{"product_id":"essential-biochemistry-isbn-9781119713203","title":"Essential Biochemistry","description":"\u003cp\u003e\u003ci\u003eEssential Biochemistry, 5th Edition\u003c\/i\u003e is comprised of biology, pre-med and allied health topics and presents a broad, but not overwhelming, base of biochemical coverage that focuses on the chemistry behind the biology. This revised edition relates the chemical concepts that scaffold the biology of biochemistry, providing practical knowledge as well as many problem-solving opportunities to hone skills. Key Concepts and Concept Review features help students to identify and review important takeaways in each section.\u003c\/p\u003e \u003cp\u003ePreface xiv\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 1 \u003c\/b\u003e\u003cb\u003eFoundations\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 \u003c\/b\u003e\u003cb\u003eThe Chemical Basis of Life 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e1.1 What Is Biochemistry? 1\u003c\/p\u003e \u003cp\u003e1.2 Biological Molecules 3\u003c\/p\u003e \u003cp\u003eCells contain four major types of biomolecules 3\u003c\/p\u003e \u003cp\u003eThere are three major kinds of biological polymers 6\u003c\/p\u003e \u003cp\u003eBox 1.A Units Used in Biochemistry 7\u003c\/p\u003e \u003cp\u003e1.3 Energy and Metabolism 10\u003c\/p\u003e \u003cp\u003eEnthalpy and entropy are components of free energy 11\u003c\/p\u003e \u003cp\u003eΔ\u003ci\u003eG \u003c\/i\u003eis less than zero for a spontaneous process 12\u003c\/p\u003e \u003cp\u003eLife is thermodynamically possible 12\u003c\/p\u003e \u003cp\u003e1.4 The Origin of Cells 14\u003c\/p\u003e \u003cp\u003ePrebiotic evolution led to cells 15\u003c\/p\u003e \u003cp\u003eBox 1.B How Does Evolution Work? 17\u003c\/p\u003e \u003cp\u003eEukaryotes are more complex than prokaryotes 17\u003c\/p\u003e \u003cp\u003eThe human body includes microorganisms 19\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 \u003c\/b\u003e\u003cb\u003eAqueous Chemistry 27\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e2.1 Water Molecules and Hydrogen Bonds 27\u003c\/p\u003e \u003cp\u003eHydrogen bonds are one type of electrostatic force 29\u003c\/p\u003e \u003cp\u003eWater dissolves many compounds 31\u003c\/p\u003e \u003cp\u003eBox 2.A Why Do Some Drugs Contain Fluorine? 31\u003c\/p\u003e \u003cp\u003e2.2 The Hydrophobic Effect 33\u003c\/p\u003e \u003cp\u003eAmphiphilic molecules experience both hydrophilic interactions and the hydrophobic effect 35\u003c\/p\u003e \u003cp\u003eThe hydrophobic core of a lipid bilayer is a barrier to diffusion 35\u003c\/p\u003e \u003cp\u003eBox 2.B Sweat, Exercise, and Sports Drinks 36\u003c\/p\u003e \u003cp\u003e2.3 Acid–Base Chemistry 37\u003c\/p\u003e \u003cp\u003e[H+] and [OH–] are inversely related 38\u003c\/p\u003e \u003cp\u003eThe pH of a solution can be altered 39\u003c\/p\u003e \u003cp\u003eBox 2.C Atmospheric CO2 and Ocean Acidification 39\u003c\/p\u003e \u003cp\u003eA p\u003ci\u003eK \u003c\/i\u003evalue describes an acid’s tendency to ionize 40\u003c\/p\u003e \u003cp\u003eThe pH of a solution of acid is related to the p\u003ci\u003eK \u003c\/i\u003e41\u003c\/p\u003e \u003cp\u003e2.4 Tools and Techniques: Buffers 44\u003c\/p\u003e \u003cp\u003e2.5 Clinical Connection: Acid–Base Balance in Humans 46\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 2 \u003c\/b\u003e\u003cb\u003eMolecular Structure and Function\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 \u003c\/b\u003e\u003cb\u003eNucleic Acid Structure and Function 57\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e3.1 Nucleotides 57\u003c\/p\u003e \u003cp\u003eNucleic acids are polymers of nucleotides 58\u003c\/p\u003e \u003cp\u003eSome nucleotides have other functions 60\u003c\/p\u003e \u003cp\u003e3.2 Nucleic Acid Structure 61\u003c\/p\u003e \u003cp\u003eDNA is a double helix 62\u003c\/p\u003e \u003cp\u003eRNA is single-stranded 64\u003c\/p\u003e \u003cp\u003eNucleic acids can be denatured and renatured 64\u003c\/p\u003e \u003cp\u003e3.3 The Central Dogma 67\u003c\/p\u003e \u003cp\u003eBox 3.A Replication, Mitosis, Meiosis, and Mendel’s Laws 67\u003c\/p\u003e \u003cp\u003eDNA must be decoded 70\u003c\/p\u003e \u003cp\u003eA mutated gene can cause disease 71\u003c\/p\u003e \u003cp\u003eGenes can be altered 72\u003c\/p\u003e \u003cp\u003eBox 3.B Genetically Modified Organisms 73\u003c\/p\u003e \u003cp\u003e3.4 Genomics 74\u003c\/p\u003e \u003cp\u003eThe exact number of human genes is not known 75\u003c\/p\u003e \u003cp\u003eGenome size varies 75\u003c\/p\u003e \u003cp\u003eGenomics has practical applications 77\u003c\/p\u003e \u003cp\u003eBox 3.C Viruses 78\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 \u003c\/b\u003e\u003cb\u003eProtein Structure 86\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e4.1 Amino Acids, the Building Blocks of Proteins 86\u003c\/p\u003e \u003cp\u003eThe 20 amino acids have different chemical properties 88\u003c\/p\u003e \u003cp\u003eBox 4.A Does Chirality Matter? 