The binding of a compound to an enzyme is observed to slow down or stop the rate of the reaction catalyzed by the enzyme. Increa
sing the substrate concentration reduces the inhibitory effects of this compound. Which of the following could account for this observation? View Available Hint(s) The binding of a compound to an enzyme is observed to slow down or stop the rate of the reaction catalyzed by the enzyme. Increasing the substrate concentration reduces the inhibitory effects of this compound. Which of the following could account for this observation? A. The compound is a competitive inhibitor.B. The compound causes a cofactor to be lost from the enzyme. C.The compound is an allosteric inhibitor. D. The compound reduces disulfide bonds, causing the enzyme molecules to partially unfold. E. The compound forms a covalent bond with one of the amino acid residues needed for enzyme activity.
The correct answer is A the compound is a competitive inhibitor
Explanation:
Competitive inhibitor competes with the substrate to bind to the active site of the target enzyme and after binding to the active site the inhibitor slow down or stop the reaction catalyzed by that enzyme.
Competitive inhibitor basically effects the Km value of the enzyme thus decreasing the activity of the later.
Increasing the substrate concentrationdisplace the inhibitor from the enzyme"s active site thus reducing the inhibitory effects of the later thus increasing the activity of the enzyme.
Helper T cells are activated by peptide antigens by MHC class II molecules. These antigens express on the surface of antigen-presenting cells (APCs). After activation, the T helper cells divide and secrete cytokines to assist the immune response.
