Lehninger Biochemistry: Core Concepts and Applications (International Edition)

Höfundar: Michael M. Cox; Aaron A. Hoskins; Alain Viel; Judith Simcox (Útgáfa: 1)
Lehninger Biochemistry: Core Concepts and Applications (International Edition)

Kaup valmöguleikar

Lehninger Biochemistry: Core Concepts and Applications offers a streamlined, focused exploration of key biochemistry concepts, tailored for students in Chemistry, Biophysics, and other STEM fields. Authored by the creators of the renowned Lehninger Principles of Biochemistry, this text emphasises clear, concise explanations, supported by visually engaging figures and relevant medical applications.

Nánar um bókina

Útgefandi
Macmillan Learning
ISBN
9781319595463
Print ISBN
9781319589967
Format
ePub
Útgáfa
1
Höfundar
Michael M. Cox; Aaron A. Hoskins; Alain Viel; Judith Simcox
Tungumál
English
Útgefið
04/04/2025
Prent takmörkun á líftíma
100
Prent takmörkun
10
Afritunar takmörkun
2

Kaflar

  • About this Book
  • Cover Page
  • Accessibility
  • Title Page
  • Copyright Page
  • Dedication
  • About the U.S. Edition Cover
  • About the Authors
  • Preface
  • A Note About AI
  • Contents in Brief
  • Contents
  • Chapter 1 Biochemistry Concepts and Themes
  • 1.1 Science and the Scientific Method
  • What Is Science?
  • What Is the Scientific Method?
  • 1.2 Organisms, Cells, Chromosomes, and Genes
  • Organisms Belong to Three Distinct Domains of Life
  • Cells Are the Structural and Functional Units of All Living Organisms
  • Viruses Cannot Live Independently of Cells
  • Bacterial Cells Feature a Relatively Simple Architecture and Streamlined Lifestyles
  • Eukaryotic Cells Have a Variety of Membranous Organelles
  • Cells Contain a Wide Range of Supramolecular Structures
  • Major Model Organisms and Systems Are Useful in Biochemistry
  • The Linear Sequence in DNA Encodes Proteins with Three-Dimensional Structures
  • 1.3 The Organic Chemistry of Biochemistry
  • Major Organic Species Are Found in Cells
  • Macromolecules Are Major Constituents of Cells
  • Molecular Weight and Molecular Mass Are Expressed by Distinct Conventions
  • Nucleophiles and Electrophiles Define How Many Reactions Proceed
  • Cofactors Facilitate Particular Classes of Biochemical Reactions
  • 1.4 A Review of Basic Thermodynamics
  • Equilibrium Constants and Rate Constants Describe Distinct but Related Thermodynamic Parameters
  • Organisms Transform Energy and Matter from Their Surroundings
  • Creating and Maintaining Order Requires Work and Energy
  • 1.5 Using Data Banks
  • End of Chapter
  • Key Terms
  • Chapter 2 Water: The Chemistry of Life
  • 2.1 Weak Interactions in Aqueous Systems
  • Hydrogen Bonds Give Water Its Unusual Properties
  • Water Interacts Electrostatically with Charged Solutes
  • Nonpolar Gases Are Poorly Soluble in Water
  • The Hydrophobic Effect Is an Entropy-based Phenomenon
  • Van der Waals Interactions and Other Weak Interactions Are Key to Macromolecular Structure and Function
  • 2.2 Ionization of Water, Weak Acids, and Weak Bases
  • The Ionization of Water Is Expressed by an Equilibrium Constant
  • The pH Scale Designates H+ and OH– Concentrations
  • Weak Acids and Bases Have Characteristic Acid Dissociation Constants
  • Titration Curves Reveal the pKa of Weak Acids
  • 2.3 Buffering Against pH Changes in Biological Systems
  • A Buffer System Resists Changes in pH in Response to Added Acid or Base
  • The Henderson-Hasselbalch Equation Relates pH, pKa, and Buffer Concentration
  • Weak Acids or Bases Buffer Cells and Tissues Against pH Changes
  • Bicarbonate Is an Important Biological Buffer System
  • Untreated Diabetes Produces Life-Threatening Acidosis
  • End of Chapter
  • Key Terms
  • Chapter 3 Amino Acids, Peptides, and Proteins
  • 3.1 Amino Acids
  • What Is an Amino Acid?
  • The Amino Acids in Proteins Are L Stereoisomers
  • Amino Acids Can Be Classified by R Group
  • Some Amino Acids Absorb Ultraviolet Light
  • Uncommon Amino Acids Also Have Important Functions
  • Amino Acids Can Act as Acids and Bases
  • Amino Acids Differ in Their Acid-Base Properties
  • 3.2 Peptides and Proteins
  • Peptides Are Chains of Amino Acids
  • Disulfide Bonds Occur in Some Proteins
  • Ionization Behavior Can Distinguish Peptides
  • Some Proteins Contain Chemical Groups Other than Amino Acids
  • 3.3 Purifying Proteins
  • Proteins Can Be Separated and Purified
  • Proteins Are Detected and Quantified Based on Their Functions
  • Proteins Can Be Separated and Characterized by Electrophoresis
  • 3.4 The Primary Structure of Proteins and Protein Chemistry
  • There Are Levels of Complexity to Protein Structure
  • The Function of a Protein Depends on Its Amino Acid Sequence
  • There Are Multiple Ways to Reduce a Polypeptide Chain into Fragments
  • Mass Spectrometry Provides Information on Molecular Mass, Amino Acid Sequence, and Entire Proteomes
  • Amino Acid Sequences Provide Important Biochemical and Evolutionary Information
  • End of Chapter
  • Key Terms
  • Chapter 4 Protein Structure
  • 4.1 Forces and Interactions That Stabilize Protein Structures
  • Protein Structures Are Largely Stabilized by Weak Interactions
  • Hydrogen Bonding, Ion Pairs, and van der Waals Interactions Also Contribute to Protein Folding
  • The Conformation of the Peptide Bond Constrains Polypeptide Conformation
  • 4.2 Secondary Protein Structure
  • The α Helix Maximizes the Use of Polypeptide Hydrogen Bonds
  • The β Strand Is a Common Secondary Structure with an Extended Conformation
  • Ramachandran Plots Describe the Distribution of Secondary Structure in a Protein
  • 4.3 Tertiary and Quaternary Protein Structure
  • Fibrous Proteins Have a Single Type of Secondary Structure
  • The Fibrous Protein Collagen Is the Most Abundant Protein in Mammals
  • Silk Is Made from a Fibrous Protein with β-Sheet Secondary Structure
  • Globular Proteins Are Compact and Highly Varied in Three-Dimensional Structure
  • Protein Tertiary Structures Can Be Described in Terms of Motifs and Domains
  • Intrinsically Disordered Proteins Lack Stable Tertiary Structures
  • Quaternary Structure Describes the Organization of Multisubunit Proteins
  • Biomolecular Structures Can Be Determined Using a Variety of Methods
  • The Protein Data Bank Is a Repository for Biomolecular Structures
  • 4.4 Protein Denaturation and Folding
  • Loss of Protein Structure Results in Loss of Function
  • Amino Acid Sequence Determines Tertiary Structure
  • Protein Folding Occurs by Defined Pathways and Can Be Assisted by Chaperones
  • Defects in Protein Folding Cause Human Disease
  • End of Chapter
  • Key Terms
  • Chapter 5 Protein Function and Ligand Binding
  • 5.1 Reversible Protein-Ligand Binding
  • Ligands Bind to Proteins Reversibly at Binding Sites
  • Protein-Ligand Interactions Can Be Described Quantitatively
  • 5.2 Reversible Binding of a Ligand to a Protein: Oxygen Binding by Myoglobin
  • Oxygen Can Bind to a Heme Prosthetic Group
  • Globins Are a Family of Oxygen-Binding Proteins
  • The Binding of Oxygen to Myoglobin Can Be Described Quantitatively
  • Protein Structure Affects How Ligands Bind
  • 5.3 Reversible and Cooperative Binding of a Ligand to a Protein: Oxygen Binding by Hemoglobin
  • Hemoglobin Subunits Are Structurally Similar to Myoglobin
  • Hemoglobin Undergoes a Structural Change on Binding Oxygen
  • Hemoglobin Binds Oxygen Cooperatively
  • Cooperative Ligand Binding Can Be Described Quantitatively
  • Hemoglobin Also Transports H+ and CO2
  • 5.4 Medical Conditions Related to Hemoglobin
  • CO Binding to Hemoglobin Poses a Serious Health Risk
  • Altered Hemoglobin Subunit Interactions in Sickle Cell Anemia Cause Pain and Suffering
  • End of Chapter
  • Key Terms
  • Chapter 6 Protein Function and Enzymes
  • 6.1 What Are Enzymes?