89\u003c\/p\u003e \u003cp\u003eBox 4.B Monosodium Glutamate 91\u003c\/p\u003e \u003cp\u003ePeptide bonds link amino acids in proteins 91\u003c\/p\u003e \u003cp\u003eThe amino acid sequence is the first level of protein structure 94\u003c\/p\u003e \u003cp\u003e4.2 Secondary Structure: The Conformation of the Peptide Group 95\u003c\/p\u003e \u003cp\u003eThe α helix exhibits a twisted backbone conformation 96\u003c\/p\u003e \u003cp\u003eThe β sheet contains multiple polypeptide strands 96\u003c\/p\u003e \u003cp\u003eProteins also contain irregular secondary structure 98\u003c\/p\u003e \u003cp\u003e4.3 Tertiary Structure and Protein Stability 99\u003c\/p\u003e \u003cp\u003eProteins can be described in different ways 99\u003c\/p\u003e \u003cp\u003eGlobular proteins have a hydrophobic core 100\u003c\/p\u003e \u003cp\u003eProtein structures are stabilized mainly by the hydrophobic effect 101\u003c\/p\u003e \u003cp\u003eBox 4.C Thioester Bonds as Spring-Loaded Traps 103\u003c\/p\u003e \u003cp\u003eProtein folding is a dynamic process 103\u003c\/p\u003e \u003cp\u003eBox 4.D Baking and Gluten Denaturation 104\u003c\/p\u003e \u003cp\u003eDisorder is a feature of many proteins 105\u003c\/p\u003e \u003cp\u003eProtein functions may depend on disordered regions 106\u003c\/p\u003e \u003cp\u003e4.4 Quaternary Structure 107\u003c\/p\u003e \u003cp\u003e4.5 Clinical Connection: Protein Misfolding and Disease 109\u003c\/p\u003e \u003cp\u003e4.6 Tools and Techniques: Analyzing Protein Structure 111\u003c\/p\u003e \u003cp\u003eChromatography takes advantage of a polypeptide’s unique properties 111\u003c\/p\u003e \u003cp\u003eMass spectrometry reveals amino acid sequences 114\u003c\/p\u003e \u003cp\u003eBox 4.E Mass Spectrometry Applications 116\u003c\/p\u003e \u003cp\u003eProtein structures are determined by NMR spectroscopy, X-ray crystallography, and cryo-electron microscopy 116\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 \u003c\/b\u003e\u003cb\u003eProtein Function 125\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e5.1 Myoglobin and Hemoglobin: Oxygen-Binding Proteins 126\u003c\/p\u003e \u003cp\u003eOxygen binding to myoglobin depends on the oxygen concentration 127\u003c\/p\u003e \u003cp\u003eMyoglobin and hemoglobin are related by evolution 128\u003c\/p\u003e \u003cp\u003eOxygen binds cooperatively to hemoglobin 129\u003c\/p\u003e \u003cp\u003eA conformational shift explains hemoglobin’s cooperative behavior 130\u003c\/p\u003e \u003cp\u003eBox 5.A Carbon Monoxide Poisoning 130\u003c\/p\u003e \u003cp\u003eH+ ions and bisphosphoglycerate regulate oxygen binding to hemoglobin \u003ci\u003ein vivo \u003c\/i\u003e132\u003c\/p\u003e \u003cp\u003e5.2 Clinical Connection: Hemoglobin Variants 134\u003c\/p\u003e \u003cp\u003e5.3 Structural Proteins 136\u003c\/p\u003e \u003cp\u003eActin filaments are most abundant 137\u003c\/p\u003e \u003cp\u003eActin filaments continuously extend and retract 138\u003c\/p\u003e \u003cp\u003eTubulin forms hollow microtubules 139\u003c\/p\u003e \u003cp\u003eKeratin is an intermediate filament 142\u003c\/p\u003e \u003cp\u003eCollagen is a triple helix 144\u003c\/p\u003e \u003cp\u003eBox 5.B Vitamin C Deficiency Causes Scurvy 144\u003c\/p\u003e \u003cp\u003eCollagen molecules are covalently cross-linked 145\u003c\/p\u003e \u003cp\u003eBox 5.C Bone and Collagen Defects 147\u003c\/p\u003e \u003cp\u003e5.4 Motor Proteins 148\u003c\/p\u003e \u003cp\u003eMyosin has two heads and a long tail 148\u003c\/p\u003e \u003cp\u003eMyosin operates through a lever mechanism 150\u003c\/p\u003e \u003cp\u003eKinesin is a microtubule-associated motor protein 151\u003c\/p\u003e \u003cp\u003eBox 5.D Myosin Mutations and Deafness 151\u003c\/p\u003e \u003cp\u003eKinesin is a processive motor 152\u003c\/p\u003e \u003cp\u003e5.5 Antibodies 154\u003c\/p\u003e \u003cp\u003eImmunoglobulin G includes two antigen-binding sites 154\u003c\/p\u003e \u003cp\u003e\u003cb\u003eB lymphocytes produce diverse antibodies 156\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eResearchers take advantage of antibodies’ affinity and specificity 157\u003c\/p\u003e \u003cp\u003e6 How Enzymes Work 167\u003c\/p\u003e \u003cp\u003e6.1 What Is an Enzyme? 