Final answer:
Enzymes do not change the equilibrium point of a reaction but speed up the rate at which equilibrium is reached. Vmax can be measured by the amount of product during late reaction stages, and competitive inhibitors usually bind reversibly, affecting Km rather than Vmax.
Step-by-step explanation:
Regarding the statements about enzymes:
- False - Enzymes do not alter the equilibrium point of a reaction. They accelerate the rate at which equilibrium is reached without changing the position of the equilibrium itself.
- True - Vmax can indeed be determined by measuring the amount of product accumulated late in the reaction. This represents the maximum reaction rate that can be achieved when the enzyme is saturated with substrate.
- False - Competitive inhibitors compete with the substrate for binding to the enzyme active site, which is usually reversible, not irreversible. They do not lower the Vmax but instead increase the apparent Km.
The subject of enzymes is a central topic in biology, particularly in understanding how biochemical reactions are catalyzed and regulated within living organisms.