Nucleic Acids, Proteins, and Enzymes

Nucleic Acids, Proteins, and Enzymes
Chapter 3

Chapter 3 Nucleic Acids, Proteins, and Enzymes
Key Concepts 3.1 Nucleic Acids Are Informational Macromolecules 3.2 Proteins Are Polymers with Important Structural and Metabolic Roles 3.3 Some Proteins Act as Enzymes to Speed up Biochemical Reactions 3.4 Regulation of Metabolism Occurs by Regulation of Enzymes

Chapter 3 Opening Question
How does an understanding of proteins and enzymes help to explain how aspirin works?

Concept 3.1 Nucleic Acids Are Informational Macromolecules
Nucleic acids are polymers that store, transmit, and express hereditary (genetic) information. DNA = deoxyribonucleic acid RNA = ribonucleic acid The monomers are nucleotides.

Nucleotide: pentose sugar + N-containing base + phosphate group Nucleosides: pentose sugar + N-containing base

Bases: Pyrimidines—single rings Purines—double rings Sugars: DNA contains deoxyribose RNA contains ribose

Figure 3.1 Nucleotides Have Three Components
Figure 3.1 Nucleotides Have Three Components Nucleotide monomers are the building blocks of DNA and RNA polymers. Nucleotides may have one to three phosphate groups; those in DNA and RNA have one.

Nucleotides bond in condensation reactions to form phosphodiester bonds. The linkage is between the #5 carbon of one ribose and the #3 carbon of the next ribose. Nucleic acids grow in the 5′ to 3′ direction.

Figure 3.2 Linking Nucleotides Together
Figure 3.2 Linking Nucleotides Together Growth of a nucleic acid (RNA in this figure) from its monomers occurs in the 5ʹ (phosphate) to 3ʹ (hydroxyl) direction.

Oligonucleotides have up to 20 monomers. Example: small RNA molecules important for DNA replication and gene expression. DNA and RNA are polynucleotides, the longest polymers in the living world.

Table 3.1

Complementary base pairing:

Base pairs are linked by hydrogen bonds, favored by the arrangement of polar bonds in the bases. There are so many hydrogen bonds in DNA and RNA that they form a fairly strong attraction, but not as strong as covalent bonds. Thus, base pairs can be separated with only a small amount of energy.

In RNA, the base pairs are A–U and C–G. RNA is usually single-stranded, but may be folded into 3-D structures by hydrogen bonding. Folding occurs by complementary base pairing, so structure is determined by the order of bases.

Figure 3.3 RNA Figure 3.3 RNA (A) RNA is usually a single strand. (B) When a single-stranded RNA folds back on itself, hydrogen bonds between complementary sequences can stabilize it into a three-dimensional shape with distinct surface characteristics.

DNA is usually double stranded. Two polynucleotide strands form a “ladder” that twists into a double helix. Sugar-phosphate groups form the sides of the ladder, the hydrogen-bonded bases form the rungs.

Figure 3.4 DNA Figure 3.4 DNA (A) DNA usually consists of two strands running in opposite directions that are held together by base pairing between purines and pyrimidines opposite one another on the two strands. (B) The two antiparallel strands in a DNA molecule are twisted into a double helix.

The two strands are antiparallel (running in opposite directions), and the double helix is right-handed.

DNA’s information is encoded in the sequence of bases. DNA has two functions: Replication Information is copied to RNA and used to specify amino acid sequences in proteins.

DNA replication and transcription depend on base pairing: 5′-TCAGCA-3′ 3′-AGTCGT-5′ transcribes to RNA with the sequence 5′-UCAGCA-3′.

DNA replication: the entire molecule must be replicated completely so that each new cell receives a complete set of DNA. Genome—complete set of DNA in a living organism Genes—DNA sequences that encode specific proteins and are transcribed into RNA

Gene expression: transcription and translation of a specific gene. Not all genes are transcribed in all cells of an organism.

Figure 3.5 DNA Replication and Transcription
Figure 3.5 DNA Replication and Transcription DNA is completely replicated during cell reproduction (A), but it is only partially transcribed (B). In transcription, the DNA code is copied to RNA. The sequence of the latter determines the amino acid sequence of a protein. Transcription of the genes for many different proteins is activated at different times and, in multicellular organisms, in different cells of the body.

