SUMMARY
An enzyme-catalyzed reaction becomes zeroth order when the substrate concentration significantly exceeds the Michaelis constant (Km), specifically when [S] >> Km. In this scenario, the reaction velocity reaches its maximum (Vmax) and is independent of substrate concentration. The correct answer to the multiple-choice question is option b, indicating that the velocity of enzyme action is very high. This conclusion is based on the understanding that zeroth-order kinetics occur under conditions where substrate concentration is not limiting.
PREREQUISITES
- Understanding of enzyme kinetics and reaction orders
- Familiarity with the Michaelis-Menten equation
- Knowledge of substrate concentration and its effect on enzyme activity
- Basic principles of enzyme catalysis
NEXT STEPS
- Study the Michaelis-Menten equation in detail
- Learn about enzyme inhibition and its effects on reaction kinetics
- Explore the differences between zero-order and first-order kinetics
- Investigate practical applications of enzyme kinetics in biochemical assays
USEFUL FOR
Students studying biochemistry, researchers in enzymology, and professionals involved in biochemical assay development will benefit from this discussion.