Final Rate Constant For Competitive Inhibition Of Enzyme Catalysis Calculator

Formula Used:

\[ k_{final} = \frac{V_0 \times (K_M \times (1 + \frac{I}{K_i}) + S)}{[E_0] \times S} \]

Initial Reaction Rate (V₀):

mol/m³·s

Michaelis Constant (K_M):

mol/m³

Inhibitor Concentration (I):

mol/m³

Enzyme Inhibitor Dissociation Constant (K_i):

mol/m³

Substrate Concentration (S):

mol/m³

Initial Enzyme Concentration ([E₀]):

mol/m³

Final Rate Constant for Catalysis (k_final):

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1. What is Final Rate Constant for Competitive Inhibition?

The Final Rate Constant for Competitive Inhibition of Enzyme Catalysis represents the rate constant when the enzyme-substrate complex, upon reaction with an inhibitor, is converted into the enzyme catalyst and product. It quantifies the catalytic efficiency under competitive inhibition conditions.

2. How Does the Calculator Work?

The calculator uses the formula:

\[ k_{final} = \frac{V_0 \times (K_M \times (1 + \frac{I}{K_i}) + S)}{[E_0] \times S} \]

Where:

\( k_{final} \) — Final rate constant for catalysis (s⁻¹)
\( V_0 \) — Initial reaction rate (mol/m³·s)
\( K_M \) — Michaelis constant (mol/m³)
\( I \) — Inhibitor concentration (mol/m³)
\( K_i \) — Enzyme inhibitor dissociation constant (mol/m³)
\( S \) — Substrate concentration (mol/m³)
\( [E_0] \) — Initial enzyme concentration (mol/m³)

Explanation: This formula accounts for the effect of competitive inhibition on the enzyme's catalytic rate constant, incorporating both substrate and inhibitor concentrations.

3. Importance of Final Rate Constant Calculation

Details: Calculating the final rate constant is crucial for understanding enzyme kinetics under inhibitory conditions, designing enzyme-based industrial processes, and developing pharmaceutical inhibitors for therapeutic applications.

4. Using the Calculator

Tips: Enter all values in appropriate units (mol/m³ for concentrations, mol/m³·s for reaction rate). Ensure all values are positive and non-zero for accurate calculation.

5. Frequently Asked Questions (FAQ)

Q1: What is competitive inhibition?
A: Competitive inhibition occurs when an inhibitor molecule competes with the substrate for binding to the enzyme's active site, reducing the enzyme's effective catalytic activity.

Q2: How does K_i affect the final rate constant?
A: A smaller K_i value indicates stronger inhibitor binding, leading to a greater reduction in the final rate constant and more effective inhibition.

Q3: What are typical values for these parameters?
A: Values vary widely depending on the specific enzyme system. K_M typically ranges from 10⁻⁶ to 10⁻² M, while K_i values for effective inhibitors are often in the nanomolar to micromolar range.

Q4: Can this calculator be used for non-competitive inhibition?
A: No, this specific formula is designed for competitive inhibition. Different equations are required for non-competitive and uncompetitive inhibition mechanisms.

Q5: What are the limitations of this calculation?
A: This model assumes ideal competitive inhibition behavior and may not accurately describe systems with mixed inhibition, allosteric effects, or enzyme inactivation over time.