DNA base sequences reveal evolutionary relationships. Closely related living species should have more similar base sequences than species that are more distantly related. Scientists are now able to determine and compare entire genomes of organisms to study evolutionary relationships.

Concept 3.2 Proteins Are Polymers with Important Structural and Metabolic Roles
Major functions of proteins: Enzymes—catalytic molecules Defensive proteins (e.g., antibodies) Hormonal and regulatory proteins—control physiological processes Receptor proteins—receive and respond to molecular signals Storage proteins—store amino acids

Structural proteins—physical stability and movement Transport proteins—carry substances (e.g., hemoglobin) Genetic regulatory proteins—regulate when, how, and to what extent a gene is expressed

Protein monomers are amino acids. Amino and carboxyl functional groups allow them to act as both acid and base.

The R group (side chain) differs in each amino acid. Only 20 amino acids occur extensively in the proteins of all organisms. They are grouped according to properties conferred by the R groups.

Table 3.2 (Part 1)

Table 3.2 (Part 2)

Table 3.2 (Part 3)

The glycine side chain is a single hydrogen atom —small enough to fit into tight corners in the interior of a protein molecule. Proline has a ring structure that limits its hydrogen-bonding ability and its ability to rotate. It often functions to stabilize bends or loops in proteins.

Cysteine side chains can form covalent bonds called disulfide bridges.

Oligopeptides or peptides—short polymers of 20 or fewer amino acids (some hormones and signaling molecules) Polypeptides are larger polymers. Functional proteins are made up of one or more polypeptides. Proteins range in size from insulin, with 51 amino acids, to huge molecules such as the muscle protein titin, with 34,350 amino acids.

Amino acids are linked in condensation reactions to form peptide bonds. Polymerization takes place in the amino to carboxyl direction.

Figure 3.6 Formation of a Peptide Bond
Figure 3.6 Formation of a Peptide Bond In living things, the reaction leading to a peptide bond has many intermediate steps, but the reactants and products are the same as those shown in this simplified diagram.

Primary structure of a protein is the sequence of amino acids.

Figure 3.7 The Four Levels of Protein Structure (Part 1)
Figure 3.7 The Four Levels of Protein Structure The primary structure (A) of a protein determines what its secondary (B and C), tertiary (D), and quaternary (E) structures will be.

Secondary structure—regular, repeated spatial patterns in different regions, resulting from hydrogen bonding α (alpha) helix—right-handed coil β (beta) pleated sheet—two or more sequences are extended and aligned

Tertiary structure—polypeptide chain is bent and folded; results in the definitive 3-D shape

Interactions between R groups determine tertiary structure: Disulfide bridges hold folded polypeptides together Hydrogen bonds stabilize folds Hydrophobic side chains can aggregate in the protein interior van der Waals interactions between hydrophobic side chains

Figure 3.8 Noncovalent Interactions between Proteins and Other Molecules
Figure 3.8 Noncovalent Interactions between Proteins and Other Molecules Noncovalent interactions allow a protein (brown) to bind tightly to another protein (blue) with specific properties. Noncovalent interactions also allow regions within a single protein to interact with one another.

Ionic interactions form salt bridges. They can also be deep within a protein, away from water.

Figure 3.9 The Structure of a Protein
Figure 3.9 The Structure of a Protein Sucrase has a specific three-dimensional structure, determined by its primary structure. Sucrase plays a role in digestion in humans.

Secondary and tertiary protein structure derive from primary structure. Denaturing—heat or chemicals disrupt weaker interactions in a protein, destroying secondary and tertiary structure. The protein can return to normal when cooled or the chemicals are removed—all the information needed to specify the unique shape is contained in the primary structure.

Figure 3.10 Primary Structure Specifies Tertiary Structure (Part 1)
Figure Primary Structure Specifies Tertiary Structure Using the protein ribonuclease, Christian Anfinsen showed that proteins spontaneously fold into functionally correct three-dimensional configurations.a As long as the primary structure is not disrupted, the information for correct folding (under the right conditions) is retained. [a C. B. Anfinsen et al Proceedings of the National Academy of Sciences USA. 47: 1309–1314.]

Figure 3.10 Primary Structure Specifies Tertiary Structure (Part 2)
Figure Primary Structure Specifies Tertiary Structure Using the protein ribonuclease, Christian Anfinsen showed that proteins spontaneously fold into functionally correct three-dimensional configurations.a As long as the primary structure is not disrupted, the information for correct folding (under the right conditions) is retained. [a C. B. Anfinsen et al Proceedings of the National Academy of Sciences USA. 47: 1309–1314.]

