Understanding Enzyme Kinetics

Easy Biochemistry Enzymes

Enzymes are biological catalysts that speed up biochemical reactions by lowering the activation energy. Each enzyme is highly specific to its substrate, often influenced by its structure. Consider the following scenario involving an enzyme that catalyzes the hydrolysis of a carbohydrate substrate into monosaccharides. This enzyme is known to follow Michaelis-Menten kinetics, and its activity is affected by various factors including substrate concentration, temperature, and pH.

Under conditions where the substrate concentration is much lower than the enzyme's Km (Michaelis constant), the reaction rate increases linearly with substrate concentration. However, as the substrate concentration approaches saturation, the rate of reaction reaches a maximum velocity (Vmax), illustrating the enzyme's saturation point. Which of the following statements best describes the characteristics of this enzyme's activity?

The enzyme activity increases indefinitely with increasing substrate concentration.

The enzyme activity shows a hyperbolic relationship with substrate concentration up to a certain point.

The enzyme remains inactive at high substrate concentrations.

The enzyme's activity is unaffected by changes in substrate concentration.

Hint

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