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Enzyme Substrate Modifying Factor Formula:
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The Enzyme Substrate Modifying Factor (α') quantifies how an inhibitor affects the enzyme-substrate complex. It is defined by the inhibitor concentration and the dissociation constant of the enzyme-substrate complex, providing insight into inhibition mechanisms.
The calculator uses the formula:
Where:
Explanation: This formula calculates how much the enzyme-substrate complex is modified in the presence of an inhibitor, based on the ratio of inhibitor concentration to the dissociation constant.
Details: Calculating the modifying factor is essential for understanding enzyme inhibition kinetics, designing pharmacological inhibitors, and studying enzyme-substrate interactions in biochemical systems.
Tips: Enter inhibitor concentration and enzyme substrate dissociation constant in mol/m³. Both values must be positive, with dissociation constant > 0.
Q1: What does a modifying factor greater than 1 indicate?
A: A value greater than 1 indicates the presence of inhibitor molecules affecting the enzyme-substrate complex, with higher values indicating stronger inhibition.
Q2: How is this different from enzyme inhibition constant?
A: While related, the modifying factor specifically quantifies the effect on the enzyme-substrate complex, whereas inhibition constants describe inhibitor binding to free enzyme.
Q3: Can this factor be less than 1?
A: No, the modifying factor is always ≥1 since it represents 1 plus a non-negative ratio of concentrations.
Q4: What are typical values for this factor?
A: Values typically range from 1 (no inhibition) to much higher values depending on inhibitor concentration and binding affinity.
Q5: How does this relate to Michaelis-Menten kinetics?
A: The modifying factor is used in modified Michaelis-Menten equations to account for competitive inhibition effects on enzyme-substrate complexes.