Michaelis-Menten Calculator
Calculate enzyme reaction velocity using the Michaelis-Menten equation for enzyme kinetics
Km = substrate concentration at ½Vmax
Understanding Michaelis-Menten Kinetics
The Michaelis-Menten equation is fundamental to enzyme kinetics, describing how the rate of an enzyme-catalyzed reaction depends on substrate concentration. It provides crucial parameters that characterize enzyme efficiency and affinity for substrates.
The Michaelis-Menten Equation
v = (Vmax × [S]) / (Km + [S])
Enzyme reaction velocity equation
v = Reaction velocity
The rate at which product is formed (units: M/s, µM/min, etc.)
Vmax = Maximum velocity
The maximum rate when enzyme is saturated with substrate
[S] = Substrate concentration
The concentration of the substrate (units: M, mM, µM)
Km = Michaelis constant
The substrate concentration at which v = ½Vmax (same units as [S])
Understanding Km
The Michaelis constant (Km) is a key parameter that indicates:
- Low Km (e.g., 10 µM): High enzyme-substrate affinity, enzyme binds substrate tightly
- High Km (e.g., 10 mM): Low enzyme-substrate affinity, weak binding
- Practical meaning: Km represents the substrate concentration needed to reach half-maximum velocity
Practical Example
Hexokinase Enzyme
- Vmax = 100 µM/min
- Km = 0.1 mM (100 µM)
- [Glucose] = 0.2 mM (200 µM)
v = (100 × 200) / (100 + 200)
v = 20,000 / 300
v = 66.67 µM/min
This is 66.67% of Vmax, showing the enzyme is working efficiently at this substrate concentration
Key Concepts
🧬 Enzyme-Substrate Complex
E + S ⇌ ES → E + P (Formation of ES complex is key)
📊 Saturation Kinetics
At high [S], all enzyme active sites are occupied
⚡ Catalytic Efficiency
kcat/Km ratio measures enzyme efficiency
🎯 Steady State
[ES] remains constant during the reaction
Experimental Determination
Lineweaver-Burk Plot
A double reciprocal plot (1/v vs 1/[S]) linearizes the Michaelis-Menten equation:
1/v = (Km/Vmax) × (1/[S]) + 1/Vmax
- • y-intercept = 1/Vmax
- • x-intercept = -1/Km
- • slope = Km/Vmax
Applications
- 💊Drug Development: Understanding enzyme inhibition for designing pharmaceuticals
- 🧬Metabolic Studies: Analyzing metabolic pathways and enzyme deficiencies
- 🔬Diagnostic Assays: Clinical enzyme assays for disease detection
- 🏭Industrial Biotechnology: Optimizing enzyme-based production processes
- 🧪Research: Characterizing new enzymes and understanding catalytic mechanisms
- 🌱Agriculture: Studying plant enzymes for crop improvement
🧬Quick Reference
Units:
M/s, µM/min, mM/s
Formula:
v = (Vmax × [S]) / (Km + [S])
At Km:
v = ½Vmax
Applications:
Enzyme kinetics, drug design
Level:
College Biochemistry
🔗Related Calculators
📐Related Formulas
🎯Where It's Used
- 💊
Pharmaceutical Industry
Drug design and testing
- 🏥
Clinical Diagnostics
Enzyme activity assays
- 🔬
Research
Enzyme characterization
- 🏭
Biotechnology
Industrial enzyme optimization