Answer:
The correct answer is d
Explanation:
Allosteric enzymes have multiple binding sites to different ligands called allosteric sites (different from the active site), these ligands can modify their kinetic properties. They are generally made up of more than one polypeptide chain, and have a quaternary structure, an enzyme with a quaternary structure can bind more than one substrate molecule. An allosteric enzyme is an enzyme whose activity is regulated by an allosteric center, which is a site, other than the active center of the enzyme, to which a regulator (called an allosteric regulator) binds in a reversible and non-covalent manner. The binding of this regulator modifies the three-dimensional structure of the enzyme and affects the configuration of the active site, thus increasing or decreasing its activity, depending on the case. The allosteric sites present in regulatory enzymes is where allosteric effectors or inhibitors are attached, causing a conformational change in the substrate binding site or catalytic site, thus regulating enzyme activity.
Answer:
Disulfiram is a drug used to support the treatment of chronic alcoholism by producing an acute sensitivity to ethanol by inhibiting the enzyme acetaldehyde dehydrogenase, an enzyme which catalyze the conversion of acetaldehyde into acetic acid. Thus, in the presence of disulfiram, the concentration of acetic acid is reduced
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Given what we know, we can confirm that If a single protein carries out multiple functions, then each function may be carried out by a specific region of the protein called a domain.
<h3>What is a domain in proteins?</h3>
This is one of the many parts that make up a protein. This is what we can call the most independent parts of a protein given that they are each self-stabilizing and form their own three-dimensional structures. Each domain of a protein is considered a functional group, and therefore a single protein can carry out multiple functions.
Therefore, we can confirm that for a protein like the one described in the question, the multiple functions being carried out can be explained by the presence of the domain regions of the protein.
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