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Chemistry LibreTexts

14.1: Enzymes

  • Page ID
    58856
  • Learning Outcomes

    • Explain the role of an enzyme in the body.
    • Define active site, substrate, and allosteric site.
    • Distinguish between competitive and noncompetitive inhibitors.
    • Describe the lock and key vs. induced-fit model of enzymes.
    • Provide the characteristics of a cofactor and a coenzyme.
    • Describe how substrate concentration, pH, and temperature affect enzyme activity.
    • Interpret graphs of reaction rate vs. reaction conditions.

    The first enzyme to be isolated was discovered in 1926 by American chemist James Sumner, who crystallized the protein. The enzyme was urease, which catalyzes the hydrolytic decomposition of urea, a component of urine, into ammonia and carbon dioxide.

    \[\ce{H_2NCON_2} \left( aq \right) + \ce{H_2O} \left( l \right) \overset{\text{urease}}{\rightarrow} 2 \ce{NH_3} \left( g \right) + \ce{CO_2} \left( g \right)\]

    His discovery was ridiculed at first because nobody believed that enzymes would behave the same way that other chemicals did. Sumner was eventually proven right and won the Nobel Prize in Chemistry in 1946.

    Enzymes and Biochemical Reactions

    Most chemical reactions within organisms would be impossible under the conditions in cells. For example, the body temperature of most organisms is too low for reactions to occur quickly enough to carry out life processes. Reactants may also be present in such low concentrations that it is unlikely they will meet and collide. Therefore, the rate of most biochemical reactions must be increased by a catalyst. A catalyst is a chemical that speeds up chemical reactions. In organisms, catalysts are called enzymes. Essentially, enzymes are biological catalysts.

    Like other catalysts, enzymes are not reactants in the reactions they control. They help the reactants interact but are not used up in the reactions. Instead, they may be used over and over again. Unlike other catalysts, enzymes are usually highly specific for particular chemical reactions. They generally catalyze only one or a few types of reactions.

    Enzymes are extremely efficient in speeding up reactions. They can catalyze up to several million reactions per second. As a result, the difference in rates of biochemical reactions with and without enzymes may be enormous. A typical biochemical reaction might take hours or even days to occur under normal cellular conditions without an enzyme, but less than a second with an enzyme.

    Figure 14.1.1 diagrams a typical enzymatic reaction. A substrate is the molecule or molecules on which the enzyme acts. In the urease catalyzed reaction, urea is the substrate.

    Diagram of enzymatic action
    Figure 14.1.1: The sequence of steps for a substrate binding to an enzyme in its active site, reacting, then being released as products.

    The first step in the reaction is that the substrate binds to a specific part of the enzyme molecule, known as the active site. The binding of the substrate is dictated by the shape of each molecule. Side chains on the enzyme interact with the substrate in a specific way, resulting in the making and breaking of bonds. The active site is the place on an enzyme where the substrate binds. An enzyme folds in such a way that it typically has one active site, usually a pocket or crevice formed by the folding pattern of the protein. Because the active site of an enzyme has such a unique shape, only one particular substrate is capable of binding to that enzyme. In other words, each enzyme catalyzes only one chemical reaction with only one substrate. Once the enzyme/substrate complex is formed, the reaction occurs and the substrate is transformed into products. Finally, the product molecule or molecules are released from the active site. Note that the enzyme is left unaffected by the reaction and is now capable of catalyzing the reaction of another substrate molecule.

    For many enzymes, the active site follows a lock and key (A in the figure below) model where the substrate fits exactly into the active site. The enzyme and substrate must be a perfect match so the enzyme only functions as a catalyst for one reaction. Other enzymes have an induced fit (B in the figure below) model. In an induced fit model, the active site can make minor adjustments to accommodate the substrate. This results in an enzyme that is capable of interacting with a small group of similar substrates. Look at the shape of the active site compared to the shape of the substrate in B of the figure below. The active site adjusts to accommodate the substrate.

    Figure 14.1.2: (A) Lock and key enzyme model and (B) induced fit enzyme model.

    Inhibitors

    An inhibitor is a molecule which interferes with the function of an enzyme, either by slowing or stopping the chemical reaction. Inhibitors can work in a variety of ways, but one of the most common is illustrated in the figure below.