  • Most Enzymes Are Proteins
  • Enzyme-Catalyzed Reactions Occur Within Active Sites
  • Enzymes Affect Reaction Rates, Not Equilibria
  • Reaction Rates and Equilibria Are Described by Constants
  • 6.2 How Enzymes Work
  • Noncovalent Interactions Between Enzyme and Substrate Are Optimized in the Transition State
  • Enzymes Use a Variety of Additional Chemical Mechanisms to Facilitate Catalysis
  • Coenzymes Facilitate Particular Types of Reactions
  • 6.3 Enzyme Kinetics
  • The Steady State of an Enzyme-Catalyzed Reaction Reflects the Concentration of ES
  • The Relationship Between Substrate Concentration and Reaction Rate Can Be Described Quantitatively
  • Scientists Compare Enzymes Using Vmax and Km
  • Enzymes Are Subject to Reversible and Irreversible Inhibition
  • Irreversible Inhibitors Inactivate Enzymes
  • 6.4 Chymotrypsin and Enzymatic Catalysis
  • The Chymotrypsin Mechanism Involves Acylation and Deacylation of an Active-Site Ser Residue
  • An Understanding of Protease Mechanisms Led to Treatments for HIV
  • An Understanding of Enzyme Mechanism Leads to Useful Antibiotics
  • 6.5 Regulatory Enzymes
  • Some Enzymes Are Regulated by Allosteric Conformational Changes in Response to Modulator Binding
  • Some Enzymes Are Regulated by Reversible Covalent Modification
  • Some Enzymes Are Regulated by Proteolytic Cleavage of an Enzyme Precursor
  • End of Chapter
  • Key Terms
  • Chapter 7 Carbohydrates
  • 7.1 Monosaccharides and Disaccharides
  • The Two Families of Monosaccharides Are Aldoses and Ketoses
  • The Common Monosaccharides Have Cyclic Structures
  • Sugars Containing and Forming Aldehydes Are Reducing Sugars
  • Disaccharides Consist of Two Monosaccharides Joined by a Glycosidic Bond
  • 7.2 Polysaccharides
  • Some Homopolysaccharides Are Storage Forms of Fuel While Others Have Structural Roles
  • Glycosaminoglycans Are Heteropolysaccharides of the Extracellular Matrix
  • 7.3 Glycoconjugates: Peptidoglycans, Proteoglycans, Glycoproteins, and Glycolipids
  • Peptidoglycan Reinforces the Bacterial Cell Wall
  • Proteoglycans Are Glycosaminoglycan-Containing Macromolecules of the Cell Surface and Extracellular Matrix
  • Glycoproteins Are Proteins with Covalently Attached Oligosaccharides
  • Glycolipids and Lipopolysaccharides Are Membrane Components
  • 7.4 Carbohydrates as Signaling Molecules
  • Oligosaccharides Have Highly Diverse Structures
  • Lectins Are Proteins That Bind Specifically to Complex Oligosaccharides and Mediate Many Biological Processes
  • End of Chapter
  • Key Terms
  • Chapter 8 Lipids, Membranes, and Membrane Proteins
  • 8.1 Membrane Lipids
  • Fatty Acids Are the Hydrocarbon Chains of Membrane Lipids
  • Fatty Acid Composition of Lipids Impacts Health
  • Structural Elements Distinguish Membrane Lipid Classes
  • Membrane Lipids Are Amphipathic Molecules That Form Lipid Bilayers
  • Membrane Lipid Composition Impacts Membrane Fluidity
  • 8.2 The Architecture of Membrane Proteins
  • Membrane Proteins Differ in How They Associate with the Membrane Bilayer
  • Integral Membrane Proteins Span Membranes and Can Be Transporters
  • Peripheral Membrane Proteins Interact with Membranes Through Electrostatic Charge
  • Lipid-Anchored Proteins Are Covalently Linked to Hydrophobic Anchors Embedded in the Membrane
  • 8.3 Moving Molecules Through Membranes
  • Membrane Transporters Are Required to Move Large and Charged Molecules Across Membranes
  • Transport into and out of Cells May Be Passive or Active
  • Transporters and Ion Channels Share Structural Properties but Have Different Mechanisms
  • The Glucose Transporter of Erythrocytes Mediates Passive Transport
  • P-Type ATPases Are Active Transporters That Change Conformation with Phosphorylation from ATP
  • Ion Channels Allow Rapid Movement of Ions Across Membranes
  • End of Chapter
  • Key Terms
  • Chapter 9 Nucleotides and Nucleic Acids
  • 9.1 Nucleotides
  • Nucleotides Have Three Molecular Components
  • The Common Nucleotides Have Many Uncommon Variants
  • Phosphodiester Bonds Link Successive Nucleotides in Nucleic Acids
  • The Properties of Nucleotide Bases Affect the Three-Dimensional Structure of Nucleic Acids
  • 9.2 Nucleic Acid Structures
  • DNA Is a Double Helix That Stores Genetic Information
  • DNA Can Occur in Different Three-Dimensional Forms
  • Certain DNA and RNA Sequences Adopt Unusual Structures
  • Messenger RNAs Code for Polypeptide Chains
  • Many RNAs Have More Complex Three-Dimensional Structures
  • 9.3 Nucleic Acid Chemistry
  • Double-Helical DNA and RNA Can Be Denatured
  • Base Stacking Affects the UV Absorption Properties of DNA and RNA
  • Nucleotides and Nucleic Acids Undergo Nonenzymatic Transformations
  • 9.4 Nucleotide Roles in Cell Energetics and Signaling
  • Nucleotides Carry Chemical Energy in Cells
  • Some Nucleotides Are Regulatory Molecules or Signals
  • Adenine Nucleotides Serve as Constituents of Many Enzymatic Cofactors; a Clue to the Origin of Life?
