31.7: Drugs as Enzyme Inhibitors (2023)

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    Learning Objectives
    • Explain what an enzyme inhibitor is.
    • Distinguish between reversible and irreversible inhibitors.
    • Distinguish between competitive and noncompetitive inhibitors.

    Previously, we noted that enzymes are inactivated at high temperatures and by changes in pH. These are nonspecific factors that would inactivate any enzyme. The activity of enzymes can also be regulated by more specific inhibitors. Many compounds are poisons because they bind covalently to particular enzymes or kinds of enzymes and inactivate them (Table \(\PageIndex{1}\)).

    (Video) Pharmaceutical Drugs: Inhibitors and the Nature of Disease

    Table \(\PageIndex{1}\): Poisons as Enzyme Inhibitors
    Poison Formula Example of Enzyme Inhibited Action
    arsenate \(\ce{AsO4^{3−}}\) glyceraldehyde 3-phosphate dehydrogenase substitutes for phosphate
    iodoacetate \(\ce{ICH2COO^{−}}\) triose phosphate dehydrogenase binds to cysteine \(\ce{SH}\) group
    diisopropylfluoro-phosphate (DIFP; a nerve poison) 31.7: Drugs as Enzyme Inhibitors (1) acetylcholinesterase binds to serine \(\ce{OH}\) group

    Irreversible Inhibition: Poisons

    An irreversible inhibitor inactivates an enzyme by bonding covalently to a particular group at the active site. The inhibitor-enzyme bond is so strong that the inhibition cannot be reversed by the addition of excess substrate. The nerve gases, especially Diisopropyl fluorophosphate (DIFP), irreversibly inhibit biological systems by forming an enzyme-inhibitor complex with a specific OH group of serine situated at the active sites of certain enzymes. The peptidases trypsin and chymotrypsin contain serine groups at the active site and are inhibited by DIFP.

    31.7: Drugs as Enzyme Inhibitors (2)

    Reversible Inhibition

    A reversible inhibitor inactivates an enzyme through noncovalent, more easily reversed, interactions. Unlike an irreversible inhibitor, a reversible inhibitor can dissociate from the enzyme. Reversible inhibitors include competitive inhibitors and noncompetitive inhibitors. (There are additional types of reversible inhibitors.) A competitive inhibitor is any compound that bears a structural resemblance to a particular substrate and thus competes with that substrate for binding at the active site of an enzyme. The inhibitor is not acted on by the enzyme but does prevent the substrate from approaching the active site.

    The degree to which a competitive inhibitor interferes with an enzyme’s activity depends on the relative concentrations of the substrate and the inhibitor. If the inhibitor is present in relatively large quantities, it will initially block most of the active sites. But because the binding is reversible, some substrate molecules will eventually bind to the active site and be converted to product. Increasing the substrate concentration promotes displacement of the inhibitor from the active site. Competitive inhibition can be completely reversed by adding substrate so that it reaches a much higher concentration than that of the inhibitor.

    (Video) Enzyme Inhibitors | A-level Biology | OCR, AQA, Edexcel

    Studies of competitive inhibition have provided helpful information about certain enzyme-substrate complexes and the interactions of specific groups at the active sites. As a result, pharmaceutical companies have synthesized drugs that competitively inhibit metabolic processes in bacteria and certain cancer cells. Many drugs are competitive inhibitors of specific enzymes.

    A classic example of competitive inhibition is the effect of malonate on the enzyme activity of succinate dehydrogenase (Figure \(\PageIndex{1}\)). Malonate and succinate are the anions of dicarboxylic acids and contain three and four carbon atoms, respectively. The malonate molecule binds to the active site because the spacing of its carboxyl groups is not greatly different from that of succinate. However, no catalytic reaction occurs because malonate does not have a CH2CH2 group to convert to CH=CH. This reaction will also be discussed in connection with the Krebs cycle and energy production.

