
What are some examples of enzyme inhibitors?
Answer
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Hint: Enzymes have a very narrow range of functions. This means that each enzyme interacts only with the particular form of substance for which it was designed. This is necessary to ensure that enzymes do not cause chemical reactions that they are not expected to.
Complete answer:
All biological processes occur due to anabolism and catabolism; both are chemical reactions, and enzymes control the majority of these chemical reactions . Many life-giving necessary reactions would not occur at all if enzymes weren't present.
Enzyme inhibitors will reduce or completely stop the functioning of the enzyme by binding to its active site. Inhibitors reduce the compatibility of substrate and enzyme by binding to their active sites. Many medications are enzyme inhibitors since blocking an enzyme's function can destroy a pathogen or correct a metabolic imbalance.
Competitive, noncompetitive/mixed, and uncompetitive inhibitors are the three types of reversible inhibitors. Competitive inhibitors compete with substrates for binding to the enzyme at the same time, as the name implies. The inhibitor binds to the active site of an enzyme, which is also where the substrate binds. Non-competitive inhibitors bind to the enzyme and the enzyme–substrate complex in the same way. Inhibitors that aren't competitive bind only to the enzyme–substrate complex. The efficacy of the inhibitor and the concentration of the substrate have different relationships as a result of these different inhibitory mechanisms.
Cimetidine, erythromycin, ciprofloxacin, and isoniazid are examples of enzyme inhibitors. Cimetidine is used to treat ulcers and GERD (gastroesophageal reflux disease), a condition in which acid from the stomach flows backward, causing heartburn and damage to the food pipe. It has the ability to inhibit ALP in an uncompetitive manner.
Antibiotic erythromycin is a type of antibiotic. It's often used to treat lung infections like pneumonia, skin issues like acne and rosacea, dental abscesses, and sexually transmitted infections, among other things. Cytochrome P450 enzyme inhibitors erythromycin and clarithromycin have been linked to clinically relevant interactions.
Cipro is an antibiotic with a wide range of action. This means it's effective against a wide range of bacteria. Many bacteria, however, have developed resistance to Cipro. Ciprofloxacin inhibits cytochrome P450 1A2, a drug-metabolizing enzyme.
Most enzymes are proteins. They are bio catalysts. Catalysts help to speed up chemical reactions. Substrates are the molecules on which enzymes can operate, and the enzyme transforms the substrates into different molecules called products.
Note:
An enzyme is a protein that serves as a catalyst in living organisms, controlling the rate at which chemical reactions occur while remaining unaffected. Some examples of enzymes are maltase, trypsin, amylase etc.
Complete answer:
All biological processes occur due to anabolism and catabolism; both are chemical reactions, and enzymes control the majority of these chemical reactions . Many life-giving necessary reactions would not occur at all if enzymes weren't present.
Enzyme inhibitors will reduce or completely stop the functioning of the enzyme by binding to its active site. Inhibitors reduce the compatibility of substrate and enzyme by binding to their active sites. Many medications are enzyme inhibitors since blocking an enzyme's function can destroy a pathogen or correct a metabolic imbalance.
Competitive, noncompetitive/mixed, and uncompetitive inhibitors are the three types of reversible inhibitors. Competitive inhibitors compete with substrates for binding to the enzyme at the same time, as the name implies. The inhibitor binds to the active site of an enzyme, which is also where the substrate binds. Non-competitive inhibitors bind to the enzyme and the enzyme–substrate complex in the same way. Inhibitors that aren't competitive bind only to the enzyme–substrate complex. The efficacy of the inhibitor and the concentration of the substrate have different relationships as a result of these different inhibitory mechanisms.
Cimetidine, erythromycin, ciprofloxacin, and isoniazid are examples of enzyme inhibitors. Cimetidine is used to treat ulcers and GERD (gastroesophageal reflux disease), a condition in which acid from the stomach flows backward, causing heartburn and damage to the food pipe. It has the ability to inhibit ALP in an uncompetitive manner.
Antibiotic erythromycin is a type of antibiotic. It's often used to treat lung infections like pneumonia, skin issues like acne and rosacea, dental abscesses, and sexually transmitted infections, among other things. Cytochrome P450 enzyme inhibitors erythromycin and clarithromycin have been linked to clinically relevant interactions.
Cipro is an antibiotic with a wide range of action. This means it's effective against a wide range of bacteria. Many bacteria, however, have developed resistance to Cipro. Ciprofloxacin inhibits cytochrome P450 1A2, a drug-metabolizing enzyme.
Most enzymes are proteins. They are bio catalysts. Catalysts help to speed up chemical reactions. Substrates are the molecules on which enzymes can operate, and the enzyme transforms the substrates into different molecules called products.
Note:
An enzyme is a protein that serves as a catalyst in living organisms, controlling the rate at which chemical reactions occur while remaining unaffected. Some examples of enzymes are maltase, trypsin, amylase etc.
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