Final answer:
The described inhibitor, where adding more substrate does not reverse its effects, is non-competitive inhibition. This type of inhibitor binds to an allosteric site on the enzyme, changing its shape to reduce its affinity for the substrate. This is distinct from competitive and uncompetitive inhibition.
Step-by-step explanation:
The type of inhibitor described, where adding more substrate does not reverse the effect of the inhibitor, aligns with the characteristics of a Non-competitive Inhibition. In non-competitive inhibition, the inhibitor binds to the enzyme at an allosteric site, a location other than the active site, and manages to block substrate binding to the active site by inducing a conformational change, reducing the enzyme's affinity for its substrate. This inhibition effect persists regardless of further substrate addition.
For comparison, Competitive inhibition involves an inhibitor molecule resembling the substrate and competing for binding at the active site. Increasing substrate concentration can overcome this inhibition type. In Uncompetitive inhibition, the inhibitor binds to the enzyme-substrate complex, preventing the complex from releasing the products and lowering the overall reaction rate.
Learn more about Non-competitive inhibition