Catalytic Rate Constant Formula:
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Definition: The catalytic rate constant (kcat) is the rate constant for conversion of the enzyme-substrate complex to enzyme and product.
Purpose: It measures the number of substrate molecules converted to product per enzyme molecule per second when the enzyme is saturated with substrate.
The calculator uses the formula:
Where:
Explanation: The formula calculates the turnover number of an enzyme at low substrate concentrations relative to KM.
Details: kcat is a fundamental parameter in enzyme kinetics that indicates the catalytic efficiency of an enzyme. Higher values indicate more efficient enzymes.
Tips: Enter the initial reaction rate, Michaelis constant, initial enzyme concentration, and substrate concentration. All values must be > 0.
Q1: What does kcat tell us about an enzyme?
A: It indicates how many substrate molecules one enzyme molecule can convert to product per second when fully saturated.
Q2: What are typical values for kcat?
A: Values range from 1 to 10⁷ s⁻¹, with most enzymes falling between 10² and 10⁴ s⁻¹.
Q3: How is kcat related to enzyme efficiency?
A: The catalytic efficiency is given by kcat/KM, combining both catalytic power and substrate binding affinity.
Q4: When is this formula most accurate?
A: When substrate concentration is much lower than KM, under initial rate conditions.
Q5: What units should I use for the inputs?
A: Use consistent units - mol/m³ for concentrations and mol/m³·s for reaction rate.