Catalytic Efficiency Calculator

Calculate Enzyme Kinetics Parameters

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Catalytic Efficiency (kcat/Km) Calculator

Calculate the catalytic efficiency from kcat and Km values

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Turnover Number (kcat) Calculator

Calculate kcat from Vmax and enzyme concentration

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Specificity Constant Calculator

Calculate specificity constant from experimental data

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Understanding Catalytic Efficiency

What is Catalytic Efficiency?

Catalytic efficiency (kcat/Km) is a measure of how efficiently an enzyme converts substrate to product. It combines both the binding affinity (Km) and catalytic rate (kcat).

Michaelis-Menten Kinetics

Key parameters in enzyme kinetics:

  • Km: Substrate concentration at half-maximum velocity
  • kcat: Maximum turnover rate per enzyme molecule
  • Vmax: Maximum reaction velocity

Specificity Constant

The specificity constant (kcat/Km):

  • Measures enzyme efficiency
  • Units: M⁻¹s⁻¹
  • Higher values indicate better catalysts
  • Limited by diffusion (~10⁸-10⁹ M⁻¹s⁻¹)

Applications

Catalytic efficiency is important in:

  • Drug development
  • Enzyme engineering
  • Metabolic pathways
  • Industrial biotechnology

Factors Affecting Efficiency

Enzyme efficiency can be affected by:

  • Temperature
  • pH
  • Substrate concentration
  • Presence of inhibitors

Essential Enzyme Kinetics Formulas

Catalytic Efficiency

kcat/Km (M⁻¹s⁻¹)

Turnover Number

kcat = Vmax/[E]t

Michaelis-Menten Equation

v = (Vmax[S])/(Km + [S])