how is the effect of inhibitors related to the protein structure of enzymes?
Answers
Explanation:
Inhibition of enzymes
Some molecules very similar to the substrate for an enzyme may be bound to the active site but be unable to react. Such molecules cover the active site and thus prevent the binding of the actual substrate to the site. This inhibition of enzyme action is of a competitive nature, because the inhibitor molecule actually competes with the substrate for the active site. The inhibitor sulfanilamide, for example, is similar enough to a substrate (p-aminobenzoic acid) of an enzyme involved in the metabolism of folic acid that it binds to the enzyme but cannot react. It covers the active site and prevents the binding of p-aminobenzoic acid. This enzyme is essential in certain disease-causing bacteria but is not essential to humans; large amounts of sulfanilamide therefore kill the microorganism but do not harm humans. Inhibitors such as sulfanilamide are called antimetabolites. Sulfanilamide and similar compounds that kill a pathogen without harming its host are widely used in chemotherapy.
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Answer:
The inhibitor changes the shape of the active site to prevent catalysis without preventing binding of the substrate. An inhibitor also can distort the active site by affecting the essential binding group; as a result, the enzyme can no longer attract the substrate.
Temperature: That's a good one. Proteins change shape as temperatures change. Because so much of an enzyme's activity is based on its shape, temperature changes can mess up the process and the enzyme won't work. High enough temperatures will cause the enzyme to denature and have its structure start to break up.
Enzyme inhibitors are substances which alter the catalytic action of the enzyme and consequently slow down, or in some cases, stop catalysis. There are three common types of enzyme inhibition - competitive, non-competitive and substrate inhibition.
Explanation:
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