  • End of Chapter
  • Key Terms
  • Chapter 10 Biological Information Part 1: DNA and RNA Metabolism
  • 10.1 DNA Replication
  • DNA Replication Follows a Set of Rules
  • DNA Polymerases Synthesize DNA
  • DNA Replication Requires Many Enzymes and Protein Factors
  • DNA Replication Occurs in Stages
  • 10.2 DNA Repair and Organization
  • All Cells Have Multiple DNA Repair Systems
  • DNA Repair Can Also Occur in the Absence of Replication
  • DNA Is Organized into Chromatin
  • 10.3 Transcription and RNA Processing
  • RNA Polymerases Synthesize RNA
  • Transcription Requires Many Enzymes and Protein Factors
  • RNA Synthesis Occurs in Stages
  • Medicines Can Target or Be Made by RNA Polymerases
  • Nearly All Eukaryotic RNAs Must Be Processed
  • Reverse Transcriptases Produce DNA from RNA
  • 10.4 Regulation of Transcription
  • Transcription of Specific Genes Requires Regulatory Proteins in Addition to RNA Polymerase
  • Regulation of Gene Expression in Bacteria
  • Regulation of Gene Expression in Eukaryotes
  • End of Chapter
  • Key Terms
  • Chapter 11 Biological Information Part 2: Protein Metabolism
  • 11.1 The Genetic Code
  • The Genetic Code Describes How Sets of Nucleic Acids Correspond to Particular Amino Acids
  • tRNA Anticodons Base-Pair with Codons
  • tRNAs Are Charged with Amino Acids for Protein Synthesis
  • tRNA Charging Requires ATP Hydrolysis
  • 11.2 Structure and Function of Ribosomes
  • Ribosomes Catalyze Protein Synthesis
  • Protein Synthesis Occurs in Stages
  • Translation Factors Interact with the Ribosome During Elongation and Termination
  • Protein Synthesis by the Ribosomes Is Energetically Expensive
  • 11.3 Protein Folding, Modification, and Degradation
  • Chaperones Help Proteins Fold into Their Native Conformation
  • Posttranslational Modifications Are Critical for the Function of Many Proteins
  • Protein Degradation Is Highly Regulated in Eukaryotes by the Ubiquitin/Proteosome Pathway
  • 11.4 Translational Control
  • Riboswitches, Small RNAs, and Attenuation Can Control Gene Expression in Bacteria
  • Eukaryotes Use mRNA Binding Proteins, RNAi, and MicroRNAs to Regulate Protein Production
  • End of Chapter
  • Key Terms
  • Chapter 12 Nucleic Acid Technologies
  • 12.1 Defining Genomic Information
  • The Genome Is All of the Nucleic Acid Needed to Support the Life of an Organism
  • The Polymerase Chain Reaction Provides Targeted Amplification of Genomic Information
  • DNA Can Be Sequenced
  • Sanger Sequencing Has Been Automated
  • Next-Generation DNA Sequencing Produces Complete Genome Sequences
  • RNA Can Be Sequenced by First Converting the RNA to DNA with Reverse Transcriptase
  • 12.2 Altering Genomic Information
  • Joining DNA Segments from Different Sources Yields Recombinant DNA
  • DNA Segments Can Be Joined Without Using Restriction Enzymes
  • Cloned DNA Can Be Altered to Study Genes and Proteins
  • CRISPR/Cas Systems Allow Targeted Cleavage or Modification of Genomic Information
  • 12.3 Using Genomic Information
  • An Altered Genome Can Lead to an Altered Transcriptome and Proteome
  • Genomic Information Can Be Used to Identify the Source of Genetic Diseases
  • Genomic Information Can Be Used to Investigate Crimes
  • End of Chapter
  • Key Terms
  • Chapter 13 Introduction to Intermediary Metabolism
  • 13.1 What Is Metabolism?
  • Molecules Are Metabolized by Anabolic and Catabolic Pathways
  • Metabolic Pathways Can Be Converging, Diverging, or Cyclic
  • 13.2 Common Enzyme Reactions in Metabolism
  • Carbonyls Are Important for Making and Breaking Carbon–Carbon Bonds
  • Rearrangement and Isomerization Reactions Reposition Reactive Groups
  • Elimination Reactions Release Good Leaving Groups
  • Free-Radical Reactions Involve Complex Rearrangements
  • Group Transfer Reactions Add or Subtract Functional Groups to Metabolites
  • Oxidation-Reduction Reactions Involve Electron Transfer to or from Biomolecules
  • 13.3 ATP and Phosphoryl Group Transfers
  • ATP Contains Phosphoanhydride Bonds
  • ATP Hydrolysis Is Thermodynamically Very Favorable
  • Many Other Metabolites and Enzyme Reaction Intermediates Also Have Large, Negative Free Energies of Hydrolysis
  • ATP Donates Phosphoryl, Pyrophosphoryl, and Adenylyl Groups
  • ATP Can Provide Energy by Group Transfers, Not Just by Hydrolysis
  • 13.4 Biological Oxidation-Reduction Reactions
  • Oxidation-Reduction Reactions Can Be Described as Half-Reactions
  • Biological Oxidations Often Involve Dehydrogenation
  • A Few Types of Coenzymes and Proteins Serve as Universal Electron Carriers
  • 13.5 Regulation of Metabolic Pathways
  • Cells and Organisms Maintain a Dynamic Steady State
  • Both the Amount and the Catalytic Activity of an Enzyme Can Be Regulated
  • End of Chapter
  • Key Terms
  • Chapter 14 Carbohydrate Metabolism Part 1: Glycolysis and Glycogen Synthesis
  • 14.1 An Overview of Glycolysis
  • Glycolysis Has Two Phases: The Preparatory and Payoff Phases
  • In Glycolysis, the Potential Energy of Glucose Is Partially Converted to ATP and NADH
  • Phosphorylated Intermediates Are Important in Glycolysis
  • 14.2 The Preparatory and Payoff Phases of Glycolysis
  • The Preparatory Phase of Glycolysis Converts Glucose to a Three-Carbon Metabolite and Consumes ATP
  • The Payoff Phase of Glycolysis Yields ATP, NADH, and Pyruvate
  • The Glycolytic Pathway Conserves Part of the Energy Released as ATP and NADH
  • Feeder Pathways Provide Additional Fuel for Glycolysis
  • 14.3 Fermentation of Pyruvate
  • There Are Two Anaerobic Fermentation Pathways
  • The Warburg Effect Describes How Cancer Cells Rely Almost Entirely on Glycolysis for Energy
  • 14.4 The Pentose Phosphate Pathway
  • The Pentose Phosphate Pathway Generates NADPH and Essential Pentose Phosphates
  • The Oxidative Phase Produces NADPH and Pentose Phosphates
  • The Nonoxidative Phase Recycles Pentose Phosphates to Glucose 6-Phosphate, Fructose 6-Phosphate, and Glyceraldehyde 3-Phosphate
  • NADPH Produced by the Pentose Phosphate Pathway Defends Cells from Reactive Oxygen Species
  • Deficiencies in the Oxidative Phase of the Pentose Phosphate Pathway Have Serious Health Consequences
  • 14.5 Glycogen Synthesis
  • Glycogen Provides a Specialized Molecular Structure for Glucose Storage
  • The Sugar Nucleotide UDP-Glucose Donates Glucose for Glycogen Synthesis
  • Defects in Glycogen Synthesis Have Important Medical Consequences
  • End of Chapter
  • Key Terms
  • Chapter 15 Carbohydrate Metabolism Part 2: Gluconeogenesis and Glycogen Degradation
  • 15.1 Gluconeogenesis
  • Gluconeogenesis and Glycolysis Share Many but Not All Steps and Enzymes
  • Glycolytic Enzymes Are Bypassed at Three Steps in Gluconeogenesis
  • Gluconeogenesis Is Energetically Expensive and Essential
  • 15.2 Coordinated Regulation of Glycolysis and Gluconeogenesis
  • Hexokinase Isozymes Are Affected Differently by Their Product, Glucose 6-Phosphate
  • Phosphofructokinase-1 and Fructose 1,6-Bisphosphatase-1 Are Reciprocally Regulated
  • Fructose 2,6-Bisphosphate Is a Potent Allosteric Regulator of PFK-1 and FBPase-1
  • 15.3 Breakdown of Glycogen and Its Regulation
  • Glycogen Breakdown Is Catalyzed by Glycogen Phosphorylase
  • Glycogen Phosphorylase Is Regulated by Hormone-Stimulated Phosphorylation and by Allosteric Effectors
