Michaelis Constant Formula:
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Definition: The Michaelis Constant (KM) is numerically equal to the substrate concentration at which the reaction rate is half of the maximum rate of the system.
Purpose: It's a key parameter in enzyme kinetics that indicates the enzyme's affinity for its substrate.
The calculator uses the formula:
Where:
Explanation: The formula calculates KM based on the relationship between substrate concentration, enzyme concentration, catalytic rate, and initial reaction rate.
Details: KM is crucial for understanding enzyme kinetics, determining enzyme efficiency, and comparing different enzymes or substrates.
Tips: Enter all required values in appropriate units. All values must be positive numbers. Typical ranges:
Q1: What does a low KM value indicate?
A: A low KM indicates high enzyme affinity for the substrate, meaning the enzyme reaches half its maximum velocity at low substrate concentrations.
Q2: How is KM related to Vmax?
A: KM is the substrate concentration at which reaction rate is half of Vmax.
Q3: What factors affect KM?
A: Temperature, pH, enzyme and substrate types, and presence of inhibitors or activators.
Q4: Can KM be negative?
A: No, KM is always positive as it represents a concentration.
Q5: How is KM determined experimentally?
A: Typically through Lineweaver-Burk plots or other kinetic studies measuring reaction rates at various substrate concentrations.