What are the key principles of advanced enzyme kinetics?

What are the key principles of advanced enzyme kinetics?

Advanced enzyme kinetics explores the rates of enzyme-catalyzed reactions, focusing on factors like substrate concentration, enzyme concentration, and the presence of inhibitors.

How do competitive and non-competitive inhibitors affect enzyme activity?

Competitive inhibitors bind to the active site, reducing substrate binding, while non-competitive inhibitors bind elsewhere, affecting the enzyme's function regardless of substrate presence.

Can you explain the Michaelis-Menten equation?

The Michaelis-Menten equation describes the rate of enzymatic reactions by relating reaction rate to substrate concentration, characterized by Vmax and Km.

What is the significance of Km in enzyme kinetics?

Km, or the Michaelis constant, indicates the substrate concentration at which the reaction rate is half of Vmax, reflecting enzyme affinity for the substrate.

Are there any limitations to the Michaelis-Menten model?

Yes, the Michaelis-Menten model assumes a single substrate and enzyme, which may not apply in complex biological systems with multiple substrates or allosteric effects.