In most enzyme-catalyzed reactions, the rate of reaction...

Name: Problem 12, Chapter 22: Introduction to General, Organic and Biochemistry
Uploaded: 2021-01-24T03:53:34-08:00
Duration: 2 min 12 s
Channel: Sandra Lundell
Description: In most enzyme-catalyzed reactions, the rate of reaction reaches a constant value with increasing substrate concentration. This relationship is described in a saturation curve diagram (Figure 22.3 ). If the enzyme concentration on a molar basis is twice the maximum substrate concentration, would you obtain a saturation curve?

In most enzyme-catalyzed reactions, the rate of reaction reaches a constant value with increasing substrate concentration. This relationship is described in a saturation curve diagram (Figure 22.3 ). If the enzyme concentration on a molar basis is twice the maximum substrate concentration, would you obtain a saturation curve?

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Key Concepts

Michaelis-Menten Kinetics

This concept describes how enzyme-catalyzed reactions depend on substrate concentration. The Michaelis-Menten model predicts that when substrate concentration is much higher than enzyme concentration, the reaction rate will increase in a hyperbolic manner and eventually level off as the enzyme’s active sites become fully occupied. This model assumes that substrate is in excess relative to the enzyme.

Saturation Curve

A saturation curve graphically represents the relationship between substrate concentration and reaction velocity, showing that at high substrate levels the rate approaches a maximum value (Vmax) because all enzyme molecules are occupied. It emphasizes the phenomenon of enzyme saturation, where additional substrate does not lead to an increase in the reaction rate.

Enzyme-Substrate Concentration Ratio

The ratio of enzyme to substrate concentrations is crucial in enzyme kinetics. For the classical saturation behavior to be observed, the substrate must be present in excess relative to the enzyme. If the enzyme concentration is too high compared to substrate, typical saturation kinetics may not be observed because the limited amount of substrate cannot fully occupy all enzyme molecules, altering the expected hyperbolic relationship.

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