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Chapter 10 Lecture

General, Organic, and Biological
Chemistry: An Integrated Approach
Laura Frost, Todd Deal and Karen Timberlake
by Richard Triplett

Chapter 10
Enzymes—Nature’s Chemists

Chapter Outline
10.1 Enzymes and Their Substrates
10.2 Thermodynamics of Chemical Reactions
10.3 Enzymes and Catalysis
10.4 Factors That Affect Enzyme Activity

© 2011 Pearson Education, Inc.

Chapter 10

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Introduction
• Enzymes are biologically active proteins that
accelerate the breakdown of food that is eaten.
• Enzymes are biological catalysts. They
accelerate reactions, but are not consumed or
changed in reactions.
• Discussions on the production or consumption of
energy, specifically heat, during chemical
reactions is called thermodynamics.
© 2011 Pearson Education, Inc.

Chapter 10

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10.1 Enzymes and Their Substrates
• Enzymes are large proteins with complex, threedimensional structures.
• Enzymes work in an aqueous environment in our
body so that the protein chain folds such that the
polar amino acids are on the surface.
• Consider hexokinase, an enzyme whose job is to
transfer a phosphate group from the high energy
molecule, adenosine triphosphate,
ATP, to D-glucose.
© 2011 Pearson Education, Inc.

Chapter 10

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10.1 Enzymes and Their Substrates, Continued

• In this equation, the enzyme name is written
above or below the reaction arrow.
• The phosphate group is represented by a P in a
circle.

© 2011 Pearson Education, Inc.

Chapter 10

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Continued The Active Site The folded structure for hexokinase is shown here. Inc. © 2011 Pearson Education.1 Enzymes and Their Substrates.10. Chapter 10 6 .

© 2011 Pearson Education. • The active site is the functional part of an enzyme where catalysis occurs. Inc. Chapter 10 7 .1 Enzymes and Their Substrates. hexokinase has an indentation on one side of the structure. and it is lined with amino acid side chains. • This indentation is known as the active site. Continued • When in its proper three-dimensional shape.10.

• Enzymes are specific for one enantiomer of the substrate. In an enzyme reaction. the reactant is called the substrate. © 2011 Pearson Education. the active site of hexokinase reacts with D-glucose. Continued • Glucose. the reactant for hexokinase. For example. but will not react with L-glucose. Chapter 10 8 . a property known as substrate specificity. fits snugly in the active site. Inc. • Enzymes have specific substrates.1 Enzymes and Their Substrates.10.

Chapter 10 9 . Continued © 2011 Pearson Education. Inc.1 Enzymes and Their Substrates.10.

Coenzymes are small organic molecules derived from vitamins.1 Enzymes and Their Substrates. Inc. Continued Some enzymes. Two categories of helpers are as follows: 1. like hexokinase. have nonprotein helpers. Cofactors are inorganic substances like magnesium ions. Riboflavin found in the coenzyme flavin adenine dinucleotide (FAD) is a coenzyme. © 2011 Pearson Education.10. Chapter 10 10 . 2.

© 2011 Pearson Education. Inc. • The initial interaction of the enzyme with the substrate is called the enzyme–substrate complex (ES). This complex forms prior to catalysis.1 Enzymes and Their Substrates. Continued Enzyme–Substrate Models • A substrate is drawn into the active site by intermolecular attractions like hydrogen bonding. • Hydrogen bonding orients the substrate properly within the active site. Chapter 10 11 .10.

the active site is thought to be a rigid.10. In the induced-fit model. and undergoes a conformational change. 2. © 2011 Pearson Education. the active site is flexible. inflexible shape that is an exact complement to the shape of the substrate. has a shape roughly complementary to the shape of its substrate. Continued There are two enzyme–substrate models: 1. adjusting to the shape of the substrate when the substrate interacts with the enzyme. Chapter 10 12 .1 Enzymes and Their Substrates. Inc. In the Lock-and-key model. The substrate fits in the active site much like a key fits in a lock.

1 Enzymes and Their Substrates. Chapter 10 13 .10. Continued © 2011 Pearson Education. Inc.

10. © 2011 Pearson Education. Chapter 10 14 . Continued A good example of an induced-fit model is when hexokinase and glucose form an enzyme– substrate complex as shown.1 Enzymes and Their Substrates. Inc.

10. some bonds are formed and some are broken. and some absorb energy as heat (endothermic reactions). and in the process. Chapter 10 15 . © 2011 Pearson Education. Inc. • A collision of reactant molecules must occur for a chemical reaction to occur. the amount of energy changes. • Some reactions release energy as heat (exothermic reactions).2 Thermodynamics of Chemical Reactions • As chemical reactions occur.