167\u003c\/p\u003e \u003cp\u003eEnzymes are usually named after the reaction they catalyze 170\u003c\/p\u003e \u003cp\u003e6.2 Chemical Catalytic Mechanisms 171\u003c\/p\u003e \u003cp\u003eA catalyst provides a reaction pathway with a lower activation energy barrier 173\u003c\/p\u003e \u003cp\u003eEnzymes use chemical catalytic mechanisms 173\u003c\/p\u003e \u003cp\u003eBox 6.A Depicting Reaction Mechanisms 175\u003c\/p\u003e \u003cp\u003eThe catalytic triad of chymotrypsin promotes peptide bond hydrolysis 177\u003c\/p\u003e \u003cp\u003e6.3 Unique Properties of Enzyme Catalysts 180\u003c\/p\u003e \u003cp\u003eEnzymes stabilize the transition state 180\u003c\/p\u003e \u003cp\u003eEfficient catalysis depends on proximity and orientation effects 181\u003c\/p\u003e \u003cp\u003eThe active-site microenvironment promotes catalysis 182\u003c\/p\u003e \u003cp\u003e6.4 Chymotrypsin in Context 183\u003c\/p\u003e \u003cp\u003eNot all serine proteases are related by evolution 183\u003c\/p\u003e \u003cp\u003eEnzymes with similar mechanisms exhibit different substrate specificity 184\u003c\/p\u003e \u003cp\u003eChymotrypsin is activated by proteolysis 185\u003c\/p\u003e \u003cp\u003eProtease inhibitors limit protease activity 186\u003c\/p\u003e \u003cp\u003e6.5 Clinical Connection: Blood Coagulation 187\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 \u003c\/b\u003e\u003cb\u003eEnzyme Kinetics and Inhibition 198\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction to Enzyme Kinetics 198\u003c\/p\u003e \u003cp\u003e7.2 Derivation and Meaning of the Michaelis–Menten Equation 201\u003c\/p\u003e \u003cp\u003eRate equations describe chemical processes 201\u003c\/p\u003e \u003cp\u003eThe Michaelis–Menten equation is a rate equation for an enzyme-catalyzed reaction 202\u003c\/p\u003e \u003cp\u003e\u003ci\u003eK\u003c\/i\u003eM is the substrate concentration at which velocity is half-maximal 204\u003c\/p\u003e \u003cp\u003eThe catalytic constant describes how quickly an enzyme can act 204\u003c\/p\u003e \u003cp\u003e\u003ci\u003ek\u003c\/i\u003ecat\/\u003ci\u003eK\u003c\/i\u003eM indicates catalytic efficiency 205\u003c\/p\u003e \u003cp\u003e\u003ci\u003eK\u003c\/i\u003eM and \u003ci\u003eV\u003c\/i\u003emax are experimentally determined 205\u003c\/p\u003e \u003cp\u003eNot all enzymes fit the simple Michaelis–Menten model 207\u003c\/p\u003e \u003cp\u003e7.3 Enzyme Inhibition 209\u003c\/p\u003e \u003cp\u003eSome inhibitors act irreversibly 209\u003c\/p\u003e \u003cp\u003eCompetitive inhibition is the most common form of reversible enzyme inhibition 210\u003c\/p\u003e \u003cp\u003eTransition state analogs inhibit enzymes 212\u003c\/p\u003e \u003cp\u003eOther types of inhibitors affect \u003ci\u003eV\u003c\/i\u003emax 213\u003c\/p\u003e \u003cp\u003eBox 7.A Inhibitors of HIV Protease 214\u003c\/p\u003e \u003cp\u003eAllosteric enzyme regulation includes inhibition and activation 216\u003c\/p\u003e \u003cp\u003eSeveral factors may influence enzyme activity 219\u003c\/p\u003e \u003cp\u003e7.4 Clinical Connection: Drug Development 219\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 \u003c\/b\u003e\u003cb\u003eLipids and Membranes 234\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e8.1 Lipids 234\u003c\/p\u003e \u003cp\u003eFatty acids contain long hydrocarbon chains 235\u003c\/p\u003e \u003cp\u003eBox 8.A Omega-3 Fatty Acids 236\u003c\/p\u003e \u003cp\u003eSome lipids contain polar head groups 237\u003c\/p\u003e \u003cp\u003eLipids perform a variety of physiological functions 239\u003c\/p\u003e \u003cp\u003eBox 8.B The Lipid Vitamins A, D, E, and K 240\u003c\/p\u003e \u003cp\u003e8.2 The Lipid Bilayer 241\u003c\/p\u003e \u003cp\u003eThe bilayer is a fluid structure 242\u003c\/p\u003e \u003cp\u003eNatural bilayers are asymmetric 243\u003c\/p\u003e \u003cp\u003e8.3 Membrane Proteins 244\u003c\/p\u003e \u003cp\u003eIntegral membrane proteins span the bilayer 245\u003c\/p\u003e \u003cp\u003eAn α helix can cross the bilayer 245\u003c\/p\u003e \u003cp\u003eA transmembrane β sheet forms a barrel 246\u003c\/p\u003e \u003cp\u003eLipid-linked proteins are anchored in the membrane 246\u003c\/p\u003e \u003cp\u003e8.4 The Fluid Mosaic Model 248\u003c\/p\u003e \u003cp\u003eMembrane proteins have a fixed orientation 249\u003c\/p\u003e \u003cp\u003eLipid asymmetry is maintained by enzymes 250\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 \u003c\/b\u003e\u003cb\u003eMembrane Transport 258\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e9.1 The Thermodynamics of Membrane Transport 258\u003c\/p\u003e \u003cp\u003eIon movements alter membrane potential 259\u003c\/p\u003e \u003cp\u003eMembrane proteins mediate transmembrane ion movement 260\u003c\/p\u003e \u003cp\u003e9.2 Passive Transport 263\u003c\/p\u003e \u003cp\u003ePorins are β barrel proteins 263\u003c\/p\u003e \u003cp\u003eIon channels are highly selective 264\u003c\/p\u003e \u003cp\u003eGated channels undergo conformational changes 265\u003c\/p\u003e \u003cp\u003eBox 9.A Pores Can Kill 265\u003c\/p\u003e \u003cp\u003eAquaporins