  • Allosteric and Hormonal Signals Coordinate Carbohydrate Metabolism Throughout the Body
  • End of Chapter
  • Key Terms
  • Chapter 16 Pyruvate Oxidation and the Citric Acid Cycle
  • 16.1 Conversion of Pyruvate to Acetyl-CoA
  • The Citric Acid Cycle Occurs in Mitochondria
  • Pyruvate Is Oxidized by Pyruvate Dehydrogenase to Generate Acetyl-CoA, NADH, and CO2
  • The Pyruvate Dehydrogenase Complex Promotes a Multistage Reaction Sequence
  • Pyruvate Dehydrogenase Is Subject to Regulation
  • 16.2 The Citric Acid Cycle
  • Citrate, the First Tricarboxylic Acid, Forms in Step 1
  • A Citrate Hydroxyl Group Moves in Step 2
  • Following the Formation of Isocitrate, Two Oxidative Decarboxylations That Form CO2 Occur with Different Mechanisms
  • Succinyl-CoA Synthetase Promotes the Formation of Succinate and GTP in Step 5
  • The Final Three Steps Convert Succinate to Oxaloacetate via a Common Oxidative Path
  • The Energy of Oxidation Is Conserved in the Citric Acid Cycle
  • The Concentration of Key Metabolites Regulates Flux Through the Citric Acid Cycle
  • 16.3 The Citric Acid Cycle as a Metabolic Hub
  • The Citric Acid Cycle Plays a Central Role in Catabolism and Anabolism
  • A Variety of Reactions Replenish Citric Acid Cycle Intermediates or Supplement Cycle Products
  • 16.4 The Citric Acid Cycle Affects Cell State and Disease State
  • Changes in Cell State Can Be Accompanied by Flux Through a Noncanonical Citric Acid Cycle
  • Vitamin Deficiencies Result in Disease
  • Amino Acid Substitutions in Isocitrate Dehydrogenase Facilitate Tumor Growth
  • End of Chapter
  • Key Terms
  • Chapter 17 Lipid Catabolism and Anabolism
  • 17.1 The Fed State: Digestion, Synthesis, and Storage of Fats
  • Biosynthesis of Fatty Acids Requires Two Enzyme Complexes
  • Fatty Acid Synthesis Is Tightly Regulated
  • Free Fatty Acids Are Incorporated into Glycerolipids
  • Triacylglycerol Biosynthesis Is Regulated by Hormones
  • 17.2 Synthesis and Transport of Cholesterol
  • Cholesterol Is Made from Acetyl-CoA in Four Stages
  • Cholesterol Has Several Fates
  • Cholesterol and Other Lipids Are Carried as Lipoprotein Particles
  • HDL and LDL Cholesterol Enter Cells Through Receptor-Mediated Interactions
  • Dysregulation of Cholesterol Can Lead to Cardiovascular Disease
  • 17.3 The Fasted State: Fatty Acid Oxidation and Production of Ketone Bodies
  • Lipid Catabolism Occurs in Fasted States
  • Fatty Acid Oxidation Occurs in the Mitochondria
  • Fatty Acid Oxidation Is Regulated by Compartmentalization
  • Ketone Bodies Are Formed in the Liver and Exported to Other Tissues
  • Ketone Bodies Are Overproduced in Diabetes and Starvation
  • End of Chapter
  • Key Terms
  • Chapter 18 Amino Acid Catabolism and Anabolism
  • 18.1 The Worldwide Nitrogen Web and Its Many Interfaces with Living Systems
  • A Global Nitrogen Web Makes Atmospheric Nitrogen Available to Cells
  • Nitrogen Is Converted to Ammonia by Enzymes of the Nitrogenase Complex
  • Ammonia Is Incorporated into Biomolecules Through Glutamate and Glutamine
  • Amino Groups Are Distributed Primarily via Transamination Facilitated by Pyridoxal Phosphate
  • Ammonia Generated by Some Cellular Processes Is Toxic to Animals
  • A Few Amino Acids Play Special Roles in Nitrogen Metabolism
  • 18.2 Disposal of Amino Groups via the Urea Cycle
  • In Extrahepatic Tissues, Amino Groups Are Incorporated into Glutamine for Transport to the Liver
  • The Urea Cycle Disposes of Excess Amino Groups
  • Connections Among Metabolic Pathways Reduce the Energetic Cost of Urea Synthesis
  • 18.3 Amino Acid Catabolism and Anabolism
  • Amino Acid Catabolism Produces Pyruvate, Acetyl-CoA, and Citric Acid Cycle Intermediates
  • Several Enzyme Cofactors Play Important Roles in Amino Acid Catabolism
  • Some Genetic Deficiency Diseases Are Linked to Amino Acid Catabolism
  • Amino Acid Anabolism Is Often Not the Reverse of Amino Acid Catabolism
  • Organisms Vary Greatly in Their Ability to Synthesize the 20 Common Amino Acids
  • α-Ketoglutarate Gives Rise to Glutamate, Glutamine, Proline, and Arginine
  • 18.4 Molecules Derived from Amino Acids
  • Heme Is Derived from Glycine and Succinyl-CoA
  • Biological Amines Are Products of Amino Acid Decarboxylation
  • Glutathione Is Synthesized from Glutamate, Cysteine, and Glycine
  • 18.5 Nucleotide Biosynthesis
  • The Ribose in Nucleotides Is Derived from Phosphoribosyl Pyrophosphate
  • Pyrimidine Nucleotides Are Made from Aspartate, PRPP, and Carbamoyl Phosphate
  • De Novo Purine Nucleotide Synthesis Begins with PRPP
  • Ribonucleotides Are the Precursors of Deoxyribonucleotides
  • Thymidylate Is Derived from dCDP and dUMP
  • End of Chapter
  • Key Terms
  • Chapter 19 Electron Transfer and Oxidative Phosphorylation
  • 19.1 The Mitochondrial Electron Transport Chain
  • Chemiosmotic Theory Describes How Electron Flow Couples to ATP Synthesis in Mitochondria
  • Mitochondrial Architecture Facilitates Electron Transport and ATP Synthesis
  • Dehydrogenases Funnel Electrons to Universal Electron Acceptors
  • Electrons Pass Through a Series of Membrane-Bound Carriers
  • Electron Carriers Function in Multienzyme Complexes
  • The Energy of Electron Transfer Is Conserved in a Proton Gradient
  • Reactive Oxygen Species Are Generated During Oxidative Phosphorylation
  • 19.2 ATP Synthesis
  • In the Chemiosmotic Model, Oxidation and Phosphorylation Are Obligately Coupled
  • ATP Synthase Has Two Functional Domains, Fo and F1
  • Chemiosmotic Coupling Allows Nonintegral Stoichiometries of O2 Consumption and ATP Synthesis
  • Shuttle Systems Indirectly Convey Cytosolic NADH into Mitochondria for Oxidation
  • Uncoupling the Proton Gradient from ATP Synthesis Produces Heat
  • 19.3 Regulation of Oxidative Phosphorylation and Mitochondrial Disease
  • An Inhibitory Protein Prevents ATP Hydrolysis During Hypoxia
  • Hypoxia Leads to ROS Production and Several Adaptive Responses
  • ATP-Producing Pathways Are Regulated
  • Mitochondrial Enzyme Defects Cause Disease
  • End of Chapter
  • Key Terms
  • Chapter 20 Metabolism and Biosignaling
  • 20.1 Hormone Structure and Action
  • Hormones Act Through Specific High-Affinity Cellular Receptors
  • Hormones Are Chemically Diverse
  • Hormones Regulate Glucose Levels
  • Diabetes Mellitus Arises from Defects in Insulin Production or Action
  • 20.2 Tissue-Specific Metabolism
  • The Liver Processes and Distributes Nutrients in the Fed State
  • The Liver Produces Ketone Bodies to Fuel Peripheral Tissues in Fasting
  • Adipose Tissue Stores and Supplies Fatty Acids
  • Muscle Uses ATP for Mechanical Work
  • 20.3 Hormonal Regulation of Satiety and Body Weight
  • Body Weight Is Tightly Regulated by Hormones
  • Adipose Tissue Produces Multiple Adipokines to Regulate Metabolism
  • The Digestive System Regulates Satiety
  • End of Chapter
  • Key Terms
  • Appendix A Self-Check Answers
  • Appendix B Section Review Questions and Answers
  • Appendix C Chapter Review Questions and Answers
  • Glossary
  • Notes
  • Index
  • Extended Descriptions
  • Cover page
  • Principles of protein structure, self-check questions, and learning goals
  • Protein folding forces and term matching
  • TABLE 1.1 Productive Paths to Scientific Knowledge
  • Dorothy Crowfoot Hodgkin's work
  • Protein misfolding and amyloid fibril formation
