1. What is Reverse Rate Constant given Michaelis Constant?

Definition: This calculator determines the reverse rate constant (k_r) in enzyme kinetics based on the Michaelis constant (K_M), forward rate constant (k_f), and catalytic rate constant (k_cat).

Purpose: It helps biochemists and enzymologists analyze enzyme kinetics and understand reaction mechanisms.

2. How Does the Calculator Work?

The calculator uses the formula:

Where:

• \( k_r \) — Reverse rate constant (mol/m³·s)
• \( K_M \) — Michaelis constant (mol/m³)
• \( k_f \) — Forward rate constant (s⁻¹)
• \( k_{cat} \) — Catalytic rate constant (s⁻¹)

Explanation: The formula calculates the reverse rate constant from fundamental enzyme kinetic parameters.

3. Importance in Enzyme Kinetics

Details: The reverse rate constant is crucial for understanding enzyme mechanisms, determining reaction equilibrium, and analyzing inhibitor effects.

4. Using the Calculator

Tips: Enter the Michaelis constant (K_M), forward rate constant (k_f), and catalytic rate constant (k_cat). All values must be ≥ 0.

5. Frequently Asked Questions (FAQ)

Q1: What is the Michaelis constant?
A: The substrate concentration at which the reaction rate is half of V_max.

Q2: How is the forward rate constant determined?
A: Typically measured experimentally or calculated from kinetic studies.

Q3: What if I get a negative result?
A: Negative values suggest the catalytic rate exceeds the product (K_M × k_f), which may indicate measurement errors.

Q4: What units should I use?
A: Maintain consistent units (mol/m³ for K_M, s⁻¹ for rate constants).

Q5: How accurate is this calculation?
A: Accuracy depends on the precision of your input parameters.