are water-specific pores 266\u003c\/p\u003e \u003cp\u003eSome transport proteins alternate between conformations 268\u003c\/p\u003e \u003cp\u003e9.3 Active Transport 269\u003c\/p\u003e \u003cp\u003eThe Na,K-ATPase changes conformation as it pumps ions across the membrane 269\u003c\/p\u003e \u003cp\u003eABC transporters mediate drug resistance 271\u003c\/p\u003e \u003cp\u003eSecondary active transport exploits existing gradients 271\u003c\/p\u003e \u003cp\u003e9.4 Membrane Fusion 272\u003c\/p\u003e \u003cp\u003eSNAREs link vesicle and plasma membranes 273\u003c\/p\u003e \u003cp\u003eBox 9.B Antidepressants Block Serotonin Transport 275\u003c\/p\u003e \u003cp\u003eEndocytosis is the reverse of exocytosis 276\u003c\/p\u003e \u003cp\u003eAutophagosomes enclose cell materials for degradation 277\u003c\/p\u003e \u003cp\u003eBox 9.C Exosomes 278\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 \u003c\/b\u003e\u003cb\u003eSignaling 287\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e10.1 General Features of Signaling Pathways 287\u003c\/p\u003e \u003cp\u003eA ligand binds to a receptor with a characteristic affinity 288\u003c\/p\u003e \u003cp\u003eMost signaling occurs through two types of receptors 289\u003c\/p\u003e \u003cp\u003eThe effects of signaling are limited 290\u003c\/p\u003e \u003cp\u003e10.2 G Protein Signaling Pathways 291\u003c\/p\u003e \u003cp\u003eG protein–coupled receptors include seven transmembrane helices 292\u003c\/p\u003e \u003cp\u003eThe receptor activates a G protein 293\u003c\/p\u003e \u003cp\u003eThe second messenger cyclic AMP activates protein kinase A 294\u003c\/p\u003e \u003cp\u003eArrestin competes with G proteins 296\u003c\/p\u003e \u003cp\u003eSignaling pathways must be switched off 296\u003c\/p\u003e \u003cp\u003eThe phosphoinositide signaling pathway generates two second messengers 297\u003c\/p\u003e \u003cp\u003eMany sensory receptors are GPCRs 298\u003c\/p\u003e \u003cp\u003eBox 10.A Opioids 299\u003c\/p\u003e \u003cp\u003e10.3 Receptor Tyrosine Kinases 300\u003c\/p\u003e \u003cp\u003eThe insulin receptor dimer changes conformation 300\u003c\/p\u003e \u003cp\u003eThe receptor undergoes autophosphorylation 302\u003c\/p\u003e \u003cp\u003eBox 10.B Cell Signaling and Cancer 303\u003c\/p\u003e \u003cp\u003e10.4 Lipid Hormone Signaling 303\u003c\/p\u003e \u003cp\u003eEicosanoids are short-range signals 305\u003c\/p\u003e \u003cp\u003eBox 10.C Inhibitors of Cyclooxygenase 306\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 \u003c\/b\u003e\u003cb\u003eCarbohydrates 315\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e11.1 Monosaccharides 315\u003c\/p\u003e \u003cp\u003eMost carbohydrates are chiral compounds 316\u003c\/p\u003e \u003cp\u003eCyclization generates α and β anomers 317\u003c\/p\u003e \u003cp\u003eMonosaccharides can be derivatized in many different ways 318\u003c\/p\u003e \u003cp\u003eBox 11.A The Maillard Reaction 319\u003c\/p\u003e \u003cp\u003e11.2 Polysaccharides 320\u003c\/p\u003e \u003cp\u003eLactose and sucrose are the most common disaccharides 321\u003c\/p\u003e \u003cp\u003eStarch and glycogen are fuel-storage molecules 321\u003c\/p\u003e \u003cp\u003eCellulose and chitin provide structural support 322\u003c\/p\u003e \u003cp\u003eBox 11.B Cellulosic Biofuel 323\u003c\/p\u003e \u003cp\u003eBacterial polysaccharides form a biofilm 324\u003c\/p\u003e \u003cp\u003e11.3 Glycoproteins 325\u003c\/p\u003e \u003cp\u003eOligosaccharides are \u003ci\u003eN\u003c\/i\u003e-linked or \u003ci\u003eO\u003c\/i\u003e-linked 325\u003c\/p\u003e \u003cp\u003eOligosaccharide groups are biological markers 326\u003c\/p\u003e \u003cp\u003eBox 11.C The ABO Blood Group System 327\u003c\/p\u003e \u003cp\u003eProteoglycans contain long glycosaminoglycan chains 327\u003c\/p\u003e \u003cp\u003eBacterial cell walls are made of peptidoglycan 328\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 3 \u003c\/b\u003e\u003cb\u003eMetabolism\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 \u003c\/b\u003e\u003cb\u003eMetabolism and Bioenergetics 337\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e12.1 Food and Fuel 337\u003c\/p\u003e \u003cp\u003eCells take up the products of digestion 338\u003c\/p\u003e \u003cp\u003eMonomers are stored as polymers 339\u003c\/p\u003e \u003cp\u003eFuels are mobilized as needed 340\u003c\/p\u003e \u003cp\u003e12.2 Metabolic Pathways 343\u003c\/p\u003e \u003cp\u003eSome major metabolic pathways share a few common intermediates 343\u003c\/p\u003e \u003cp\u003eMany metabolic pathways include oxidation–reduction reactions 344\u003c\/p\u003e \u003cp\u003eMetabolic pathways are complex 346\u003c\/p\u003e \u003cp\u003eHuman metabolism depends on vitamins 347\u003c\/p\u003e \u003cp\u003eBox 12.A The