  • Two conventions for numbering carbons
  • Complex buffer titration problem solving
  • Lipopolysaccharides as bacterial surface
  • Diabetes diagnosis using H b A 1 c
  • e-book page on globular proteins, discussing their compact structure, and varied functions
  • Study guide section on amino acids, an amino acid structure diagram, and a quiz matching amino acid codes
  • Self-evaluation
  • Titration graph, solution steps, and explanation
  • An interactive question
  • Case study topics covering biomolecules and signal transduction
  • Transcription initiation and elongation in E.coli
  • Mechanism of the interaction of acetaldehyde with a molecule
  • Two overlapping windows
  • Phylogeny of the three domains of life. A “family tree” of this type illustrates evolutionary relationships
  • Common features of bacterial cells and eukaryotic cells
  • Bacterial cell features
  • Eukaryotic cell features
  • Supramolecular structures in cells
  • Common model organisms in biochemistry
  • Biological information transfer from D N A to protein
  • Elements essential to life
  • Atomic bonding patterns and bond cleavage types
  • Geometry of carbon bonding
  • Common functional groups in biochemistry
  • Multiple functional groups often occur together in biochemical molecules
  • The major molecular components of a living cell
  • Comparison between nucleophiles and electrophiles
  • Structure of phenylacetate
  • Reaction coordinate diagram
  • Free energy versus reaction coordinate
  • Light-driven reduction of carbon dioxide
  • Energy yielding oxidation of glucose
  • Adenosine triphosphate (A T P) provides energy
  • Hydrogen bonds between water molecules
  • Bonding within and between water molecules
  • Ice cube with the arrangement of the ball-and-stick models of water molecules
  • Hydrogen bonds between different molecules
  • Strong and weak hydrogen bond
  • Four pairs of hydrogen acceptors and hydrogen donors
  • Chemical structures of 5 polar, 1 nonpolar, and 2 amphipathic biomolecules as ionic forms at p H 7
  • Water dissolves salts by surrounding ions and breaking up the crystal lattice
  • Haworth projection of glucose
  • Noncovalent interactions among biomolecules in aqueous solvent
  • Noncovalent interactions among biomolecules in aqueous solvent
  • Noncovalent interactions among biomolecules in aqueous solvent
  • Noncovalent interactions among biomolecules in aqueous solvent
  • Noncovalent interactions among biomolecules in aqueous solvent
  • Formation of hydrogen bond between the functional groups within a macromolecule
  • Interconversion of two water molecules with a hydronium ion and hydroxyl ion
  • Proton hopping from hydronium ion to water molecules
  • p H scale shows the p H of some aqueous fluids
  • Nine conjugate acid-base pairs arranged along a p H scale
  • Titration curve of acetic acid
  • Interaction of acetic acid and acetate in a buffer system
  • Titration curves for C H 3 C O O H, H 2 P O 4 superscript minus, and N H 4 superscript plus
  • Ionization of histidine
  • Bicarbonate buffer system in blood in capillaries and air in lungs
  • p H optima of pepsin and trypsin
  • General structure of an amino acid
  • Stereoisomerism in alpha-amino acids
  • Two ball-and-stick models of isomers of an amino acid
  • Structural formula of lysine
  • Structure of an amino acid
  • 20 common amino acids in proteins
  • Absorption of ultraviolet light by aromatic amino acids
  • Structures of 4-hydroxyproline and gamma-carboxyglutamate
  • Structures of ornithine and citrulline
  • Effect of the loss of protons on the structure and charge of an amino acid
  • Nonionic and zwitterionic forms
  • Titration of amino acids
  • General structure of an amino acid
  • Formation of a peptide bond
  • Reversible formation of a disulfide bond by the oxidation of two molecules of cysteine
  • Structure of Alanylglutamylglycyllysine
  • Column chromatography
  • Ion-exchange chromatography
  • Size-exclusion and affinity chromatography methods
  • Electrophoresis
  • Levels of organization in a protein
  • Amino acid sequence of bovine insulin
  • Breaking disulfide bonds in proteins
  • Two examples of sequence logos
  • Sequence logo of a polypeptide
  • Figure 4.1 The four levels of protein structure
  • Figure 4.2 The roles of entropy and the hydrophobic effect on protein folding
  • Figure 4.3 The double-bond character of a peptide bond limits the possible conformations of a peptide chain
  • Figure 4.4 phi and psi dihedral angles in a peptide
  • Figure 4.5 Models of the alpha helix, showing different aspects of its structure
  • Figure 4.6 Left and right-handed helices
  • Figure 4.7 The β conformation of polypeptide chains
  • Figure 4.8 Ramachandran plot
  • Different shapes of protein depicted as ribbon structures
  • Figure 4.10 Structure of hair
  • Figure 4.11 Structure of collagen
  • Figure 4.12 Structure of fibroin protein
  • Figure 4.13 Globular protein structures are compact and varied
  • Figure 4.14 Tertiary structure of myoglobin
  • Figure 4.15 Protein structural motifs and domains
  • Figure 4.16 The mammalian vault protein
  • Figure 4.17 Protein denaturation
  • Figure 4.18 A protein-folding pathway for a small protein
  • Figure 4.19 Formation of disease-causing amyloid fibrils
  • Figure 4.20 Pharmacochaperones for treatment of CFTR-folding defects in cystic fibrosis
  • Reversible binding of a protein to a ligand
  • Reversible binding of a protein to a ligand via induced fit
  • Graphical representation of a ligand binding curve
  • Dissociation constants of different interactions
  • Binding curves of two proteins with the same ligand
  • Heme
  • Myoglobin
  • The heme group viewed from the side
  • Graphical representation of binding of oxygen to myoglobin
  • Effects caused by ligand binding to the heme of myoglobin
  • View of myoglobin showing the arrangement of key amino acid residues around the heme
  • Quaternary structure of deoxyhemoglobin
  • All globins have a similar structure
  • Comparison of whale myoglobin with the alpha and beta chains of human hemoglobin
  • The T to R transition
  • Changes in conformation near heme on O2 binding to deoxyhemoglobin
  • A sigmoid (cooperative) binding curve
  • Cooperative binding of oxygen to hemoglobin
  • Formation of carbamino-terminal residue
  • Effect of p H on oxygen binding to hemoglobin
  • Relationship between levels of C O H b in blood and concentration of C O in the surrounding air
  • Several oxygen-binding curves to illustrate the effects of C O binding
  • The effect of the sickle cell anemia mutation
  • Enzyme substrate-complex
  • Reaction coordinate diagram
  • Reaction coordinate diagram comparing enzyme-catalyzed and uncatalyzed reactions
  • Reaction coordinate diagram
  • Uncatalyzed reaction
  • An enzyme active site that is complementary to the structure of the substrate
  • Enzyme catalyzed reaction
  • Interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate
  • A transition state analog
  • General acid and base catalysis
  • The course of an enzyme-catalyzed reaction
  • Effect of substrate concentration on the initial velocity of an enzyme-catalyzed reaction
  • Dependence of initial velocity on substrate concentration
  • Competitive inhibition
  • Uncompetitive inhibition
  • Mixed inhibition