Inc. Continued • Energy is required to cause reactant molecules to collide. © 2011 Pearson Education.2 Thermodynamics of Chemical Reactions.10. • Reactant molecules must be aligned properly in order for a reaction to occur. Chapter 10 16 . • Activation energy is required to properly align reactant molecules and to cause them to collide to produce products.

Continued If the energy that is available is lower than the activation energy. Inc.10. © 2011 Pearson Education. the molecules will not collide with enough force to form products. Chapter 10 17 .2 Thermodynamics of Chemical Reactions.

10. Continued • The activation energy that must be overcome before products are formed is shown as: • The heat of reaction is the difference between the energy of reactants and the energy of products. Chapter 10 18 . © 2011 Pearson Education.2 Thermodynamics of Chemical Reactions. Inc.

10.2 Thermodynamics of Chemical Reactions. © 2011 Pearson Education. so heat is released. the energy of reactants is higher than the energy of products. • The height of the activation energy peak gives an indication of how fast the reaction proceeds. the energy of products is higher than the energy of reactants. Inc. Continued • In an exothermic reaction. Chapter 10 19 . • In an endothermic reaction. so heat is absorbed.

© 2011 Pearson Education. Continued • Reactions with a low activation energy will proceed at a faster rate than reactions with a high activation energy.2 Thermodynamics of Chemical Reactions. • A catalyst will not affect the energy of products or reactants. • Activation energy can be lowered with a catalyst.10. Inc. which will cause the reaction to proceed at a faster rate. Chapter 10 20 .

Chapter 10 21 . Inc. © 2011 Pearson Education.2 Thermodynamics of Chemical Reactions.10. Continued An enzyme-catalyzed reaction increases the rate of a reaction by forming ES before forming a product.

Inc.10. • Without catalase. • A high concentration of oxygen is produced at the wound site that kills germs. © 2011 Pearson Education. this reaction occurs very slowly. The area bubbles considerably because oxygen is produced by the enzyme catalase found in blood. Continued • Consider the addition of hydrogen peroxide to a cut. Chapter 10 22 .2 Thermodynamics of Chemical Reactions.

• ES is formed through the interactions between the enzyme and substrate. • These interactions combine to lower the activation energy of the reaction.3 Enzymes and Catalysis • Enzymes lower the activation energy by forming ES complex. Each interaction releases a small amount of energy to stabilize the complex. Chapter 10 23 . © 2011 Pearson Education.10. Inc. • Some interactions that help lower the activation energy are discussed in the next several slides .

• Amino acid side chains in the active site are used to facilitate the reaction. the active site is filled with substrate.3 Enzymes and Catalysis. Inc. • The reacting molecules are in close proximity to each other. • When ES forms.10. Continued Proximity • The active site of enzymes has a small volume. Chapter 10 24 . and the closer they are the more likely a reaction will occur. © 2011 Pearson Education.

3 Enzymes and Catalysis. • This lowers the activation energy needed for the reaction to occur. substrate molecules are held at the appropriate distance and in correct alignment to each other for the reaction to occur. Chapter 10 25 . © 2011 Pearson Education. Inc. • Amino acid side chains in the active site create interactions that orient the substrates.10. Continued Orientation • In the active site.

10.3 Enzymes and Catalysis. Chapter 10 26 . Inc. Continued Proper orientation is shown as: © 2011 Pearson Education.

the bonds of the substrate molecule are weakened (strained). Chapter 10 27 . • Strained bonds in the substrate means that the reaction will proceed more rapidly because the activation energy is lowered by this effect. Continued Bond Energy • When an enzyme interacts with substrate to form ES.10. © 2011 Pearson Education.3 Enzymes and Catalysis. Inc.

3 Enzymes and Catalysis. Chapter 10 28 . which stabilizes ES and lowers the activation energy. © 2011 Pearson Education. • Amino acid side chains in the active site form multiple hydrogen bonds with glucose. • Mg2+ (a coenzyme) holds ATP in one area of the active site and glucose interacts with another area. Continued • Consider the hexokinase reaction that catalyzes glucose to glucose-6-phosphate.10. Inc.

Inc. Continued • A conformational change in the enzyme occurs when glucose enters the active site.3 Enzymes and Catalysis. • ATP is in close proximity to the glucose and is in proper orientation for the reaction. so the lobes of the enzyme move apart and the products are released.10. • The enzyme is less attracted to the products. Chapter 10 29 . • Glucose-6-phosphate is formed along with ADP. © 2011 Pearson Education.

© 2011 Pearson Education. Chapter 10 30 .10.3 Enzymes and Catalysis. Inc. Continued This figure shows the formation of glucose-6-phosphate by hexokinase.

Chapter 10 31 . • Enzyme reactions are affected by reaction conditions such as substrate concentration. the flesh of sliced apples will turn brown by a process known as oxidation. © 2011 Pearson Education.4 Factors That Affect Enzyme Activity • If allowed to sit untouched. temperature. the vitamin C in the lemon juice will inhibit the formation of this brown color by changing the pH of the environment of the enzyme.10. Inc. • If lemon juice is sprinkled on the sliced apple. caused by an enzyme. and the presence of inhibitors. pH.

