Michaelis Constant For Competitive Inhibition Of Enzyme Catalysis Calculator

Michaelis Constant Formula:

\[ KM = \frac{((k2 \times [E0] \times S)/V0)-S}{1+(I/Ki)} \]

Final Rate Constant (k2):

1/s

Initial Enzyme Concentration ([E0]):

mol/m³

Substrate Concentration (S):

mol/m³

Initial Reaction Rate (V0):

mol/m³·s

Inhibitor Concentration (I):

mol/m³

Enzyme Inhibitor Dissociation Constant (Ki):

mol/m³

Michaelis Constant (KM):

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1. What is Michaelis Constant For Competitive Inhibition?

The Michaelis Constant (KM) for competitive inhibition represents the substrate concentration at which the reaction rate is half of the maximum rate in the presence of a competitive inhibitor. It provides insight into enzyme-substrate affinity under inhibitory conditions.

2. How Does the Calculator Work?

The calculator uses the Michaelis Constant formula for competitive inhibition:

\[ KM = \frac{((k2 \times [E0] \times S)/V0)-S}{1+(I/Ki)} \]

Where:

\( k2 \) — Final rate constant (1/s)
\( [E0] \) — Initial enzyme concentration (mol/m³)
\( S \) — Substrate concentration (mol/m³)
\( V0 \) — Initial reaction rate (mol/m³·s)
\( I \) — Inhibitor concentration (mol/m³)
\( Ki \) — Enzyme inhibitor dissociation constant (mol/m³)

Explanation: The formula accounts for the effect of competitive inhibitors on the apparent Michaelis constant, where inhibitors compete with substrates for the enzyme's active site.

3. Importance of Michaelis Constant Calculation

Details: Calculating KM under competitive inhibition conditions is crucial for understanding enzyme kinetics, designing enzyme inhibitors for therapeutic purposes, and studying metabolic pathways regulation.

4. Using the Calculator

Tips: Enter all values in appropriate units. All concentrations must be positive values, and the dissociation constant must be greater than zero for valid results.

5. Frequently Asked Questions (FAQ)

Q1: What is competitive inhibition?
A: Competitive inhibition occurs when an inhibitor molecule competes with the substrate for binding to the enzyme's active site, increasing the apparent KM value.

Q2: How does competitive inhibition affect KM?
A: Competitive inhibition increases the apparent Michaelis constant (KM), meaning more substrate is needed to achieve half-maximal velocity compared to uninhibited reactions.

Q3: What are typical values for Michaelis constant?
A: KM values vary widely depending on the enzyme and substrate, typically ranging from 10⁻⁶ to 10⁻² mol/m³, reflecting the enzyme's affinity for its substrate.

Q4: How is Ki related to inhibitor potency?
A: The inhibition constant (Ki) represents the concentration of inhibitor needed to reduce enzyme activity by half. Lower Ki values indicate more potent inhibitors.

Q5: Can this calculator be used for non-competitive inhibition?
A: No, this specific formula is designed for competitive inhibition. Different equations are used for non-competitive and uncompetitive inhibition types.