Enzyme Inhibitor Dissociation Constant Formula:
From: | To: |
Definition: The Enzyme Inhibitor Dissociation Constant (Ki) measures the affinity between an enzyme and its inhibitor.
Purpose: It helps biochemists understand enzyme inhibition mechanisms and design effective inhibitors for therapeutic or research purposes.
The calculator uses the formula:
Where:
Explanation: The formula calculates the dissociation constant by comparing the apparent enzyme concentration in the presence of inhibitor with the actual enzyme concentration.
Details: A lower Ki value indicates stronger inhibitor binding. This is crucial for drug development and understanding metabolic pathways.
Tips: Enter the inhibitor concentration, initial enzyme concentration, and apparent initial enzyme concentration. All values must be > 0.
Q1: What does a high Ki value indicate?
A: A high Ki indicates weak binding between the enzyme and inhibitor.
Q2: How is apparent enzyme concentration different from actual concentration?
A: Apparent concentration is measured in the presence of inhibitor and reflects reduced enzyme activity.
Q3: What units should I use for concentrations?
A: The calculator uses mol/m³, but you can convert from molarity (M) by multiplying by 1000 (1 M = 1000 mol/m³).
Q4: Can this calculator be used for competitive inhibitors?
A: This specific formula is for non-competitive inhibitors. Competitive inhibitors require a different calculation.
Q5: What's a typical range for Ki values?
A: Ki values typically range from 10-12 to 10-3 mol/m³, depending on the enzyme-inhibitor pair.