Inc. Chapter 10 32 . Continued Substrate Concentration • Recall that the first step in an enzyme-catalyzed reaction is the formation of ES.10. an increase in substrate concentration will cause an increase in the enzyme activity up to the point where the enzyme becomes saturated with substrate. © 2011 Pearson Education. • At a constant concentration of enzyme.4 Factors That Affect Enzyme Activity.

4 Factors That Affect Enzyme Activity.10. • A condition known as steady state is when an enzyme is operating under maximum activity. Inc. Chapter 10 33 . Continued • Increasing substrate concentration will not affect the rate of the reaction. © 2011 Pearson Education.

Continued pH • When the enzyme environment is changed by pH. the enzyme maintains its tertiary structure and its active site. © 2011 Pearson Education.10. its tertiary structure is disrupted. Chapter 10 34 . • At optimum pH. altering the active site and causing the enzyme’s activity to decrease. • Enzymes are most active at a pH known as their optimum pH. Inc.4 Factors That Affect Enzyme Activity.

4 Factors That Affect Enzyme Activity. Chapter 10 35 .10. • The optimum pH for enzymes is based on the location of the enzymes as shown: © 2011 Pearson Education. Continued • Changes in pH will also affect the nature of the amino acid side chains in the active site. Inc.

Continued Temperature • Enzymes have an optimum temperature at which they are most active. Inc.4 Factors That Affect Enzyme Activity.10. enzymes lose activity due to disruption of intermolecular forces stabilizing the tertiary structure. Chapter 10 36 . • Above optimum temperature. © 2011 Pearson Education. 37 oC. • The optimum temperature for most human enzymes is normal body temperature.

© 2011 Pearson Education. • Food is stored in a refrigerator or freezer to slow spoilage brought on by enzymes.10. enzymes denature. Inc. enzyme activity is low due to a lack of energy for the reaction to occur. Chapter 10 37 . • At low temperatures. which modifies the active site. Continued • At high temperatures. • Boiling contaminated water will destroy enzymes in bacteria that are present in the water.4 Factors That Affect Enzyme Activity.

© 2011 Pearson Education. Inc. Chapter 10 38 .4 Factors That Affect Enzyme Activity. • Enzyme inhibitors prevent the active site from interacting with substrate to form ES. • Some inhibitors cause temporary loss of activity. while others cause permanent loss of activity. Continued Inhibitors • Inhibitors are types of molecules that will cause enzymes to lose activity.10.

activity is regained if the inhibitor is removed. Inc. Continued • Reversible inhibition occurs when the inhibitor causes a temporary loss of activity. • Competitive inhibitors are molecules that compete with a substrate for the active site. and have a structure similar to the substrate. © 2011 Pearson Education. Chapter 10 39 . • Reversible inhibitors can be competitive or noncompetitive. However.4 Factors That Affect Enzyme Activity.10.

the enzyme cannot react with the substrate to form product. © 2011 Pearson Education. Inc.4 Factors That Affect Enzyme Activity. Chapter 10 40 .10. Continued As long as an inhibitor remains in the active site.

Continued • An example of a medical therapy that involves a competitive inhibitor involves liver alcohol dehydrogenase (LAD). the alcohol found in alcoholic beverages.10. and will compete with ethanol for the active site. which are found in antifreeze. a slow intravenous infusion of ethanol is administrated. • This enzyme will also react with ethylene glycol and methanol. Chapter 10 41 . © 2011 Pearson Education. This enzyme oxidizes ethanol. Inc. • If a pet is poisoned by drinking antifreeze.4 Factors That Affect Enzyme Activity.

• Noncompetitive inhibitors bind at a site on the enzyme that is usually remote to the active site. giving the kidneys time to eliminate these two substrates. • Noncompetitive inhibitors do not resemble the substrate. They do not compete for the enzyme’s active site.4 Factors That Affect Enzyme Activity. Chapter 10 42 . Inc.10. © 2011 Pearson Education. Continued • Administration of ethanol slows the production of the toxic metabolites of ethylene glycol and methanol.

Inc. Chapter 10 43 . © 2011 Pearson Education. • As long as this type of inhibitor is bound to the enzyme. This change in shape causes the active site to no longer interact with the substrate. it will no longer function effectively.4 Factors That Affect Enzyme Activity. it causes a conformational change in the enzyme. Continued • When a noncompetitive inhibitor binds to an enzyme.10.

10.4 Factors That Affect Enzyme Activity. Inc. © 2011 Pearson Education. Continued This figure diagrams how a noncompetitive inhibitor functions. Chapter 10 44 .

