What are the key kinetic parameters in enzyme kinetics?

What are the key kinetic parameters in enzyme kinetics?

The key kinetic parameters in enzyme kinetics include Vmax, Km, and kcat. Vmax is the maximum reaction rate, Km is the substrate concentration at which the reaction rate is half of Vmax, and kcat is the turnover number.

How do you determine Vmax and Km experimentally?

Vmax and Km can be determined using Michaelis-Menten kinetics. You can plot the reaction rate against substrate concentration and fit the data to the Michaelis-Menten equation.

What is the significance of kcat in enzyme activity?

kcat, or the turnover number, indicates how many substrate molecules an enzyme converts to product per unit time when fully saturated with substrate. It's a measure of enzyme efficiency.

Can you explain the difference between competitive and non-competitive inhibition?

Sure! Competitive inhibition occurs when an inhibitor competes with the substrate for the active site, increasing Km without affecting Vmax. Non-competitive inhibition occurs when the inhibitor binds to an allosteric site, decreasing Vmax without affecting Km.