    31.7: Drugs as Enzyme Inhibitors (3)
    To Your Health: Penicillin

    Chemotherapy is the strategic use of chemicals (that is, drugs) to destroy infectious microorganisms or cancer cells without causing excessive damage to the other, healthy cells of the host. From bacteria to humans, the metabolic pathways of all living organisms are quite similar, so the search for safe and effective chemotherapeutic agents is a formidable task. Many well-established chemotherapeutic drugs function by inhibiting a critical enzyme in the cells of the invading organism.

    An antibiotic is a compound that kills bacteria; it may come from a natural source such as molds or be synthesized with a structure analogous to a naturally occurring antibacterial compound. Antibiotics constitute no well-defined class of chemically related substances, but many of them work by effectively inhibiting a variety of enzymes essential to bacterial growth.

    Penicillin, one of the most widely used antibiotics in the world, was fortuitously discovered by Alexander Fleming in 1928, when he noticed antibacterial properties in a mold growing on a bacterial culture plate. In 1938, Ernst Chain and Howard Florey began an intensive effort to isolate penicillin from the mold and study its properties. The large quantities of penicillin needed for this research became available through development of a corn-based nutrient medium that the mold loved and through the discovery of a higher-yielding strain of mold at a United States Department of Agriculture research center near Peoria, Illinois. Even so, it was not until 1944 that large quantities of penicillin were being produced and made available for the treatment of bacterial infections.

    (Video) Enzyme Examples, Cofactors/Coenzymes, Inhibitors, and Feedback Inhibition

    Penicillin functions by interfering with the synthesis of cell walls of reproducing bacteria. It does so by inhibiting an enzyme—transpeptidase—that catalyzes the last step in bacterial cell-wall biosynthesis. The defective walls cause bacterial cells to burst. Human cells are not affected because they have cell membranes, not cell walls.

    Several naturally occurring penicillins have been isolated. They are distinguished by different R groups connected to a common structure: a four-member cyclic amide (called a lactam ring) fused to a five-member ring. The addition of appropriate organic compounds to the culture medium leads to the production of the different kinds of penicillin.

    The penicillins are effective against gram-positive bacteria (bacteria capable of being stained by Gram’s stain) and a few gram-negative bacteria (including the intestinal bacterium Escherichia coli). They are effective in the treatment of diphtheria, gonorrhea, pneumonia, syphilis, many pus infections, and certain types of boils. Penicillin G was the earliest penicillin to be used on a wide scale. However, it cannot be administered orally because it is quite unstable; the acidic pH of the stomach converts it to an inactive derivative. The major oral penicillins—penicillin V, ampicillin, and amoxicillin—on the other hand, are acid stable.

    31.7: Drugs as Enzyme Inhibitors (4)

    Some strains of bacteria become resistant to penicillin through a mutation that allows them to synthesize an enzyme—penicillinase—that breaks the antibiotic down (by cleavage of the amide linkage in the lactam ring). To combat these strains, scientists have synthesized penicillin analogs (such as methicillin) that are not inactivated by penicillinase.

    Some people (perhaps 5% of the population) are allergic to penicillin and therefore must be treated with other antibiotics. Their allergic reaction can be so severe that a fatal coma may occur if penicillin is inadvertently administered to them. Fortunately, several other antibiotics have been discovered. Most, including aureomycin and streptomycin, are the products of microbial synthesis. Others, such as the semisynthetic penicillins and tetracyclines, are made by chemical modifications of antibiotics; and some, like chloramphenicol, are manufactured entirely by chemical synthesis. They are as effective as penicillin in destroying infectious microorganisms. Many of these antibiotics exert their effects by blocking protein synthesis in microorganisms.