  • Irreversible inhibition
  • Structure of chymotrypsin
  • Two phases of the chymotrypsin reaction
  • Transition state for the acylation phase of the chymotrypsin reaction
  • The p H dependence of chymotrypsin-catalyzed reactions
  • The p H-rate profile of chymotrypsin
  • Mechanism of action of H I V protease
  • H I V protease inhibitors
  • Transpeptidase reaction
  • General structures of penicillins and the inactivation of transpeptidase
  • Subunit interactions in an allosteric enzyme
  • Kinetic behavior of an allosteric enzyme
  • Some enzyme modification reactions
  • Activation of zymogens by proteolytic cleavage
  • Monosaccharides
  • Two enantiomers of glyceraldehyde
  • Fischer projection structures
  • Fischer projection structures of D-Mannose, D-Glucose, D-Galactose, and D-Fructose
  • Fischer projections labeled (a) to (d)
  • Formation of hemiacetals and hemiketals
  • Formation of the two cyclic forms of d-glucose
  • Structure of alpha and beta anomers in aldohexose and ketohexose
  • Structures of different pyranoses and furanoses
  • Fisher projection of D-glucose and Haworth perspective of alpha-D-glucopyranose
  • Fischer projection structures of D-mannose and D-galactose
  • Chair structures of Greek letter alpha-D-Glucopyranose and Greek letter beta-D-Glucopyranose
  • Four sugars labeled (a) to (d) as part of a question
  • Four sugars labeled (a) to (d) as part of a question
  • Formation of maltose
  • Two common disaccharides
  • Disaccharide
  • Homopolysaccharides and heteropolysaccharides
  • Helical structure of starch or glycogen
  • Starch and glycogen
  • Chemical structure and structural model of cellulose chains
  • Repeating units of some common glycosaminoglycans of extracellular matrix
  • Structures of alpha-L-Iduronate (I lowercase D O uppercase A) and beta D-glucuronate (G lowercase L C uppercase A)
  • Repeating units of four common glycosaminoglycans
  • The structure of peptidoglycan
  • Two families of membrane proteoglycans
  • Proteoglycan aggregate of the extracellular matrix
  • Interactions between cells and the extracellular matrix
  • Oligosaccharide linkages in glycoproteins
  • Bacterial lipopolysaccharide
  • Role of lectin-ligand interactions in leukocyte movement to the site of an infection or injury
  • Role of oligosaccharides in recognition events at the cell surface and in the endomembrane system
  • Fatty acid structure and packing
  • Eicosapentaenoic acid (E P A)
  • Fatty acid composition of commonly used dietary oils
  • Three major classes of membrane lipids
  • The three membrane lipid backbones
  • Diversity of glycerophospholipid head groups
  • Structures of a micelle and lipid bilayer with close-ups of the units in the micelle and bilayer
  • Lipid composition of cellular organelles
  • Two extreme states of bilayer lipids
  • Membrane proteins can be integral, peripheral, or lipid-anchored
  • Fluid mosaic model
  • Integral membrane protein aquaporin
  • Lipid-anchored membrane proteins
  • Sequence from 151 to 175
  • Membrane permeability of small molecules
  • Transportation of charged and uncharged molecules
  • Summary of transport types
  • Three general classes of transport systems
  • the diffusion of Polar hydrated substates across a membrane bilayer
  • The difference between transporters and ion channels
  • Role of N a superscript plus K superscript plus A T P ase in animal cells
  • Ligand- and voltage-gated ion channels
  • Formation of nucleotides from individual components followed by the formation of D N A and R N A
  • General structure of a nucleotide and basic structure of a purine and a pyrimidine
  • Structures of purine bases like adenine and guanine and the pyrimidine bases like cytosine, thymine, and uracil
  • Structure of uracil
  • Nucleosides and symbols for four deoxyribonucleotides and four ribonucleotides
  • Structures of the minor purine found in D N A and R N A and additional minor bases found in R N A
  • Structure of a nucleoside
  • Structure of four adenosine monophosphates
  • Guanosine pentaphosphate
  • Phosphodiester linkages in the covalent backbones of D N A and R N A
  • Hydrolysis of R N A
  • Absorption spectra of common nucleotides
  • Three-nucleotide segment of R N A
  • hydrogen-bonding in double stranded D N A
  • Structure of D N A double helix
  • Complementary base pairing in a vertical double helix of D N A
  • A, B, and Z forms of D N A
  • Hairpins and cruciform
  • Chemical structure and stick model of G quadruplex
  • Monocistronic and polycistronic bacterial m R N A
  • Common secondary structures of R N A and R N A hairpin double helix
  • Three-dimensional structure of phenylalanine t R N A with unusual base-pairing, a hammerhead ribozyme, and an m R N A intron
  • Denaturation and annealing
  • Melting curves of two D N A specimens and the relationship between the t subscript lowercase m and the G plus C content of D N A
  • Deamination of cytosine, 5-methylcytosine, adenine, and guanine
  • Removal of guanine from a guanosine residue in D N A
  • Formation of thymine dimer in presence of U V light
  • Different types of nucleoside phosphates
  • A T P, acetic anhydride, and methyl acetate
  • Tyrosine residue modified by an adenylyl group
  • Regulatory nucleotides
  • Structures of adenine nucleotides or nucleosides
  • Structure of adenine with five constituent H C N molecules highlighted inside ovals
  • Replication of a circular double-stranded D N A molecule
  • D N A strands at a replication fork of a linear D N A molecule
  • D N A polymerase reaction
  • Base-pair geometry in case of correct base pairs and incorrect base pairs
  • Greatly simplified depiction of E. coli replisome
  • D N A replication initiation, elongation, and termination in bacteria
  • Steps in lagging strand synthesis
  • Synthesis of lagging strand segments
  • Methyl-directed mismatch repair in E. coli
  • Base-excision repair pathway for D N A repair
  • Nucleotide-excision repair pathway in E. coli
  • Schematic and microscopic view of nucleosomes
  • D N A wrapped around a histone core
  • Transcription by R N A polymerase in italicized E. coli end italics
  • Sequence of D N A nontemplate strand, D N A template strand, and R N A transcript
  • Sigma superscript 70 R N A polymerase holoenzyme of E. coli
  • Transcription initiation and elongation in E.coli
  • Rho-independent termination and rho-dependent termination
  • Structure of rifampin and x-ray crystallographic structure of rifampin bound to R N A polymerase of the pathogen italicized M. tuberculosis end italics
  • Formation of the primary transcript and its processing during the maturation of m R N A in a eukaryotic cell
  • Processing of a eukaryotic m R N A
  • Alternative splicing of m R N A
  • Reverse transcription of m R N A
  • Effect of activators and repressors on gene expression
  • Positive and negative regulation of initiation of transcription
  • Representative bacterial operon with three genes
  • lac operon induction
  • Nuclear envelope, heterochromatin, and euchromatin
  • Overlapping versus nonoverlapping genetic codes
  • Reading frames in the genetic code
  • A codon table for the standard genetic code
  • Pairing relationship of codon and anticodon
  • Structures of t R N A
  • Aminoacylation of t R N A by aminoacyl-t R N A synthetases
