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Michaelis-Menten Equation Calculator

Michaelis-Menten Equation Calculator

Calculate enzyme kinetics parameters using the Michaelis-Menten equation V = (Vmax × [S]) / (Km + [S])

Calculate Enzyme Kinetics

Maximum rate when enzyme is saturated

Initial concentration of substrate

Substrate concentration at half Vmax

Michaelis-Menten Results

0.000000
Reaction Rate (per_second)
Enzyme Efficiency:0.00 M⁻¹s⁻¹
% of Vmax achieved:0.0%
[S]/Km ratio:0

Michaelis-Menten Equation: V = (Vmax × [S]) / (Km + [S])

Input values: Vmax: 0 per_second, [S]: 0 M, Km: 0 M

Kinetics Analysis

Example Calculation

Catalase Enzyme Example

Enzyme: Catalase (breaks down hydrogen peroxide)

Vmax: 1.0 × 10⁻³ M/s

Km: 2.5 × 10⁻² M

Substrate concentration [H₂O₂]: 1.0 × 10⁻² M

Calculation

V = (Vmax × [S]) / (Km + [S])

V = (1.0 × 10⁻³ × 1.0 × 10⁻²) / (2.5 × 10⁻² + 1.0 × 10⁻²)

V = (1.0 × 10⁻⁵) / (3.5 × 10⁻²)

V = 2.86 × 10⁻⁴ M/s

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Enzyme Kinetics Principles

E

Enzyme (E)

Biological catalyst

Lowers activation energy

S

Substrate (S)

Reactant molecule

Binds to enzyme active site

P

Product (P)

Reaction product

Formed from substrate

Key Parameters

Vmax

Maximum reaction rate when enzyme is saturated

Km

Substrate concentration at half Vmax (indicates enzyme affinity)

[S]

Substrate concentration at given time

V

Reaction rate at given substrate concentration

Understanding the Michaelis-Menten Equation

What is the Michaelis-Menten Equation?

The Michaelis-Menten equation describes the kinetics of enzyme-catalyzed reactions. It relates the reaction rate to the substrate concentration and provides insights into enzyme behavior and efficiency.

Key Assumptions

  • Enzyme-substrate complex formation is rapid and reversible
  • Product formation is slow compared to ES complex formation
  • Initial reaction conditions (no product inhibition)
  • Single substrate, single product reaction

Equation Forms

V = (Vmax × [S]) / (Km + [S])

Standard form

Vmax = V × (Km + [S]) / [S]

Solve for Vmax

Km = (Vmax × [S] - V × [S]) / V

Solve for Km

Note: Lower Km values indicate higher enzyme affinity for substrate

Reaction Mechanism

E + S ⇄ ES → E + P

Step 1: Enzyme (E) binds substrate (S) to form complex (ES)

Step 2: Complex breaks down to form product (P) and regenerate enzyme

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