    (Video) Enzyme inhibition

    Initially, antibiotics were considered miracle drugs, substantially reducing the number of deaths from blood poisoning, pneumonia, and other infectious diseases. Some seven decades ago, a person with a major infection almost always died. Today, such deaths are rare. Seven decades ago, pneumonia was a dreaded killer of people of all ages. Today, it kills only the very old or those ill from other causes. Antibiotics have indeed worked miracles in our time, but even miracle drugs have limitations. Not long after the drugs were first used, disease organisms began to develop strains resistant to them. In a race to stay ahead of resistant bacterial strains, scientists continue to seek new antibiotics. The penicillins have now been partially displaced by related compounds, such as the cephalosporins and vancomycin. Unfortunately, some strains of bacteria have already shown resistance to these antibiotics.

    Some reversible inhibitors are noncompetitive. A noncompetitive inhibitor can combine with either the free enzyme or the enzyme-substrate complex because its binding site on the enzyme is distinct from the active site. Binding of this kind of inhibitor alters the three-dimensional conformation of the enzyme, changing the configuration of the active site with one of two results. Either the enzyme-substrate complex does not form at its normal rate, or, once formed, it does not yield products at the normal rate. Because the inhibitor does not structurally resemble the substrate, the addition of excess substrate does not reverse the inhibitory effect.

    31.7: Drugs as Enzyme Inhibitors (5)

    Feedback inhibition is a normal biochemical process that makes use of noncompetitive inhibitors to control some enzymatic activity. In this process, the final product inhibits the enzyme that catalyzes the first step in a series of reactions. Feedback inhibition is used to regulate the synthesis of many amino acids. For example, bacteria synthesize isoleucine from threonine in a series of five enzyme-catalyzed steps. As the concentration of isoleucine increases, some of it binds as a noncompetitive inhibitor to the first enzyme of the series (threonine deaminase), thus bringing about a decrease in the amount of isoleucine being formed (Figure \(\PageIndex{2}\)).


    An irreversible inhibitor inactivates an enzyme by bonding covalently to a particular group at the active site. A reversible inhibitor inactivates an enzyme through noncovalent, reversible interactions. A competitive inhibitor competes with the substrate for binding at the active site of the enzyme. A noncompetitive inhibitor binds at a site distinct from the active site.


      What drugs act as enzyme inhibitors? ›

      Examples of enzyme-inhibiting agents are cimetidine, erythromycin, ciprofloxacin, and isoniazid.

      How do drugs act as enzyme inhibitors? ›

      Inhibitors. Enzyme inhibitors are compounds which modify the catalytic properties of the enzyme and, therefore, slow down the reaction rate, or in some cases, even stop the catalysis. Such inhibitors work by blocking or distorting the active site.

      What are the 3 types of enzyme inhibitors? ›

      Enzyme inhibition is an important means of regulating activity in living cells. There are three basic types of enzyme inhibition: competitive, noncompetitive, and uncompetitive.

      Can drugs be enzyme inhibitors? ›

      Many drugs are competitive inhibitors of specific enzymes. A classic example of competitive inhibition is the effect of malonate on the enzyme activity of succinate dehydrogenase (Figure 31.7. 1).

      Why are certain drugs called enzyme inhibitors? ›

      Some drugs interfere with this interaction by blocking the binding site of an enzyme and also prevent the binding of the actual substrate with an enzyme. This inhibits the catalytic activity of the enzyme. Therefore, these are called inhibitors.

      Is ibuprofen an enzyme inhibitor? ›

      The main mechanism of action of ibuprofen is the non-selective, reversible inhibition of the cyclooxygenase enzymes COX-1 and COX-2 (coded for by PTGS1 and PTGS2, respectively; Fig. 2) [1].

      What happens when a drug inhibits an enzyme? ›

      Drug-drug interactions

      Enzyme inhibition decreases the rate of drug metabolism, thereby increasing the systemic exposure of a substrate drug, leading to an increased propensity for side effects and potential toxicity.

      What are enzyme inhibitors and why are they important? ›

      A substance that blocks the action of an enzyme. Enzymes help speed up chemical reactions in the body and take part in many cell functions, including cell signaling, growth, and division. In cancer treatment, enzyme inhibitors may be used to block certain enzymes that cancer cells need to grow.