  • Ribosomes
  • Stages of translation
  • Formation of the initiation complex in bacteria
  • First elongation step in protein synthesis
  • Second elongation step in bacteria: formation of the first peptide bond
  • Third elongation step in bacteria
  • Termination of protein synthesis in bacteria
  • Schematic of a ricin umbrella gun
  • Chaperonins in protein folding
  • Reactions carried out by chaperone isomerases during protein folding
  • Some modified amino acid residues
  • Farnesylation of a cysteine residue
  • Metallochaperone C C S in complex with S O D 1
  • Structure of ubiquitin
  • Biochemistry of protein ubiquitination
  • Three-dimensional structure of the eukaryotic proteasome
  • Posttranscriptional gene regulation in bacteria
  • R N A silencing in petunias
  • Gene regulation by micro-R N As in animals
  • Eukaryotic m R N As
  • A snapshot of a bacterial genome
  • A snapshot of the human genome
  • The components of the P C R process
  • Amplification of a D N A segment by the polymerase chain reaction (P C R)
  • D N A sequencing by the Sanger method
  • Structure of a dideoxynucleotide
  • Automation of Sanger D N A sequencing reactions
  • Next-generation reversible terminator sequencing: the flow cell
  • Next-generation reversible terminator sequencing: nucleotides and chemistry
  • Next-generation reversible terminator sequencing: recording results
  • Sequence assembly
  • R N A-Sequencing method
  • Elements of a plasmid
  • Use of restriction endonucleases in cloning
  • Gibson assembly joins two D N As
  • Protein fusions used for protein purification
  • Green fluorescent protein (G F P)
  • The C R I S P R slash Cas9 system for genomic engineering
  • C R I S P R-based treatment of Victoria Gray
  • Proteomic changes due to evolution of antibiotic resistance
  • Linkage analysis in the discovery of disease genes
  • Using P C R to solve crimes
  • S T R sequences
  • Cycling of carbon dioxide and oxygen between the autotrophic (photosynthetic) and heterotrophic domains in the biosphere
  • Energy relationships between catabolic and anabolic pathways
  • Three types of nonlinear metabolic pathways
  • Overview of the biochemistry of cellular metabolism.
  • Condensation and decarboxylation reactions
  • Isomerization reactions
  • An elimination reaction
  • A free radical–initiated decarboxylation reaction
  • A group transfer reaction
  • Group transfer by hexokinase
  • Oxidation levels of carbon in common biomolecules.
  • An oxidation-reduction reaction
  • Chemical structure of A T P
  • Chemical basis for the large free energy change associated with A T P hydrolysis
  • Hydrolysis of phosphoenolpyruvate (P E P)
  • Hydrolysis of acetyl-coenzyme A.
  • A T P can be attacked by nucleophiles at three separate positions
  • A T P produces reactive intermediates
  • N A D (P) as a redox cofactor
  • F A D and F M N as redox cofactors
  • The E. coli metabolome
  • Factors affecting the activity of enzymes
  • Protein phosphorylation and dephosphorylation
  • Glycolysis, fermentation, the pentose phosphate pathway, and glycogen synthesis
  • An overview of glycolysis
  • Preparatory phase of glycolysis
  • Payoff phase of glycolysis.
  • Glycolysis
  • Figure 14.3 The chemical reactions of the preparatory phase of glycolysis
  • Preparatory phase of glycolysis
  • Structure of sedoheptulose-7-phosphate
  • Chemical reactions in the payoff phase of glycolysis
  • Pay off phase of glycolysis
  • Enzymatic reaction mechanism of enolase, where 2-phosphoglycerate is converted into phosphoenolpyruvate
  • Glycolysis
  • Feeder pathways for glycolysis
  • Fermentation process
  • Production of N A D H in glycolysis
  • Ethanol fermentation
  • Lactic acid fermentation occurs in tissues that lack sufficient oxygen
  • Detection of cancerous tissue by positron emission tomography (P E T)
  • Pentose phosphate pathway
  • Overview of the pentose phosphate pathway
  • The oxidative phase of the pentose phosphate pathway
  • Nonoxidative reactions of the pentose phosphate pathway
  • Reactive oxygen species
  • Glycogen
  • Glycogen granuleas in a hepatocyte
  • Structure of a glycogen beta-granule
  • Structure of U D P-glucose
  • Glycogen synthesis.
  • Glucogenesis
  • Many different precursors are converted into carbohydrates
  • An overview of gluconeogenesis
  • The glycolysis and glycolytic pathways share some but not all steps
  • Role of biotin in the pyruvate carboxylase reaction
  • Synthesis of phosphoenolpyruvate from oxaloacetate by P E P carboxykinase
  • Glycolysis and glucogenesis
  • A futile metabolic cycle
  • Comparison of the kinetic properties of liver hexokinase Roman numeral 4 and hexokinase Roman numeral 1
  • Phosphofructokinase-1 (P F K-1) and its regulation
  • Regulation of P F K-1 and F B Pase-1
  • Fructose 2,6-bisphosphate structure
  • Fructose 2,6-bisphosphate (F 26 B P) has opposite effects on the enzymatic activities of P F K-1 and F B Pase-1
  • Figure 15.12 Regulation of fructose 2,6-bisphosphate level
  • Glycolysis and glucogenesis
  • Overview of glycogenesis and glycogenolysis and their regulation by hormones
  • Removal of a glucose residue from the nonreducing end of a glycogen chain by glycogen phosphorylase
  • Glycogen breakdown near an (alpha 1 forward arrow 6) branch point
  • The phosphoglucomutase reaction
  • Regulation of muscle glycogen phosphorylase
  • Regulation of liver glycogen phosphorylase
  • Regulation of carbohydrate metabolism in the liver
  • Difference in the regulation of carbohydrate metabolism in liver and muscle
  • Metabolic pathways within a mitochondrion
  • Catabolism of proteins, fats, and carbohydrates in cellular respiration
  • Formation of C O 2 in the citric acid cycle
  • The conversion of pyruvate to acetyl C o A
  • Overall reaction catalyzed by the pyruvate dehydrogenase complex
  • Coenzyme A
  • Reactions of the pyruvate dehydrogenase complex
  • The oxidized, reduced, and acetylated forms of lipoate
  • Regulation of pyruvate dehydrogenase
  • Citric acid cycle
  • Citric acid cycle overview
  • Citric acid cycle
  • Formation of citrate
  • Citric acid cycle
  • Decarboxylation facilitated by a carbonyl group
  • Formation of isocitrate
  • Citric acid cycle
  • Citric acid cycle
  • Formation of succinyl-Co A
  • Repeating patterns in biochemistry, example 1
  • Citric acid cycle
  • Formation of succinate
  • Reaction sequence for succinyl-CoA synthetase
  • Citric acid cycle
  • Repeating patterns in biochemistry: example 2
  • Products of the citric acid cycle
  • Citric acid cycle: fate of the carbons of acetyl-C o A
  • Regulation sites in the citric acid cycle
  • Citric acid cycle connections with anabolic (biosynthetic) reaction pathways
  • Cofactors that feature long flexible molecular arms
  • The malate-aspartate shuttle moves reducing equivalents into the mitochondria to provide N A D H
  • Noncanonical citric acid cycle shuttle
  • Formation of alpha ketoglutarate
  • Lipid anabolism and catabolism
  • The acetyl-Co A carboxylase reaction
  • The synthesis of a fatty acid
  • Regulation of fatty acid synthesis
  • Biosynthesis of phosphatidic acid
  • Phosphatidic acid in lipid biosynthesis
  • Regulation of triacylglycerol storage between the adipose tissue and the liver in fed and fasted states
