Final answer:
Competitive inhibitors compete with the substrate for the active site and do not affect the maximal reaction rate, while noncompetitive inhibitors bind to a separate site,
Step-by-step explanation:
Comparing and contrasting competitive inhibitors and noncompetitive inhibitors reveals distinct differences in their interaction with enzymes. Competitive inhibitors bind reversibly at the enzyme's active site, directly competing with the substrate because of their structural similarity. This reversible binding affects the initial rate of the reaction but not the maximal rate; the inhibition is concentration-dependent, meaning high substrate concentration can overcome the inhibition.altering enzyme conformation and decreasing the maximal reaction rate.
In contrast, noncompetitive inhibitors bind to a separate site, which is not the active site, and thus have a different mode of action. They alter the enzyme's three-dimensional conformation, affecting the active site indirectly. This results in a decreased maximal rate of reaction, as it changes either the rate of formation or the activity of the enzyme-substrate complex. Even with increased substrate concentration, the inhibition by a noncompetitive inhibitor cannot be overcome due to the alteration in enzyme structure.