      What are the 2 types of enzyme inhibition? ›

      Explanation: The molecule in the question is classified as an enzyme inhibitor because it inhibits an enzymatic reaction. There are two types of inhibitors; competitive and noncompetitive inhibitors.

      What are the common types of enzyme inhibition? ›

      Types of Inhibition
      • Competitive Inhibition. A competitive inhibitor binds only to free enzyme. ...
      • Noncompetitive Inhibition. ...
      • Uncompetitive Inhibition. ...
      • Allosteric Inhibition. ...
      • Partial Inhibition. ...
      • Tight-Binding Inhibition. ...
      • Time-Dependent Inhibition.
      May 1, 2012

      What are the 2 major types of enzyme inhibitors and how do they work? ›

      Competitive inhibitors bind to the active site. Non-competitive inhibitors bind to the allosteric site. Uncompetitive inhibitors bind to the enzyme-substrate complex. Each of these types of inhibitors keeps the enzyme from doing its job.

      Is Viagra an enzyme inhibitor medication? ›

      Viagra works by inhibiting one specific type of enzyme called a cyclic GMP phosphodiesterase. “There is not just one, but many phosphodiesterases. Different PDEs are expressed in different tissues and in different parts of the cell, and have different physiological functions.

      Is aspirin an enzyme inhibitor? ›

      Aspirin is well known for its analgesic, antipyretic, anti-inflammatory, and anti-platelet aggregation properties, working through the inhibition of the cyclooxygenase (COX) enzyme (17, 56).

      Is omeprazole an enzyme inhibitor? ›

      Omeprazole is a proton pump inhibitor that inhibits secretion of gastric acid by irreversibly blocking the enzyme system of hydrogen/potassium adenosine triphosphatase, the “proton pump” of the gastric parietal cell.

      What are common inhibitors? ›

      Strong inhibitorsWeak inhibitors
      CYP2C19fluconazole(f), fluoxetine(g), fluvoxamine(a), ticlopidine(c)omeprazole
      CYP2D6bupropion, fluoxetine(g), paroxetine, quinidine(h), terbinafineamiodarone(h), celecoxib, cimetidine, clobazam, cobicistat, escitalopram, fluvoxamine(a), labetalol, sertraline, vemurafenib
      6 more rows
      Aug 24, 2022

      What are enzyme inducing drugs? ›

      Examples of enzyme-inducing medicines
      • Antibiotics – rifampicin and rifabutin.
      • Antiepileptics – carbamazepine, eslicarbazepine acetate, oxcarbazepine, perampanel, phenobarbital, phenytoin, primidone, rufinamide and topiramate (doses of 200mg daily or higher)
      • Antiretrovirals – ritonavir, efavirenz and nevirapine.
      Feb 13, 2023

      How many inhibitors are there? ›

      Every three Inhibitors will allow you to upgrade either Aiden's Health, or Stamina. While there are a total of 126 to collect, individual locations can contain between one and three of the upgrade item.

      What is the difference between enzyme inhibition and inhibitor? ›

      Inhibitors that do not contribute to the development of the product carry out the inhibition. The inhibitors can impact both the substrate and the enzyme. The stoppage of enzyme activity is referred to as enzyme inhibition. These enzyme inhibitors can attach to active areas and halt or inhibit further activity.

      What is an example of a competitive enzyme inhibitor? ›

      An example of a competitive inhibitor is the antineoplastic drug methotrexate. Methotrexate has a structure similar to that of the vitamin folic acid (Fig. 4-5). It acts by inhibiting the enzyme dihydrofolate reductase, preventing the regeneration of dihydrofolate from tetrahydrofolate.

      What are the anti-inflammatory enzymes? ›

      Several studies have shown that proteolytic enzymes are effective at reducing inflammation and symptoms related to inflammatory conditions. One study found that injecting the proteolytic enzymes chymotrypsin, trypsin and serratiopeptidase into rats reduced inflammation more than aspirin ( 17 ).