    Diagram illustrating competitive inhibition
    Figure 14.1.3: A competitive inhibitor is a molecule that binds to the active site of an enzyme without reacting, thus preventing the substrate from binding.

    A competitive inhibitor binds competitively at the active site and blocks the substrate from binding. Since no reaction occurs with the inhibitor, the enzyme is prevented from catalyzing the reaction.

    A non-competitive inhibitor does not bind at the active site. It attaches at an allosteric site, which is some other site on the enzyme, and changes the shape of the protein. The allosteric site is any site on the enzyme that is not the active site. The attachment of the non-competitive inhibitor to the allosteric site results in a shift in three-dimensional structure that alters the shape of the active site so that the substrate will no longer fit in the active site properly (see figure below).

    Diagram illustrating non-competitive inhibition
    Figure 14.1.4: Non-competitive inhibition.

    Cofactors and Coenzymes

    Some enzymes require the presence of another substrate as a "helper" molecule in order to function properly. Cofactors and coenzymes serve in this role. Cofactors are inorganic species and coenzymes are small organic molecules. Many vitamins, such as B vitamins, are coenzymes. Some metal ions which function as cofactors for various enzymes include zinc, magnesium, potassium, and iron.

    Catalytic Activity of Enzymes

    Enzymes generally lower activation energy by reducing the energy needed for reactants to come together and react. One way that enzymes act is to bring reactants (substrates) together so they don't have to expend energy moving about until they collide at random. Enzymes bind both reactant molecules (substrates), tightly and specifically, at a site on the enzyme's active site. Enzymes can also bring molecules to the active site to break them apart. For example, sucrase is the enzyme for the breakdown of sucrose which enters the active site of the enzyme and helps weaken the interactions between the fructose and glucose that make up sucrose. Sucrase is specific to the breakdown of sucrose as are most enzymes. The active site is specific for the reactants of the biochemical reaction the enzyme catalyzes. Similar to puzzle pieces fitting together, the active site can only bind certain substrates. The activities of enzymes also depend on the temperature, concentration, and the pH of the surroudings.

    Concentration

    As with most reactions, the concentration of the reactant(s) affects the reaction rate. This is also true in enzyme concentration. When either substrate or enzyme concentration is low, the rate of the reaction will be slower than where there are higher concentrations. The two species must interact for a reaction to occur and higher concentrations of one or both will result in more effective interactions between the two.

    However, continuing to increase the substrate's concentration will not always increase the reaction rate. This is because at some point, all of the enzymes will be occupied and unavailable to bind with another substrate molecule until the substrate forms a product molecule and is released from the enzyme.

    pH

    Some enzymes work best at acidic pHs, while others work best in neutral environments. For example, digestive enzymes secreted in the acidic environment (low pH) of the stomach help break down proteins into smaller molecules. The main digestive enzyme in the stomach is pepsin, which works best at a pH of about 1.5. These enzymes would not work optimally at other pHs. Trypsin is another enzyme in the digestive system, which breaks protein chains in food into smaller particles. Trypsin works in the small intestine, which is not an acidic environment. Trypsin's optimum pH is about 8.

    Different reactions and different enzymes will achieve their maximum rate at certain pH values. As shown in the figure below, the enzyme achieves a maximum reaction rate at a pH of 4. Notice that the reaction will continue at lower and higher pH values because the enzyme will still function at other pH values but will not be as effective. At very high or very low pH values, denaturation will occur because an enzyme is just a protein with a specific function.

    Figure 14.1.5: Relationship between rate and pH.

    Temperature

    As with pH, reactions also have an ideal temperature where the enzyme functions most effectively. It will still function at higher and lower temperatures, but the rate will be less. For many biological reactions, the ideal temperature is at physiological conditions which is around \(37^\text{o} \text{C}\) which is normal body temperature. Many enzymes lose function at lower and higher temperatures. At higher temperatures, an enzyme's shape deteriorates. Only when the temperature comes back to normal does the enzyme regain its shape and normal activity unless the temperature was so high that it caused irreversible damage.

    Figure 14.1.6: Relationship between temperature and rate.

    Supplemental Resources

    Contributors

    • CK-12 Foundation by Sharon Bewick, Richard Parsons, Therese Forsythe, Shonna Robinson, and Jean Dupon.

    • Allison Soult, Ph.D. (Department of Chemistry, University of Kentucky)