Apparent Michaelis Constant Formula:
Definition: The Apparent Michaelis Constant is defined as the Michaelis-Menten constant in the presence of a competitive inhibitor.
Purpose: It helps biochemists and enzymologists understand how inhibitors affect enzyme kinetics.
The calculator uses the formula:
Where:
Explanation: The Michaelis Constant is multiplied by a factor that accounts for the inhibitor concentration relative to its dissociation constant.
Details: This calculation is crucial for understanding competitive inhibition in enzyme kinetics and drug interactions.
Tips: Enter the Michaelis Constant, Inhibitor Concentration, and Dissociation Constant. All values must be > 0 (except inhibitor can be 0).
Q1: What does the apparent Michaelis constant tell us?
A: It shows how much a competitive inhibitor increases the measured KM of an enzyme reaction.
Q2: What's a typical value for Ki?
A: This varies widely depending on the enzyme and inhibitor, often in the micromolar to millimolar range.
Q3: When would Kmapp equal KM?
A: When [I] = 0 (no inhibitor present) or when Ki is very large (very weak binding).
Q4: How does this relate to drug development?
A: Competitive inhibitors are often drug candidates, and this calculation helps predict their effects.
Q5: Can this calculator be used for non-competitive inhibition?
A: No, this formula is specific for competitive inhibition.