Formula Used:
Definition: The apparent Michaelis constant (Kmapp) is the Michaelis-Menten constant observed in the presence of a competitive inhibitor, representing the substrate concentration at which the reaction rate is half of Vmax.
Purpose: It helps biochemists understand enzyme kinetics when competitive inhibitors are present, which is crucial for drug development and metabolic studies.
The calculator uses the formula:
Where:
Explanation: The formula calculates how the apparent affinity of the enzyme for its substrate changes in the presence of competitive inhibition.
Details: Understanding Kmapp helps in determining inhibitor potency, designing drugs, and studying enzyme mechanisms in biological systems.
Tips: Enter substrate concentration, maximum rate, initial reaction rate, and tolerance percentage (default ±5%). All values must be positive.
Q1: What's the difference between Km and Kmapp?
A: Km is the Michaelis constant without inhibitor, while Kmapp is the apparent value in the presence of a competitive inhibitor.
Q2: How does competitive inhibition affect Km?
A: Competitive inhibitors increase the apparent Km (Kmapp) without affecting Vmax.
Q3: What units should I use for input values?
A: Use consistent units (mol/m³ for concentrations, mol/m³·s for rates). The calculator will output Kmapp in mol/m³.
Q4: What is the tolerance percentage for?
A: It calculates the ±% range around the calculated Kmapp to account for experimental error (default ±5%).
Q5: Can this calculator be used for non-competitive inhibition?
A: No, this formula is specific for competitive inhibition. Non-competitive inhibition affects Vmax rather than Km.