      Is acetaminophen an inhibitor? ›

      Acetaminophen (paracetamol) is a selective cyclooxygenase-2 inhibitor in man.

      What enzyme is in inflammatory? ›

      Glyceraldehyde-3-phosphate dehydrogenase, or GADPH, is another glycolytic enzyme that plays a crucial role in inflammation.

      What is the most common way drugs affect enzymes? ›

      The majority of drugs which act on enzymes act as inhibitors and most of these are competitive, in that they compete for binding with the enzyme's substrate- for example the majority of the original (first generation) kinase inhibitors bind to the ATP pocket of the enzyme.

      Is amoxicillin a reversible or irreversible inhibitor? ›

      Traditionally, irreversible inhibitors have been discovered either through serendipity, such as omeprazole,8 or as natural product derivatives, such as the β-lactam antibiotic amoxicillin derived from penicillin.

      What kind of inhibitor is penicillin? ›

      Penicillin is an active-site inhibitor for four genera of bacteria.

      Are antibiotics enzyme inhibitors? ›

      Antibiotics such as penicillin kill bacteria by inhibiting the enzyme transpeptidase which is required for cell wall synthesis. All antibiotics are not enzyme inhibitors.

      What is an irreversible enzyme inhibitor? ›

      Listen to pronunciation. (eer-ree-VER-sih-bul EN-zime in-HIH-bih-ter) A substance that permanently blocks the action of an enzyme. In cancer treatment, irreversible enzyme inhibitors may block certain enzymes that cancer cells need to grow and may kill cancer cells.

      What is an example of an irreversible enzyme inhibitor? ›

      In irreversible inhibition, the inhibitor binds very tightly to the enzyme either via covalent or non-covalent means and ultimately does not dissociate very easily, if at all, from the enzyme. Some examples of irreversible inhibitors include nerve gas, penicillin and aspirin.

      What are the factors affecting enzyme inhibition? ›

      Enzyme activity can be affected by a variety of factors, such as temperature, pH, and concentration. Enzymes work best within specific temperature and pH ranges, and sub-optimal conditions can cause an enzyme to lose its ability to bind to a substrate.

      What are enzyme 11 inhibitors? ›

      There are certain molecules(inhibitors) which interfere with the enzyme activity and does not lead to the formation of the product. This is known as enzyme inhibition. These inhibitors can bind to the active sites and prevent/interfere with the further activity.

      What is a reversible inhibitor? ›

      A reversible inhibitor is one that, once removed, allows the enzyme it was inhibiting to begin working again. It has no permanent effects on the enzyme - it does not change the shape of the active site, for example.

      What are 5 inhibitors in erectile dysfunction? ›

      [1] There are several available PDE5 inhibitors: sildenafil, vardenafil, tadalafil, and avanafil, which are FDA approved; lodenafil, udenafil, and mirodenafil are the other non-FDA commercially available drugs.

      What is the best pill to stay hard? ›

      The best treatment for erectile dysfunction (ED) is the one that is best for you. Sildenafil (Viagra) and tadalafil (Cialis) are the most commonly prescribed medications for ED, and they have the longest track record. For occasional use, most people start with sildenafil. For regular use, tadalafil can be a better fit.

      Is coffee a PDE5 inhibitor? ›

      Caffeine is a nonselective PDE inhibitor and it also inhibits cGMP-specific PDEs such as PDE5. cGMP causes vasodilatation in blood vessels by regulating their smooth muscle physiology.

      Is ibuprofen an irreversible inhibitor? ›

      As with all of the non-steroidal antiinflammatory drugs (NSAIDs), ibuprofen is a reversible, competitive inhibitor of the catalytic site for AA metabolism within the hydrophobic channel of the COX-1 enzyme.

      What enzymes is inhibited by 325 mg of aspirin? ›

      Aspirin, like the vast majority of NSAIDs, is thought to exert its anti-inflammatory effects through inhibition of cyclooxygenase enzymes (COX enzymes) that regulate the production of prostaglandins.