Quaternary structure—two or more polypeptide chains (subunits) bind together by hydrophobic and ionic interactions, hydrogen bonds, and van der Waals forces.

Factors that can disrupt the interactions that determine protein structure (denaturing): Temperature Change in concentration of H+ High concentrations of polar substances Nonpolar substances

Proteins interact with other molecules. R groups on the surface may form weak interactions (e.g., hydrogen bonds) with groups on the surface of another molecule. This can change the tertiary structure and thus the shape of the protein. Protein structure can also be modified by covalent bonding of a chemical group to the side chain of one or more of its amino acids.

Figure 3.11 Protein Structure Can Change
Proteins can change Their tertiary structure When they bind to Other molecules or Are modified chemically. Figure Protein Structure Can Change Proteins can change their tertiary structure when they bind to other molecules (A) or are modified chemically (B).

Concept 3.3 Some Proteins Act as Enzymes to Speed up Biochemical Reactions
Living systems depend on reactions that occur spontaneously, but at very slow rates. Catalysts are substances that speed up the reactions without being permanently altered. No catalyst makes a reaction occur that cannot otherwise occur. Most biological catalysts are proteins (enzymes); a few are RNA molecules (ribozymes).

1. Enzymes speed up metabolic reactions by lowering energy barriers 2. Enzymes are substrate specific 3. The active site in an enzyme’s catalytic center 4. A cell’s physical and chemical environment affects enzyme activity

An exergonic reaction releases free energy (G), the amount of energy in a system that is available to do work. Without a catalyst, the reaction will be very slow because there is an energy barrier between reactants and products. An input of energy initiates the reaction (activation energy or Ea), which puts reactants into a transition state.

Figure 3.12 Activation Energy Initiates Reactions
Figure Activation Energy Initiates Reactions (A) In any chemical reaction, an initial stable state must become less stable before change is possible. (B) A ball on a hillside provides a physical analogy to the biochemical principle graphed in A. Although these graphs show an exergonic reaction, activation energy is needed for endergonic reactions as well.

Activation energy can come from heat—the molecules have more kinetic energy. This would not work in living systems because all reactions would be accelerated, including destructive ones.

Enzymes lower the activation energy by enabling reactants to come together and react more easily. Example: A molecule of sucrose in solution may hydrolyze in about 15 days; with sucrase present, the same reaction occurs in 1 second!

Figure 3.13 Enzymes Lower the Energy Barrier
Figure Enzymes Lower the Energy Barrier The activation energy (Ea) is lower in an enzyme-catalyzed reaction than in an uncatalyzed reaction, but the free energy released is the same with or without catalysis. A lower activation energy means the reaction will take place at a faster rate.

Enzymes are highly specific—each one catalyzes only one chemical reaction. Reactants are substrates: they bind to specific sites on the enzyme—the active sites. Specificity results from the exact 3-D shape and chemical properties of the active site.

Enzymes use a variety of mechanisms to lower activation energy and speed a reaction.
The active site orients substrates in the correct orientation for the reaction. As the active site binds the substrate, it may put stress on bonds that must be broken, making it easier to reach the transition state. R groups at the active site may create a conducive microenvironment for a specific reaction. Enzymes may even bind covalently to substrates in an intermediate step before returning to normal.

Figure Enzyme Action Figure Enzyme Action Sucrase catalyzes the hydrolysis of sucrose. After the reaction, the enzyme is unchanged and is ready to accept another substrate molecule.

The enzyme–substrate complex (ES) is held together by hydrogen bonding, electrical attraction, or temporary covalent bonding. The enzyme is not changed at the end of the reaction.

Enzymes use one or more mechanisms to catalyze a reaction: Inducing strain—bonds in the substrate are stretched, putting it in an unstable transition state.

Substrate orientation—substrates are brought together so that bonds can form. Adding chemical groups—R groups may be directly involved in the reaction.

Enzyme 3-D structures are so specific that they bind only one or a few related substrates. Many enzymes change shape when the substrate binds. The binding is like a baseball in a catcher’s mitt. The enzyme changes shape to make the binding tight—“induced fit.”

