1. What is the Michaelis-Menten Equation?

Definition: The Michaelis-Menten equation describes the rate of enzymatic reactions by relating reaction rate to substrate concentration.

Purpose: It helps biochemists and researchers understand enzyme kinetics and predict reaction rates under different conditions.

2. How Does the Calculator Work?

The calculator uses the Michaelis-Menten equation:

Where:

• \( V_0 \) — Initial reaction rate (mol/m³·s)
• \( V_{max} \) — Maximum reaction rate (mol/m³·s)
• \( [S] \) — Substrate concentration (mol/m³)
• \( K_M \) — Michaelis constant (mol/m³)

Explanation: The equation shows that reaction rate increases with substrate concentration but approaches \( V_{max} \) asymptotically as the enzyme becomes saturated.

3. Importance of Michaelis-Menten Kinetics

Details: Understanding these kinetics is crucial for enzyme characterization, drug development, and metabolic pathway analysis.

4. Using the Calculator

Tips: Enter the maximum rate (\( V_{max} \)), substrate concentration (\( [S] \)), and Michaelis constant (\( K_M \)). All values must be > 0.

5. Frequently Asked Questions (FAQ)

Q1: What does the Michaelis constant represent?
A: \( K_M \) is the substrate concentration at which the reaction rate is half of \( V_{max} \). It indicates enzyme-substrate affinity.

Q2: What units should I use?
A: Consistent units are required (mol/m³ for concentrations, mol/m³·s for rates). Convert your data if necessary.

Q3: When is the reaction rate half of \( V_{max} \)?
A: When \( [S] = K_M \), the reaction rate will be exactly \( V_{max}/2 \).

Q4: What does a low \( K_M \) value indicate?
A: A low \( K_M \) suggests high enzyme-substrate affinity (the enzyme reaches half-maximal rate at low substrate concentrations).

Q5: Can this be used for inhibitor studies?
A: Yes, but inhibitors change \( K_M \) and/or \( V_{max} \) values, which would need to be determined experimentally.