Answer:
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
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).
The answer is C, having many specialized parts.
Be alone make you go faster but be in a community make you go longer.
I don’t think it can So no
<span>ATP
Definition. Adenosine triphosphate, or ATP for short, is the energy currency of life. ATP is a high-energy molecule found in every cell. Its job is to store and supply the cell with needed energy</span>