Factors that affect rate of reaction
The rate that a specific number of enzymes converts substrates to products depends in part on substrate concentrations. At low substrate concentrations, an increase in substrate speeds binding to available active sites. However, there is a limit to how fast a reaction can occur. At some substrate concentrations, the active sites on all enzymes are engaged, called enzyme saturation. The only way to increase productivity at this point is to add more enzyme molecules.

Homeostasis greatly affects enzymes’ efficacy
The three-dimensional structures of enzymes (almost all proteins) depend on environmental conditions. Changes in shape influence the reaction rate. Some conditions lead to the most active conformation and lead to optimal rate of reaction

Effect of Temperature on Enzymes
Temperature has a major impact on reaction rate. As temperature increases, collisions between substrates and active sites occur more frequently as molecules move faster. However, at some point thermal agitation begins to disrupt the weak bonds that stabilize the protein’s active conformation and the protein denatures. Each enzyme has an optimal temperature.

Temperatures affect rates

pH and enzyme function Because pH also influences shape and therefore reaction rate, each enzyme has an optimal pH too. This falls between pH for most enzymes. However, digestive enzymes in the stomach are designed to work best at pH 2 while those in the intestine are optimal at pH 8, both matching their working environments.

Difference in pH on function

Induced fit The active site of an enzymes is typically a pocket or groove on the surface of the protein into which the substrate fits. The specificity of an enzyme is due to the fit between the active site and that of the substrate. As the substrate binds, the enzyme changes shape leading to a tighter induced fit, bringing chemical groups in position to catalyze the reaction.

Induced fit of active site

Enzymes are efficient A single enzyme molecule can catalyze thousands or more reactions a second. Enzymes are unaffected by the reaction and are reusable. Most metabolic enzymes can catalyze a reaction in both the forward and reverse direction. The actual direction depends on the relative concentrations of products and reactants. Enzymes catalyze reactions in the direction of equilibrium.

Figure 3.15 Some Enzymes Change Shape When Substrate Binds to Them
Figure Some Enzymes Change Shape When Substrate Binds to Them Shape changes result in an induced fit between enzyme and substrate, improving the catalytic ability of the enzyme. Induced fit can be observed in the enzyme hexokinase, seen here with and without its substrates, glucose (green) and ATP (yellow).

Some enzymes require ions or other molecules (cofactors) in order to function: Metal ions Coenzymes add or remove chemical groups from the substrate. They can participate in reactions with many different enzymes. Prosthetic groups (nonamino acid groups) permanently bound to their enzymes.

Cofactors Many enzymes require nonprotein helpers, cofactors, for catalytic activity. They bind permanently to the enzyme or reversibly. Some inorganic cofactors include zinc, iron, and copper. Organic cofactors, coenzymes, include vitamins or molecules derived from vitamins. The manners by which cofactors assist catalysis are diverse.

Table 3.3

Rates of catalyzed reactions: There is usually less enzyme than substrate present, so reaction rate levels off when all enzyme molecules are bound to substrate molecules. The enzyme is said to be saturated.

Figure 3.16 Catalyzed Reactions Reach a Maximum Rate
Figure Catalyzed Reactions Reach a Maximum Rate Because there is usually less enzyme than substrate present, the reaction rate levels off when the enzyme becomes saturated.

Maximum reaction rate is used to calculate enzyme efficiency—molecules of substrate converted to product per unit time (turnover). Turnover ranges from 1 to 40 million molecules per second!

Concept 3.4 Regulation of Metabolism Occurs by Regulation of Enzymes
Enzyme-catalyzed reactions operate in metabolic pathways. The product of one reaction is a substrate for the next reaction. Each step is catalyzed by a specific enzyme. Cell have hundreds of enzymes that participate in interconnecting metabolic pathways, forming a metabolic system.

Figure 3.17 A Biochemical System
Figure A Biochemical System The complex interactions of metabolic pathways can be studied using the tools of systems biology. Enzymes are a major element controlling these pathways.

