Maximum Rate if Substrate Concentration is Higher than Michaelis Constant Calculator

Maximum Rate Formula:

\[ V_{max} = k_{cat} \times [E_0] \]

Maximum Rate (mol/m³·s):

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1. What is Maximum Rate if Substrate Concentration is Higher than Michaelis Constant?

Definition: The maximum rate (V_max) is the maximum reaction velocity achieved when all enzyme active sites are saturated with substrate.

Purpose: This calculation helps biochemists and enzymologists understand enzyme kinetics and predict reaction rates under saturating conditions.

2. How Does the Calculator Work?

The calculator uses the formula:

\[ V_{max} = k_{cat} \times [E_0] \]

Where:

\( V_{max} \) — Maximum reaction rate (mol/m³·s)
\( k_{cat} \) — Catalytic rate constant (s^-1)
\( [E_0] \) — Initial enzyme concentration (mol/m³)

Explanation: The turnover number (k_cat) multiplied by the total enzyme concentration gives the maximum possible reaction rate.

3. Importance of Maximum Rate Calculation

Details: Knowing V_max is crucial for understanding enzyme efficiency, comparing different enzymes, and designing experiments.

4. Using the Calculator

Tips: Enter the catalytic rate constant (k_cat) in s^-1 and initial enzyme concentration in mol/m³. All values must be > 0.

5. Frequently Asked Questions (FAQ)

Q1: What does k_cat represent?
A: k_cat (turnover number) represents the number of substrate molecules converted to product per enzyme active site per second.

Q2: When is substrate concentration considered "higher than Michaelis constant"?
A: When [S] > 10×K_M, the reaction operates near V_max.

Q3: How do I determine k_cat experimentally?
A: Typically determined from V_max measurements at known [E₀] (k_cat = V_max/[E₀]).

Q4: What units should I use for enzyme concentration?
A: mol/m³ is standard, but you can convert from mg/mL using molecular weight.

Q5: Does this calculation account for enzyme inhibition?
A: No, this is the theoretical maximum rate without inhibitors present.