What is the difference in zero order kinetics and first order reactions relative to enzyme kinetics?
In first order kinetics, the enzyme is in excess and the substrate concentration is the limiting factor. Enzymes are generally not assayed in this manner due to limited accuracy. In zero order kinetics, the “rate” of the reaction is directly proportional to the enzyme concentration and independent of the substrate concentration. The substrate is provided in excess. The Michaelis-Menten equation describes this relationship and will be studied in more detail in Clinical Chemistry. You are off the hook, for now.