Metabolism Totality of an organism’s chemical processes
Emergent property from specific molecular interactions within the cell Management of cellular resources: material and energy

2 metabolic pathways Catabolic pathways: metabolic pathways which release energy by breaking down complex molecules to simpler cmpds (cell respiration) (CATABOLIC: CATACLISMIC) Anabolic pathways: these pathways CONSUME energy to build complicated molecules from simpler ones (photosynthesis)

Metabolic reactions are coupled
Most metabolic reactions are coupled so that the energy released from a catabolic reaction can be used to drive an anabolic one

Distinguish between open and closed systems
Closed system: collection of matter under study which is isolated from its surroundings Open system: system in which energy can be transferred between the system and its surroundings

1st and 2nd Laws of Thermodynamics
Thermodynamics: study of energy transformations 1st: energy can be transferred and transformed, but it cannot be created or destroyed (energy of the universe is constant) 2nd: every energy transfer of transformation makes the universe more disordered (every process increases the entropy of the universe) Entropy: quantitative measure of disorder that is proportional to randomness (designated by the letter S)

Why don’t living organisms violate the 2nd Law of thermodynamics?
The entropy of a system may decrease, but the entropy of the system plus its surroundings must always increase. If the system is open, highly ordered organisms don’t violate the 2nd law. They maintain highly ordered structure at the expense of increased entropy of their surroundings Take in complex high energy molecules such as food and extract chemical energy to create and maintain order Return to the surroundings simpler low energy molecules (CO2 and H2) and heat

Systems biology is a new field that describes the components of metabolic pathways mathematically. Computer algorithms are used to make predictions about what would happen if a component were altered.

Cells can regulate metabolism by controlling the amount of an enzyme. Cells often have the ability to turn synthesis of enzymes off or on. Activity of enzymes can also be regulated, which is often faster.

Regulating Enzyme Activity
As the chemical conditions in the cell shift, the pattern of allosteric regulation will shift as well. In many cases both inhibitors and activators are similar enough in shape that they compete for the same allosteric sites. Consequently, concentrations directly contribute to the direction of the reactions.

Chemical inhibitors can bind to enzymes and slow reaction rates. Natural inhibitors regulate metabolism. Artificial inhibitors are used to treat diseases, kill pests, and study enzyme function.

inhibitors and activators
These molecules may be products and substrates of a metabolic pathway. For example, some catabolic pathways have allosteric sites that are inhibited when ATP binds and activated when AMP binds. When ATP levels are low, AMP levels are high, and the pathway is turned on until ATP levels rise, AMP levels fall and inhibition by ATP dominates.

Irreversible inhibition: Inhibitor covalently binds to a side chain in the active site. The enzyme is permanently inactivated. Some insecticides act in this way.

Figure 3.18 Irreversible Inhibition
Figure Irreversible Inhibition DIPF forms a stable covalent bond with the amino acid serine at the active site of the enzyme acetylcholinesterase, thus irreversibly disabling the enzyme.

Reversible inhibition: A competitive inhibitor binds at the active site but no reaction occurs. It competes with the natural substrate. ANIMATED TUTORIAL 3.2 Enzyme Catalysis

Reversible inhibition: A noncompetitive inhibitor binds at a site distinct from the active site, causing change in enzyme shape and function. It prevents substrate binding or slows the reaction rate. ANIMATED TUTORIAL 3.2 Enzyme Catalysis 101

Figure 3.19 Reversible Inhibition
Figure Reversible Inhibition (A) A competitive inhibitor binds temporarily to the active site of an enzyme. (B) A noncompetitive inhibitor binds temporarily to the enzyme at a site away from the active site. In both cases, the enzyme’s function is disabled for only as long as the inhibitor remains bound.

Allosteric regulation—non-substrate molecule binds a site other than the active site (the allosteric site) The enzyme changes shape, which alters the chemical attraction (affinity) of the active site for the substrate. Allosteric regulation can activate or inactivate enzymes.

Allosteric sites can be modified by: Noncovalent binding (reversible) Covalent binding of a molecule or chemical group, such as phosphorylation (reversible) 104

Figure 3.20 Allosteric Regulation of Enzyme Activity
Figure Allosteric Regulation of Enzyme Activity (A) Noncovalent binding of a regulator (in this case an activator) can cause an enzyme to change shape and expose an active site. B) Enzymes can also be activated by covalent modification, in this case phosphorylation. Note that allosteric regulation can be negative as well, with the active site becoming hidden.

Inhibitors Binding by some molecules, inhibitors, prevent enzymes from catalyzing reactions. If binding involves covalent bonds, then inhibition is often irreversible. If binding is weak, inhibition may be reversible. If the inhibitor binds to the same site as the substrate, then it blocks substrate binding via competitive inhibition.