      What enzyme does aspirin block? ›

      He proved that aspirin and other non-steroid anti-inflammatory drugs (NSAIDs) inhibit the activity of the enzyme now called cyclooxygenase (COX) which leads to the formation of prostaglandins (PGs) that cause inflammation, swelling, pain and fever.

      Is pantoprazole an enzyme inhibitor? ›

      Pantoprazole was a competitive inhibitor of both CYP2C9-catalyzed diclofenac 4'-hydroxylation and CYP3A4-catalyzed midazolam 1'-hydroxylation (K(i) of 6 and 22 microM, respectively), which were at least 2 times more potent than the other PPIs.

      What are digestive enzyme inhibitors in food? ›

      Speaking of sprouts, raw seeds and nuts contain enzyme inhibitors which neutralize some enzymes our body produces. Raw peanuts, for example, are said to contain an especially large amount of enzyme inhibitors. Raw wheat germ is another food that makes enzymes work harder.

      What are the strong CYP3A4 inhibitors? ›

      Potent inhibitors of CYP3A4 include clarithromycin, erythromycin, diltiazem, itraconazole, ketoconazole, ritonavir, verapamil, goldenseal and grapefruit. Inducers of CYP3A4 include phenobarbital, phenytoin, rifampicin, St. John's Wort and glucocorticoids.

      Which drugs are classified as enzyme inducers and enzyme inhibitors? ›

      Examples of enzyme inducers include aminoglutethimide, barbiturates, carbamazepine, glutethimide, griseofulvin, phenytoin, primidone, rifabutin, rifampin, and troglitazone. Some drugs, such as ritonavir, may act as either an enzyme inhibitor or an enzyme inducer, depending on the situation.

      What are two examples for enzyme containing drugs? ›

      UrokinaseMacrophage metalloelastaseenzyme
      AnistreplaseFibrinogen alpha chaintarget
      AnistreplasePlasminogen activator inhibitor 1target
      58 more rows

      What are enzyme inhibitors and what do they do? ›

      A substance that blocks the action of an enzyme. Enzymes help speed up chemical reactions in the body and take part in many cell functions, including cell signaling, growth, and division. In cancer treatment, enzyme inhibitors may be used to block certain enzymes that cancer cells need to grow.

      What are some enzyme inhibitors and what do they do? ›

      1. Enzyme Inhibitors Used As Drugs To Treat Diseases: This is the most common use for enzyme inhibitors because they target human enzymes and try to correct a pathological condition. For example, the drug Viagra contains sildenafil which is an enzyme inhibitor used to treat male erectile dysfunction.

      Are statins enzyme inducers or inhibitors? ›

      ) reductase inhibitors (statins) are a well-established class of drugs in the treatment of hypercholesterolemia, and members of this class have been shown to reduce the risk of cardiovascular morbidity and mortality in patients with or at risk for coronary heart disease (CHD)1,2 in several clinical trials.

      What are the three most common enzymes? ›

      Amylase (made in the mouth and pancreas; breaks down complex carbohydrates) Lipase (made in the pancreas; breaks down fats) Protease (made in the pancreas; breaks down proteins)

      Is gabapentin an enzyme inducer? ›

      Gabapentin, vigabatrin and in particular levetiracetam appear to be devoid of significant enzyme inducing or inhibiting properties.

      Is grapefruit juice an inducer or inhibitor? ›

      Background: Grapefruit juice is a potent inhibitor of CYP3A4-mediated drug metabolism.

      Is St John's wort an inducer or inhibitor? ›

      The available data indicate that St John's wort is a potent inducer of CYP 3A4 and P-glycoprotein (PgP), although it may inhibit or induce other CYPs, depending on the dose, route and duration of administration.

      What is an inhibitor for stomach acid? ›

      Proton-pump inhibitors (PPIs) — medications like esomeprazole (Nexium), omeprazole (Prilosec), lansoprazole (Prevacid, and others) and pantoprazole (Prontonix) — are the most commonly used medications to treat stomach-acid issues.


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