Answer:
C. The inhibitor binds to the enzyme's active site, because its shape is similar to that of the substrate.
Explanation:
An enzyme can be defined as a biological catalyst that typically lowers the activation energy of a biological reaction. When the activation energy of a reaction is low, the rate of the reaction would be faster. Therefore, an enzyme speeds or catalyzes the rate of a reaction by lowering its activation energy. Also, if the conditions are not optimal for an enzyme, it limits the ability of an enzyme to bind or be joined with its substrates.
Generally, enzymes function best at a specific pH and temperature level. An increase in temperature increases or speeds up the rate of a reaction while low temperature limits or reduces the rate of a reaction. The optimal temperature for enzymes in the human body is around 37 degrees celsius.
An allosteric effector can be defined as an agent, organ or molecule that is being binded to an enzyme at a site, thereby causing a reduction (negative effect) or an increase (positive effect) in an enzyme activity.
An inhibitor is any substance that slows down or stops a biological process or chemical reaction.
Hence, the statement which best describes the function of a competitive inhibitor in an enzyme-catalyzed reaction is that the inhibitor binds to the enzyme's active site, because its shape is similar to that of the substrate and consequently, slowing down or stopping the process.