Competitive Inhibitor

Binding to allosteric site
If the inhibitor binds somewhere other than the active site, it blocks substrate binding via noncompetitive inhibition. Binding by the inhibitor causes the enzyme to change shape, rendering the active site unreceptive at worst or less effective at catalyzing the reaction. Reversible inhibition of enzymes is a natural part of the regulation of metabolism.

Noncompetitive Inhibitor

Phosphorylation by protein kinases is an important regulatory mechanism. Phosphorylation can change a hydrophobic region to hydrophilic. The enzyme twists and exposes the active site. Protein phosphatases reverse the process by removing phosphate groups.

Metabolic pathways: The first reaction is the commitment step—the other reactions then happen in sequence. Feedback inhibition (end-product inhibition)—the final product acts as an inhibitor of the first enzyme, which shuts down the pathway.

Figure 3.21 Feedback Inhibition of Metabolic Pathways
Figure Feedback Inhibition of Metabolic Pathways The first reaction in a metabolic pathway is referred to as the commitment step. Often the end product of the pathway can inhibit the enzyme that catalyzes the commitment step. The specific pathway shown here is the synthesis of isoleucine from threonine in bacteria. It is typical of many enzyme-catalyzed biosynthetic pathways.

pH affects protein structure and enzyme activity: Acidic side chains generate H+ and become anions. Basic side chains attract H+ and become cations.

Example: glutamic acid—COOH glutamic acid—COO– + H+ The law of mass action: the higher the H+ concentration, the more the reaction is driven to the left, to the less hydrophilic form. This can affect enzyme shape and function.

Protein tertiary structure (and thus function) is very sensitive to the concentration of H+ (pH) in the environment. All enzymes have an optimal pH for activity.

Temperature affects protein structure and enzyme activity: Warming increases rates of chemical reactions, but if temperature is too high, noncovalent bonds can break, inactivating enzymes. All enzymes have an optimal temperature for activity.

Figure 3.22 Enzyme Activity Is Affected by the Environment
Figure Enzyme Activity Is Affected by the Environment (A) The activity curve for each enzyme peaks at its optimal pH. For example, pepsin is active in the acidic environment of the stomach, whereas chymotrypsin is active in the neutral environment of the small intestine, and arginase is active in a basic environment. (B) Similarly, there is an optimal temperature for each enzyme. At higher temperatures the enzyme becomes denatured and inactive; this explains why the activity curve falls off abruptly at temperatures that are above optimal.

Isozymes catalyze the same reaction but have different composition and physical properties. Isozymes may have different optimal temperatures or pH, allowing an organism to adapt to changes in its environment.

One of the common methods of metabolic control is feedback inhibition in which a metabolic pathway is turned off by its end product. The end product acts as an inhibitor of an enzyme in the pathway. When the product is abundant the pathway is turned off, when rare the pathway is active. Feedback Inhibition

Cooperativity In enzymes with multiple catalytic subunits, binding by a substrate to one active site stabilizes favorable conformational changes at all other subunits, a process called cooperativity. This mechanism amplifies the response of enzymes to substrates, priming the enzyme to accept additional substrates

Stabilization of all subunits

The localization of enzymes within a cell helps order metabolism
Structures within the cell bring order to metabolic pathways. A team of enzymes for several steps of a metabolic pathway may be assembled together as a multienzyme complex. The product from the first can then pass quickly to the next enzyme until the final product is released

Enzyme location Some enzymes and enzyme complexes have fixed locations within the cells as structural components of particular membranes. Others are confined within membrane- enclosed eukaryotic organelles. Both methods concentrate enzymes for efficiency.

Enzymes embedded in membranes

Metabolism is emergent property
Metabolism is a concerted interplay of thousands of different kinds of molecules in the cell.

Answer to Opening Question
Aspirin binds to and inhibits the enzyme cyclooxygenase. Cyclooxygenase catalyzes the commitment step for metabolic pathways that produce: Prostaglandins—involved in inflammation and pain Thromboxanes—stimulate blood clotting and constriction of blood vessels

Figure 3.23 Aspirin: An Enzyme Inhibitor
Figure Aspirin: An Enzyme Inhibitor Aspirin inhibits a key enzyme in the metabolic pathways leading to inflammation and blood clotting.

Answer to Opening Question
Aspirin binds at the active site of cyclooxygenase and transfers an acetyl group to a serine residue. Serine becomes more hydrophobic, which changes the shape of the active site and makes it inaccessible to the substrate.

Nucleic Acids, Proteins, and Enzymes

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