Transcriptome, the Proteome, and the Metabolome 348\u003c\/p\u003e \u003cp\u003eBox 12.B Iron Metabolism 351\u003c\/p\u003e \u003cp\u003e12.3 Free Energy Changes in Metabolic Reactions 352\u003c\/p\u003e \u003cp\u003eThe free energy change depends on reactant concentrations 352\u003c\/p\u003e \u003cp\u003eUnfavorable reactions are coupled to favourable reactions 354\u003c\/p\u003e \u003cp\u003eEnergy can take different forms 356\u003c\/p\u003e \u003cp\u003eRegulation occurs at the steps with the largest free energy changes 357\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 \u003c\/b\u003e\u003cb\u003eGlucose Metabolism 366\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e13.1 Glycolysis 366\u003c\/p\u003e \u003cp\u003eEnergy is invested at the start of glycolysis 367\u003c\/p\u003e \u003cp\u003eATP is generated near the end of glycolysis 373\u003c\/p\u003e \u003cp\u003eBox 13.A Catabolism of Other Sugars 378\u003c\/p\u003e \u003cp\u003eSome cells convert pyruvate to lactate or ethanol 379\u003c\/p\u003e \u003cp\u003eBox 13.B Alcohol Metabolism 380\u003c\/p\u003e \u003cp\u003ePyruvate is the precursor of other molecules 381\u003c\/p\u003e \u003cp\u003e13.2 Gluconeogenesis 383\u003c\/p\u003e \u003cp\u003eFour gluconeogenic enzymes plus some glycolytic enzymes convert pyruvate to glucose 383\u003c\/p\u003e \u003cp\u003eGluconeogenesis is regulated at the fructose bisphosphatase step 385\u003c\/p\u003e \u003cp\u003e13.3 Glycogen Synthesis and Degradation 386\u003c\/p\u003e \u003cp\u003eGlycogen synthesis consumes the energy of UTP 386\u003c\/p\u003e \u003cp\u003eGlycogen phosphorylase catalyzes glycogenolysis 388\u003c\/p\u003e \u003cp\u003e13.4 The Pentose Phosphate Pathway 389\u003c\/p\u003e \u003cp\u003eThe oxidative reactions of the pentose phosphate pathway produce NADPH 389\u003c\/p\u003e \u003cp\u003eIsomerization and interconversion reactions generate a variety of monosaccharides 390\u003c\/p\u003e \u003cp\u003eA summary of glucose metabolism 392\u003c\/p\u003e \u003cp\u003e13.5 Clinical Connection: Disorders of Carbohydrate Metabolism 393\u003c\/p\u003e \u003cp\u003eGlycogen storage diseases affect liver and muscle 394\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 \u003c\/b\u003e\u003cb\u003eThe Citric Acid Cycle 403\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e14.1 The Pyruvate Dehydrogenase Reaction 403\u003c\/p\u003e \u003cp\u003eThe pyruvate dehydrogenase complex contains multiple copies of three different enzymes 404\u003c\/p\u003e \u003cp\u003ePyruvate dehydrogenase converts pyruvate to acetyl-CoA 404\u003c\/p\u003e \u003cp\u003e14.2 The Eight Reactions of the Citric Acid Cycle 406\u003c\/p\u003e \u003cp\u003e1. Citrate synthase adds an acetyl group to oxaloacetate 407\u003c\/p\u003e \u003cp\u003e2. Aconitase isomerizes citrate to isocitrate 409\u003c\/p\u003e \u003cp\u003e3. Isocitrate dehydrogenase releases the first CO2 410\u003c\/p\u003e \u003cp\u003e4. α-Ketoglutarate dehydrogenase releases the second CO2 410\u003c\/p\u003e \u003cp\u003e5. Succinyl-CoA synthetase catalyzes substrate-level phosphorylation 411\u003c\/p\u003e \u003cp\u003e6. Succinate dehydrogenase generates ubiquinol 412\u003c\/p\u003e \u003cp\u003e7. Fumarase catalyzes a hydration reaction 412\u003c\/p\u003e \u003cp\u003e8. Malate dehydrogenase regenerates oxaloacetate 412\u003c\/p\u003e \u003cp\u003e14.3 Thermodynamics of the Citric Acid Cycle 413\u003c\/p\u003e \u003cp\u003eThe citric acid cycle is an energy-generating catalytic cycle 413\u003c\/p\u003e \u003cp\u003eThe citric acid cycle is regulated at three steps 414\u003c\/p\u003e \u003cp\u003eBox 14.A Mutations in Citric Acid Cycle Enzymes 415\u003c\/p\u003e \u003cp\u003eThe citric acid cycle probably evolved as a synthetic pathway 415\u003c\/p\u003e \u003cp\u003e14.4 Anabolic and Catabolic Functions of the Citric Acid Cycle 416\u003c\/p\u003e \u003cp\u003eCitric acid cycle intermediates are precursors of other molecules 416\u003c\/p\u003e \u003cp\u003eAnaplerotic reactions replenish citric acid cycle intermediates 418\u003c\/p\u003e \u003cp\u003eBox 14.B The Glyoxylate Pathway 419\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 \u003c\/b\u003e\u003cb\u003eOxidative Phosphorylation 428\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e15.1 The Thermodynamics of Oxidation–Reduction Reactions 428\u003c\/p\u003e \u003cp\u003eReduction potential indicates a substance’s tendency to accept electrons 429\u003c\/p\u003e \u003cp\u003eThe free energy change can be calculated from the change in reduction potential 431\u003c\/p\u003e \u003cp\u003e15.2 Mitochondrial Electron Transport 432\u003c\/p\u003e \u003cp\u003eMitochondrial membranes define two compartments 433\u003c\/p\u003e \u003cp\u003eComplex I transfers electrons