Enzyme Substrate Complex Concentration For Competitive Inhibition Of Enzyme Catalysis Calculator

Formula Used:

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

Substrate Concentration (S):

mol/m³

Initial Enzyme Concentration ([E₀]):

mol/m³

Michaelis Constant (Kₘ):

mol/m³

Inhibitor Concentration (I):

mol/m³

Enzyme Inhibitor Dissociation Constant (Kᵢ):

mol/m³

Enzyme Substrate Complex Concentration (ES):

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1. What is Enzyme Substrate Complex Concentration?

The Enzyme Substrate Complex Concentration is defined as the concentration of intermediate formed from the reaction of enzyme and substrate in competitive inhibition scenarios. It represents the amount of enzyme bound to substrate at a given time.

2. How Does the Calculator Work?

The calculator uses the competitive inhibition formula:

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

Where:

\( ES \) — Enzyme Substrate Complex Concentration (mol/m³)
\( S \) — Substrate Concentration (mol/m³)
\( [E_0] \) — Initial Enzyme Concentration (mol/m³)
\( K_M \) — Michaelis Constant (mol/m³)
\( I \) — Inhibitor Concentration (mol/m³)
\( K_i \) — Enzyme Inhibitor Dissociation Constant (mol/m³)

Explanation: This formula calculates the concentration of enzyme-substrate complex in the presence of a competitive inhibitor, which competes with the substrate for the enzyme's active site.

3. Importance of ES Calculation

Details: Calculating enzyme-substrate complex concentration is crucial for understanding enzyme kinetics, determining reaction rates, and studying the effects of inhibitors on enzymatic reactions in biochemical systems.

4. Using the Calculator

Tips: Enter all concentration values in mol/m³. Ensure all values are positive (concentrations > 0) for accurate calculation. The inhibitor concentration can be zero if no inhibitor is present.

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, increasing the apparent Kₘ value.

Q2: How does competitive inhibition affect enzyme kinetics?
A: Competitive inhibition increases the apparent Michaelis constant (Kₘ) without affecting the maximum reaction rate (Vₘₐₓ), meaning more substrate is needed to achieve half-maximal velocity.

Q3: What are typical values for Kᵢ?
A: Kᵢ values vary widely depending on the enzyme and inhibitor, ranging from nanomolar to millimolar concentrations, indicating the inhibitor's binding affinity.

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

Q5: What are the limitations of this calculation?
A: This calculation assumes steady-state conditions, ideal behavior, and that the inhibitor is purely competitive. It may not account for more complex inhibition patterns or allosteric effects.