BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The Michaelis-Menten equation arises from the general equation for an enzymatic reaction: E + S ↔ ES ↔ E + P, where E is the enzyme, S is the substrate, ES is the enzyme-substrate complex, and P is the product.

Detailed explanation-2: -The Michaelis–Menten equation (Eqn (4)) is the rate equation for a one-substrate enzyme-catalyzed reaction. This equation relates the initial reaction rate (v0), the maximum reaction rate (Vmax), and the initial substrate concentration [S] through the Michaelis constant KM-a measure of the substrate-binding affinity.

Detailed explanation-3: -Et is the concentration of enzyme catalytic sites. If the enzyme has multiple subunits, note that Et is the concentration of catalytic sites, which can be larger than the concentration of enzyme molecules.

Detailed explanation-4: -In a Michaelis-Menten plot of enzyme kinetics, the reaction rate is plotted as a function of substrate concentration. Why is it that as substrate concentration increases, the curve of the graph levels off and reaches a plateau?