from NADH to ubiquinone 434\u003c\/p\u003e \u003cp\u003eOther oxidation reactions contribute to the ubiquinol pool 436\u003c\/p\u003e \u003cp\u003eComplex III transfers electrons from ubiquinol to cytochrome \u003ci\u003ec \u003c\/i\u003e437\u003c\/p\u003e \u003cp\u003eComplex IV oxidizes cytochrome \u003ci\u003ec \u003c\/i\u003eand reduces O2 439\u003c\/p\u003e \u003cp\u003eRespiratory complexes associate with each other 441\u003c\/p\u003e \u003cp\u003eBox 15.A Reactive Oxygen Species 442\u003c\/p\u003e \u003cp\u003e15.3 Chemiosmosis 443\u003c\/p\u003e \u003cp\u003eChemiosmosis links electron transport and oxidative phosphorylation 443\u003c\/p\u003e \u003cp\u003eThe proton gradient is an electrochemical gradient 443\u003c\/p\u003e \u003cp\u003e15.4 ATP Synthase 445\u003c\/p\u003e \u003cp\u003eProton translocation rotates the \u003ci\u003ec \u003c\/i\u003ering of ATP synthase 445\u003c\/p\u003e \u003cp\u003eThe binding change mechanism explains how ATP is made 447\u003c\/p\u003e \u003cp\u003eThe P:O ratio describes the stoichiometry of oxidative phosphorylation 447\u003c\/p\u003e \u003cp\u003eBox 15.B Uncoupling Agents Prevent ATP Synthesis 448\u003c\/p\u003e \u003cp\u003eThe rate of oxidative phosphorylation reflects the need for ATP 448\u003c\/p\u003e \u003cp\u003eBox 15.C Powering Human Muscles 449\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 \u003c\/b\u003e\u003cb\u003ePhotosynthesis 458\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e16.1 Chloroplasts and Solar Energy 458\u003c\/p\u003e \u003cp\u003ePigments absorb light of different wavelengths 459\u003c\/p\u003e \u003cp\u003eLight-harvesting complexes transfer energy to the reaction center 461\u003c\/p\u003e \u003cp\u003e16.2 The Light Reactions 463\u003c\/p\u003e \u003cp\u003ePhotosystem II is a light-activated oxidation–reduction enzyme 463\u003c\/p\u003e \u003cp\u003eThe oxygen-evolving complex of Photosystem II oxidizes water 464\u003c\/p\u003e \u003cp\u003eCytochrome \u003ci\u003eb\u003c\/i\u003e6\u003ci\u003ef \u003c\/i\u003elinks Photosystems I and II 466\u003c\/p\u003e \u003cp\u003eA second photooxidation occurs at Photosystem I 467\u003c\/p\u003e \u003cp\u003eChemiosmosis provides the free energy for ATP synthesis 469\u003c\/p\u003e \u003cp\u003e16.3 Carbon Fixation 471\u003c\/p\u003e \u003cp\u003eRubisco catalyzes CO2 fixation 471\u003c\/p\u003e \u003cp\u003eThe Calvin cycle rearranges sugar molecules 472\u003c\/p\u003e \u003cp\u003eBox 16.A The C4 Pathway 473\u003c\/p\u003e \u003cp\u003eThe availability of light regulates carbon fixation 475\u003c\/p\u003e \u003cp\u003eCalvin cycle products are used to synthesize sucrose and starch 476\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 \u003c\/b\u003e\u003cb\u003eLipid Metabolism 483\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e17.1 Lipid Transport 483\u003c\/p\u003e \u003cp\u003e17.2 Fatty Acid Oxidation 486\u003c\/p\u003e \u003cp\u003eFatty acids are activated before they are degraded 487\u003c\/p\u003e \u003cp\u003eEach round of β oxidation has four reactions 488\u003c\/p\u003e \u003cp\u003eDegradation of unsaturated fatty acids requires isomerization and reduction 491\u003c\/p\u003e \u003cp\u003eOxidation of odd-chain fatty acids yields propionyl-CoA 492\u003c\/p\u003e \u003cp\u003eSome fatty acid oxidation occurs in peroxisomes 494\u003c\/p\u003e \u003cp\u003e17.3 Fatty Acid Synthesis 495\u003c\/p\u003e \u003cp\u003eAcetyl-CoA carboxylase catalyzes the first step of fatty acid synthesis 496\u003c\/p\u003e \u003cp\u003eFatty acid synthase catalyzes seven reactions 497\u003c\/p\u003e \u003cp\u003eOther enzymes elongate and desaturate newly synthesized fatty acids 500\u003c\/p\u003e \u003cp\u003eBox 17.A Fats, Diet, and Heart Disease 500\u003c\/p\u003e \u003cp\u003eFatty acid synthesis can be activated and inhibited 501\u003c\/p\u003e \u003cp\u003eBox 17.B Inhibitors of Fatty Acid Synthesis 502\u003c\/p\u003e \u003cp\u003eAcetyl-CoA can be converted to ketone bodies 503\u003c\/p\u003e \u003cp\u003e17.4 Synthesis of Other Lipids 505\u003c\/p\u003e \u003cp\u003eTriacylglycerols and phospholipids are built from acyl-CoA groups 505\u003c\/p\u003e \u003cp\u003eCholesterol synthesis begins with acetyl-CoA 508\u003c\/p\u003e \u003cp\u003eA summary of lipid metabolism 510\u003c\/p\u003e \u003cp\u003e\u003cb\u003e18 \u003c\/b\u003e\u003cb\u003eNitrogen Metabolism 518\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e18.1 Nitrogen Fixation and Assimilation 518\u003c\/p\u003e \u003cp\u003eNitrogenase converts N2to NH3 519\u003c\/p\u003e \u003cp\u003eAmmonia is assimilated by glutamine synthetase and glutamate synthase 519\u003c\/p\u003e \u003cp\u003eTransamination moves amino groups between compounds 521\u003c\/p\u003e \u003cp\u003eBox 