Question

PLEASE HELP!!!!!!!!!!!!!!!!!!!!!!!!

Which of the following best describes an example of how an enzyme inhibitor can work in a reaction catalyzed by an enzyme?
The enzyme inhibitor catalyzes the reverse reaction, which counteracts the work of the enzyme.
The enzyme inhibitor attacks and destroys the enzyme, which prevents the enzyme from helping in the reaction.
The enzyme inhibitor binds to the products of the reaction, which makes the work of the enzyme unproductive.
The enzyme inhibitor fits into the enzyme’s active site, which prevents the enzyme from catalyzing the reaction.

Answer 1

a

Step-by-step explanation:

Answer 2

I'm not sure but I think it should be the enzyme inhibitor binds to the products of the reaction which makes the enzyme unproductive

Step-by-step explanation:

By binding to enzymes' active sites, inhibitors reduce the compatibility of substrate and enzyme and this leads to the inhibition of Enzyme-Substrate complexes' formation, preventing the catalyzation of reactions and decreasing (at times to zero) the amount of product produced by a reaction. It can be said that as the concentration of enzyme inhibitors increases, the rate of enzyme activity decreases, and thus, the amount of product produced is inversely proportional to the concentration of inhibitor molecules. Since blocking an enzyme's activity can kill a pathogen or correct a metabolic imbalance, many drugs are enzyme inhibitors. The binding of an inhibitor can stop a substrate from entering the enzyme's active site and/or hinder the enzyme from catalyzing its reaction. Inhibitor binding is either reversible or irreversible. Irreversible inhibitors usually react with the enzyme and change it chemically (e.g. via covalent bond formation).