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Dissociation Constant In Presence Of Noncompetitive Inhibitor Calculator

Formula Used:

\[ K_i = \frac{I}{\left(\frac{V_{max}}{V_{maxapp}} - 1\right)} \]

mol/m³
mol/m³·s
mol/m³·s

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1. What is Enzyme Inhibitor Dissociation Constant?

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 form half of the enzyme-inhibitor complex under equilibrium conditions.

2. How Does the Calculator Work?

The calculator uses the formula for noncompetitive inhibition:

\[ K_i = \frac{I}{\left(\frac{V_{max}}{V_{maxapp}} - 1\right)} \]

Where:

Explanation: This formula calculates the dissociation constant for noncompetitive inhibitors, where the inhibitor binds to both the enzyme and enzyme-substrate complex.

3. Importance of Ki Calculation

Details: The dissociation constant is crucial for understanding enzyme inhibition mechanisms, drug design, and determining the potency of enzyme inhibitors in biochemical and pharmacological studies.

4. Using the Calculator

Tips: Enter inhibitor concentration in mol/m³, maximum rate in mol/m³·s, and apparent maximum rate in mol/m³·s. All values must be positive and non-zero.

5. Frequently Asked Questions (FAQ)

Q1: What is the difference between competitive and noncompetitive inhibition?
A: Competitive inhibitors bind only to the free enzyme, while noncompetitive inhibitors can bind to both the free enzyme and the enzyme-substrate complex.

Q2: How does Ki relate to inhibitor potency?
A: Lower Ki values indicate higher inhibitor potency, as less inhibitor is needed to achieve the same level of enzyme inhibition.

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: When is this formula applicable?
A: This formula is specifically for noncompetitive inhibition where the inhibitor reduces Vmax but doesn't affect Km.

Q5: How does temperature affect Ki values?
A: Temperature can affect Ki values as it influences both enzyme-inhibitor binding affinity and the stability of the enzyme-inhibitor complex.

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