18.A Transaminases in the Clinic 523\u003c\/p\u003e \u003cp\u003e18.2 Amino Acid Biosynthesis 523\u003c\/p\u003e \u003cp\u003eSeveral amino acids are easily synthesized from common metabolites 524\u003c\/p\u003e \u003cp\u003eAmino acids with sulfur, branched chains, or aromatic groups are more difficult to synthesize 526\u003c\/p\u003e \u003cp\u003eBox 18.B Homocysteine, Methionine, and One-Carbon Chemistry 527\u003c\/p\u003e \u003cp\u003eBox 18.C Glyphosate, the Most Popular Herbicide 528\u003c\/p\u003e \u003cp\u003eAmino acids are the precursors of some signaling molecules 530\u003c\/p\u003e \u003cp\u003eBox 18.D Nitric Oxide 531\u003c\/p\u003e \u003cp\u003e18.3 Amino Acid Catabolism 532\u003c\/p\u003e \u003cp\u003eAmino acids are glucogenic, ketogenic, or both 532\u003c\/p\u003e \u003cp\u003eBox 18.E Diseases of Amino Acid Metabolism 535\u003c\/p\u003e \u003cp\u003e18.4 Nitrogen Disposal: The Urea Cycle 536\u003c\/p\u003e \u003cp\u003eGlutamate supplies nitrogen to the urea cycle 537\u003c\/p\u003e \u003cp\u003eThe urea cycle consists of four reactions 538\u003c\/p\u003e \u003cp\u003e18.5 Nucleotide Metabolism 540\u003c\/p\u003e \u003cp\u003ePurine nucleotide synthesis yields IMP and then AMP and GMP 541\u003c\/p\u003e \u003cp\u003ePyrimidine nucleotide synthesis yields UTP and CTP 542\u003c\/p\u003e \u003cp\u003eRibonucleotide reductase converts ribonucleotides to deoxyribonucleotides 543\u003c\/p\u003e \u003cp\u003eThymidine nucleotides are produced by methylation 544\u003c\/p\u003e \u003cp\u003eNucleotide degradation produces urate or amino acids 545\u003c\/p\u003e \u003cp\u003e\u003cb\u003e19 \u003c\/b\u003e\u003cb\u003eRegulation of Mammalian Fuel Metabolism 555\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e19.1 Integration of Fuel Metabolism 555\u003c\/p\u003e \u003cp\u003eOrgans are specialized for different functions 556\u003c\/p\u003e \u003cp\u003eMetabolites travel between organs 557\u003c\/p\u003e \u003cp\u003eBox 19.A The Intestinal Microbiota Contribute to Metabolism 558\u003c\/p\u003e \u003cp\u003e19.2 Hormonal Control of Fuel Metabolism 560\u003c\/p\u003e \u003cp\u003eInsulin is released in response to glucose 560\u003c\/p\u003e \u003cp\u003eInsulin promotes fuel use and storage 561\u003c\/p\u003e \u003cp\u003emTOR responds to insulin signaling 563\u003c\/p\u003e \u003cp\u003eGlucagon and epinephrine trigger fuel mobilization 564\u003c\/p\u003e \u003cp\u003eAdditional hormones influence fuel metabolism 565\u003c\/p\u003e \u003cp\u003eAMP-dependent protein kinase acts as a fuel sensor 566\u003c\/p\u003e \u003cp\u003eFuel metabolism is also controlled by redox balance and oxygen 566\u003c\/p\u003e \u003cp\u003e19.3 Disorders of Fuel Metabolism 568\u003c\/p\u003e \u003cp\u003eThe body generates glucose and ketone bodies during starvation 568\u003c\/p\u003e \u003cp\u003eBox 19.B Marasmus and Kwashiorkor 568\u003c\/p\u003e \u003cp\u003eObesity has multiple causes 569\u003c\/p\u003e \u003cp\u003eDiabetes is characterized by hyperglycemia 570\u003c\/p\u003e \u003cp\u003eObesity, diabetes, and cardiovascular disease are linked 572\u003c\/p\u003e \u003cp\u003e19.4 Clinical Connection: Cancer Metabolism 573\u003c\/p\u003e \u003cp\u003eAerobic glycolysis supports biosynthesis 573\u003c\/p\u003e \u003cp\u003eCancer cells consume large amounts of glutamine 574\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 4 \u003c\/b\u003e\u003cb\u003eGenetic Information\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e20 \u003c\/b\u003e\u003cb\u003eDNA Replication and Repair 582\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e20.1 The DNA Replication Machinery 582\u003c\/p\u003e \u003cp\u003eReplication occurs in factories 583\u003c\/p\u003e \u003cp\u003eHelicases convert double-stranded DNA to single-stranded DNA 584\u003c\/p\u003e \u003cp\u003eDNA polymerase faces two problems 585\u003c\/p\u003e \u003cp\u003eDNA polymerases share a common structure and mechanism 587\u003c\/p\u003e \u003cp\u003eDNA polymerase proofreads newly synthesized DNA 589\u003c\/p\u003e \u003cp\u003eAn RNase and a ligase are required to complete the lagging strand 590\u003c\/p\u003e \u003cp\u003e20.2 Telomeres 593\u003c\/p\u003e \u003cp\u003eTelomerase extends chromosomes 594\u003c\/p\u003e \u003cp\u003eBox 20.A HIV Reverse Transcriptase 595\u003c\/p\u003e \u003cp\u003eIs telomerase activity linked to cell immortality? 