Tips: Enter inhibitor concentration, apparent Michaelis constant, and Michaelis constant in mol/m³. All values must be positive, and Kmapp must be greater than KM for a valid result.
Q1: What does a lower Ki value indicate?
A: A lower Ki value indicates stronger inhibitor binding and higher affinity between the enzyme and inhibitor.
Q2: When is this formula applicable?
A: This formula is specifically for competitive inhibitors where the inhibitor binds to the enzyme's active site.
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: How does Ki relate to IC50?
A: For competitive inhibitors, Ki can be calculated from IC50 using the Cheng-Prusoff equation when substrate concentration and KM are known.
Q5: What factors can affect Ki measurements?
A: Temperature, pH, ionic strength, and the presence of other molecules can influence Ki values and should be controlled during measurements.