1. What is Maximum Reaction Rate in Presence of Uncompetitive Inhibitor?

Definition: This calculator determines the maximum reaction rate (V_max) of an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor.

Purpose: It helps biochemists and researchers understand how uncompetitive inhibitors affect enzyme kinetics and reaction rates.

2. How Does the Calculator Work?

The calculator uses the formula:

Where:

• \( V_{max} \) — Maximum reaction rate (mol/m³·s)
• \( V_0 \) — Initial reaction rate (mol/m³·s)
• \( K_M \) — Michaelis constant (mol/m³)
• \( \alpha' \) — Enzyme substrate modifying factor
• \( S \) — Substrate concentration (mol/m³)

Explanation: The formula accounts for the effect of an uncompetitive inhibitor on the enzyme's maximum reaction rate.

3. Importance of Maximum Reaction Rate Calculation

Details: Understanding the maximum reaction rate helps in drug development, enzyme characterization, and biochemical research.

4. Using the Calculator

Tips: Enter the initial reaction rate, Michaelis constant, enzyme substrate modifying factor, and substrate concentration. All values must be positive.

5. Frequently Asked Questions (FAQ)

Q1: What is an uncompetitive inhibitor?
A: An uncompetitive inhibitor binds only to the enzyme-substrate complex, not to the free enzyme.

Q2: How does α' affect the reaction rate?
A: α' represents how much the inhibitor affects the enzyme-substrate complex's dissociation constant.

Q3: What are typical values for Kₘ?
A: Kₘ values vary widely depending on the enzyme and substrate, ranging from 10⁻⁶ to 10⁻² M.

Q4: Why does Vmax change with uncompetitive inhibition?
A: Unlike competitive inhibition, uncompetitive inhibition decreases both Vmax and apparent Kₘ.

Q5: How is this different from competitive inhibition?
A: Competitive inhibitors affect Kₘ but not Vmax, while uncompetitive inhibitors affect both.