Chapter 10 45 . the more likely it will overcome the competition for the active site. © 2011 Pearson Education.4 Factors That Affect Enzyme Activity.10. Inc. • Inhibition by competitive inhibitors can be reversed by adding more substrate. The higher the concentration of substrate. Continued • Inhibitions caused by competitive and noncompetitive inhibitors can be reversed. • Adding more substrate with noncompetitive inhibitors has no effect on overcoming inhibition.

4 Factors That Affect Enzyme Activity. Inc. Chapter 10 46 . • Irreversible inhibition is a permanent inhibition. Continued • Reversing a noncompetitive inhibitor requires a special chemical reagent to remove the inhibitor and restore catalytic activity. • An irreversible inhibitor forms a covalent bond with an amino acid side chain in the enzyme’s active site. • Irreversible inhibition causes the substrate to be excluded from the active site. © 2011 Pearson Education.10.

• Heavy metals like silver. Inc.10. and lead are examples of irreversible inhibitors. Chapter 10 47 . © 2011 Pearson Education. mercury.4 Factors That Affect Enzyme Activity. Continued • Irreversible inhibition is demonstrated in this figure.

• Penicillin is an example of an irreversible inhibitor. © 2011 Pearson Education. Chapter 10 48 .10. and slows the growth of cell walls.4 Factors That Affect Enzyme Activity. Continued Antibiotics Inhibit Bacterial Enzymes • Enzyme inhibitors are used to fight bacterial infections. • Without a cell wall. bacteria cannot survive and the infection stops. Inc. It binds to the enzyme that bacteria use to synthesize cell walls.

1 Enzymes and Their Substrates • Enzymes are large. globular proteins that serve as biological catalysts. © 2011 Pearson Education. and they bind to the active site to form ES.Chapter Summary 10. Chapter 10 49 . Inc. • Substrates are the reactants for an enzyme reaction. • The functional part of an enzyme is the active site.

• Two theories. Continued • Enzymes are specific for one substrate that will bind to the active site and react. Continued 10. Inc. Chapter 10 50 .Chapter Summary. lock-and-key and induced-fit.1 Enzymes and Their Substrates. © 2011 Pearson Education. explain how an enzyme interacts with its substrate to form ES.

2 Thermodynamics of Chemical Reactions • Thermodynamics is a study of the energy changes that occur during a chemical reaction. and plays a role in the rate of reaction. Inc. • Heat of reaction is a measure of the production or consumption of energy in a reaction. • The lower the activation energy. © 2011 Pearson Education. • Activation energy is the energy required to start a reaction.Chapter Summary. Chapter 10 51 . Continued 10. the faster the rate of reaction.

Inc. Chapter 10 52 .2 Thermodynamics of Chemical Reactions. • Enzymes form ES before catalysis.Chapter Summary. • An endothermic reaction absorbs heat from its environment. Continued 10. which causes a lowering of the activation energy. Continued • An exothermic reaction releases heat to its environment. • Catalysts lower the activation energy causing an increase in the rate of reaction. © 2011 Pearson Education.

Inc. Chapter 10 53 . • In the active site.Chapter Summary. atoms are brought close together and aligned with amino acid side chains. Continued 10. © 2011 Pearson Education.3 Enzymes and Catalysis • Formation of the ES complex lowers the activation energy for a catalyzed reaction.

© 2011 Pearson Education.3 Enzymes and Catalysis.Chapter Summary. Inc. Continued • The active site also aligns the reactants with the optimal orientation for a reaction to occur. • The interaction of substrate with the active site weakens bonds between atoms in the substrate so the reaction can form products easier. Chapter 10 54 . Continued 10.

Inc. When substrate concentration is increased. temperature. © 2011 Pearson Education. Continued 10. • An increase in substrate concentration increases the rate of an enzyme-catalyzed reaction. the active site becomes saturated with substrate. substrate concentration. and the presence of inhibitors can affect the activity of an enzyme.Chapter Summary. Chapter 10 55 .4 Factors That Affect Enzyme Activity • Factors such as pH.

Chapter 10 56 . • Enzymes have an optimum pH and temperature at which they function best. Continued 10. Continued • When the active site is saturated. Inc. • Inhibitors decrease or eliminate an enzyme’s catalytic abilities. © 2011 Pearson Education.Chapter Summary. the enzyme is operating at steady state.4 Factors That Affect Enzyme Activity.

• Reversible inhibitors can be competitive inhibitors. Continued • The effect of inhibitors can be reversible or irreversible. • Reversible inhibitors can also be noncompetitive. Chapter 10 57 . Continued 10. which bind to a site on the enzyme other than the active site. Inc.Chapter Summary. © 2011 Pearson Education.4 Factors That Affect Enzyme Activity. and causes a conformational change in the enzyme. which compete with the substrate for the active site.