596\u003c\/p\u003e \u003cp\u003e20.3 DNA Damage and Repair 596\u003c\/p\u003e \u003cp\u003eDNA damage is unavoidable 597\u003c\/p\u003e \u003cp\u003eRepair enzymes restore some types of damaged DNA 598\u003c\/p\u003e \u003cp\u003eBase excision repair corrects the most frequent DNA lesions 598\u003c\/p\u003e \u003cp\u003eNucleotide excision repair targets the second most common form of DNA damage 599\u003c\/p\u003e \u003cp\u003eDouble-strand breaks can be repaired by joining the ends 601\u003c\/p\u003e \u003cp\u003eRecombination also restores broken DNA molecules 601\u003c\/p\u003e \u003cp\u003eBox 20.B Gene Editing with CRISPR 602\u003c\/p\u003e \u003cp\u003e20.4 Clinical Connection: Cancer as a Genetic Disease 604\u003c\/p\u003e \u003cp\u003eTumor growth depends on multiple events 605\u003c\/p\u003e \u003cp\u003eDNA repair pathways are closely linked to cancer 605\u003c\/p\u003e \u003cp\u003e20.5 DNA Packaging 607\u003c\/p\u003e \u003cp\u003eDNA is negatively supercoiled 607\u003c\/p\u003e \u003cp\u003eTopoisomerases alter DNA supercoiling 608\u003c\/p\u003e \u003cp\u003eEukaryotic DNA is packaged in nucleosomes 610\u003c\/p\u003e \u003cp\u003e20.6 Tools and Techniques: Manipulating DNA 611\u003c\/p\u003e \u003cp\u003eCutting and pasting generates recombinant DNA 612\u003c\/p\u003e \u003cp\u003eThe polymerase chain reaction amplifies DNA 614\u003c\/p\u003e \u003cp\u003eDNA sequencing uses DNA polymerase to make a complementary strand 615\u003c\/p\u003e \u003cp\u003e\u003cb\u003e21 \u003c\/b\u003e\u003cb\u003eTranscription and RNA 627\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e21.1 Initiating Transcription 627\u003c\/p\u003e \u003cp\u003eWhat is a gene? 628\u003c\/p\u003e \u003cp\u003eDNA packaging affects transcription 628\u003c\/p\u003e \u003cp\u003eDNA also undergoes covalent modification 631\u003c\/p\u003e \u003cp\u003eTranscription begins at promoters 631\u003c\/p\u003e \u003cp\u003eTranscription factors recognize eukaryotic promoters 633\u003c\/p\u003e \u003cp\u003eMediator integrates multiple regulatory signals 634\u003c\/p\u003e \u003cp\u003eBox 21.A DNA-Binding Proteins 635\u003c\/p\u003e \u003cp\u003eProkaryotic operons allow coordinated gene expression 636\u003c\/p\u003e \u003cp\u003e21.2 RNA Polymerase 638\u003c\/p\u003e \u003cp\u003eRNA polymerases have a common structure and mechanism 639\u003c\/p\u003e \u003cp\u003eBox 21.B RNA-Dependent RNA Polymerase 640\u003c\/p\u003e \u003cp\u003eRNA polymerase is a processive enzyme 641\u003c\/p\u003e \u003cp\u003eTranscription elongation requires changes in RNA polymerase 642\u003c\/p\u003e \u003cp\u003eTranscription is terminated in several ways 644\u003c\/p\u003e \u003cp\u003e21.3 RNA Processing 645\u003c\/p\u003e \u003cp\u003eEukaryotic mRNAs receive a 5′ cap and a 3′ poly(A) tail 645\u003c\/p\u003e \u003cp\u003eSplicing removes introns from eukaryotic RNA 646\u003c\/p\u003e \u003cp\u003emRNA turnover and RNA interference limit gene expression 649\u003c\/p\u003e \u003cp\u003eBox 21.C The Nuclear Pore Complex 649\u003c\/p\u003e \u003cp\u003erRNA and tRNA processing includes the addition, deletion, and modification of nucleotides 652\u003c\/p\u003e \u003cp\u003eRNAs have extensive secondary structure 653\u003c\/p\u003e \u003cp\u003e\u003cb\u003e22 \u003c\/b\u003e\u003cb\u003eProtein Synthesis 663\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e22.1 tRNA and the Genetic Code 663\u003c\/p\u003e \u003cp\u003eThe genetic code is redundant 664\u003c\/p\u003e \u003cp\u003etRNAs have a common structure 665\u003c\/p\u003e \u003cp\u003etRNA aminoacylation consumes ATP 666\u003c\/p\u003e \u003cp\u003eEditing increases the accuracy of aminoacylation 667\u003c\/p\u003e \u003cp\u003etRNA anticodons pair with mRNA codons 668\u003c\/p\u003e \u003cp\u003eBox 22.A The Genetic Code Expanded 669\u003c\/p\u003e \u003cp\u003e22.2 Ribosome Structure 669\u003c\/p\u003e \u003cp\u003eThe ribosome is mostly RNA 670\u003c\/p\u003e \u003cp\u003eThree tRNAs and one mRNA bind to the ribosome 671\u003c\/p\u003e \u003cp\u003e22.3 Translation 673\u003c\/p\u003e \u003cp\u003eInitiation requires an initiator tRNA 673\u003c\/p\u003e \u003cp\u003eThe appropriate tRNAs are delivered to the ribosome during elongation 675\u003c\/p\u003e \u003cp\u003eThe peptidyl transferase active site catalyzes peptide bond formation 677\u003c\/p\u003e \u003cp\u003eBox 22.B Antibiotic Inhibitors of Protein Synthesis 679\u003c\/p\u003e \u003cp\u003eRelease factors mediate translation termination 680\u003c\/p\u003e \u003cp\u003eTranslation is efficient and dynamic 681\u003c\/p\u003e \u003cp\u003e22.4 Post-Translational Events 683\u003c\/p\u003e \u003cp\u003eChaperones promote protein folding 684\u003c\/p\u003e \u003cp\u003eThe signal recognition particle targets some proteins for membrane translocation 685\u003c\/p\u003e \u003cp\u003eMany proteins undergo covalent modification 687\u003c\/p\u003e \u003cp\u003eGlossary G-1\u003c\/p\u003e \u003cp\u003eOdd-Numbered Solutions S-1\u003c\/p\u003e \u003cp\u003eIndex i-1\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default 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