  • Cholesterol structure
  • Cholesterol biosynthesis
  • Formation of mevalonate from acetyl-Co A
  • Regulation of cholesterol formation balances synthesis with dietary uptake and energy state
  • Statins mimic the structure of mevalonate
  • Metabolic fates of cholesterol
  • Lipoprotein particles
  • Lipoproteins and lipid transport
  • Uptake of cholesterol by receptor mediated endocytosis
  • Formation of plaques
  • Mobilization of free fatty acids from triacylglycerol
  • Activation of a fatty acid by conversion to a fatty acyl–Co A
  • Fatty acid entry into the mitochondria
  • Stages of fatty acid oxidation
  • Greek letter beta oxidation pathway
  • Coordinated regulation of fatty acid synthesis and breakdown
  • Formation of ketone bodies from acetyl- Co A
  • Ketone body production and export from the liver
  • Ketones as fuel
  • Lipid anabolism and catabolism
  • Amino acid and nitrogen metabolism
  • Metabolic pathways
  • Marine dead zones
  • The global nitrogen web
  • Nitrogen fixation
  • Structure of gamma glutamyl phosphate
  • Transamination of amino acids
  • Pyridoxal phosphate (vitamin B 6)
  • Nitrogen paths from tissues to liver
  • Metabolic pathways
  • Glutamate, glutamine, and the urea cycle
  • Formation of L-glutamate
  • The reaction catalyzed by glutamate dehydrogenase
  • The urea cycle
  • The reaction of carbamoyl phosphate synthetase
  • Overview of the catabolism of carbon skeletons derived from amino acids
  • Cofactors important in one-carbon transfer reactions
  • Tetrahydrofolate (folate or B 9) in one-carbon metabolism at different oxidation states
  • Synthetic cycle for S-adenosylmethionine
  • Diseases associated with degradation of phenylalanine and tyrosine
  • The first two steps in the catabolism of branched-chain amino acids
  • Metabolic pathways
  • Overview of amino acid biosynthesis
  • Proline biosynthesis
  • The first few steps of arginine biosynthesis parallel those in proline biosynthesis
  • Metabolic pathways
  • Biosynthesis of heme in vertebrates
  • Amino acid decarboxylation catalyzed by pyridoxal phosphate
  • The generation of biological amines from amino acids
  • Biosynthesis of glutathione from amino acids
  • Metabolic pathways
  • Formation of P R P P
  • Synthesis of pyrimidine nucleotides
  • Biosynthesis of purine nucleotides
  • Ribonucleotide reductase
  • Thymidylate synthesis pathway
  • Oxidative phosphorylation
  • A T P synthesis in mitochondria
  • Anatomy of a mitochondrion
  • 4 Ubiquinone (Q, or coenzyme Q)
  • Prosthetic groups of cytochromes
  • Iron-sulfur protein centers
  • Paths of electron transfer to ubiquinone in the electron transport chain
  • Complex Roman numeral 1 (N A D H:ubiquinone oxidoreductase)
  • Complex Roman numeral 2 (succinate dehydrogenase)
  • Complex Roman numeral 3 of the respiratory chain (cytochrome b c subscript 1 complex or ubiquinone: cytochrome c oxidoreductase)
  • Cytochrome c
  • Complex Roman numeral 4 (cytochrome oxidase)
  • Electron movement through respiratory pathways
  • A respirasome composed of complexes Roman numeral 1, Roman numeral 2, and Roman numeral 4
  • R O S formation in mitochondria and mitochondrial defenses
  • Chemiosmotic model
  • Coupling of electron transfer and A T P synthesis in mitochondria
  • Mitochondrial ATP synthase complex
  • Binding-change model for A T P synthase
  • N A D H shuttle systems
  • Two mechanisms of thermogenesis in mitochondria
  • Structure of bovine F subscript 1 end subscript-A T Pase in a complex with its regulatory protein I F subscript 1 end subscript
  • Regulation of gene expression by hypoxia-inducible factor (HIF-1) to reduce ROS formation
  • Regulation of A T P-producing pathways
  • Heteroplasmy in mitochondrial genomes
  • Coordination and division of carbohydrate and lipid catabolism in fasting and feeding
  • Signaling by the neuroendocrine system
  • General mechanisms of hormone action
  • Structure of norepinephrine
  • Structure of oxytocin
  • Structure of prostaglandin
  • Representation of human growth hormone
  • Structures of testosterone and progesterone
  • Insulin
  • The endocrine system of the pancreas
  • Regulation of insulin secretion in β cells
  • Blood glucose range in humans
  • Specialized metabolic functions of mammalian tissues
  • Figure 20.9 Plasma concentrations of fatty acids, glucose, and ketone bodies during six weeks of starvation
  • Liver processing of circulating metabolites in the fed state
  • Glucose uptake in the liver is regulated by hexokinase IV
  • White adipocyte
  • Energy sources for muscle contraction
  • Addition of phosphocreatine and A D P
  • Metabolic cooperation between skeletal muscle and liver: the Cori cycle
  • Set point theory for maintaining body weight
  • Hypothalamic regulation of food intake and energy expenditure
  • Hormones that control eating
  • Adipokine regulation of numerous tissues
  • Production of adiponectin and its actions through A M P K
  • Regulation of feeding behavior by hormones produced throughout the body
  • Eukaryotic cell
  • Structure of three molecules
  • Five compounds
  • Structure of a 6-membered heterocyclic hexagonal ring
  • Two sets of reactants
  • Common functional groups in biomolecules
  • Free energy versus reaction coordinate
  • Eukaryotic cell
  • Bacterial cell features
  • Structure of three molecules
  • Five compounds grouped as electrophiles and nucleophiles
  • Structure of a 6-membered heterocyclic hexagonal ring with two structural errors
  • Two sets of reactants
  • Common functional groups in biomolecules
  • Energy versus reaction progress
  • Three ionization states of the amino acid histidine with its three ionizable functional groups
  • Amino acid
  • Structure of isoleucine
  • Structures of compounds labeled from a through j
  • Structure of a glutathione molecule
  • Rate versus amount of enzyme solution
  • Structure of three amino acids
  • Two representations of a signature sequence
  • Three ionization states of the amino acid histidine with its three ionizable functional groups
  • Rectangular electrophoresis gel
  • Rectangular electrophoresis gel
  • Rectangular electrophoresis gel
  • Tertiary structure of a protein segment
  • Structures of two side chains
  • Structures of two side chains
  • Ribbon diagram of a zinc metallo-beta-lactamase protein
  • Seven different conformations of molecules
  • Theta versus concentration of L.
  • Y versus p O 2
  • Five catalysts
  • Concentration of Y versus time
  • Five catalysts
  • Concentration of Y versus time
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Common disaccharides
  • Structures of sugars A and B
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Formation of a Haworth projection by cyclization
  • Glucose homopolymer structures
  • Structure of a pentasaccharide
  • Structure of an oligosaccharide
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Fischer projection structure of a compound
  • Formation of a Haworth projection by cyclization
  • Lipid molecule
  • Lipid molecule
  • Three lipid molecules
  • Section of a lipid bilayer
  • Section of a lipid bilayer
  • Section of a lipid bilayer
  • Section of a lipid bilayer
  • Section of a lipid bilayer
  • Membrane proteins can be integral, peripheral, or lipid-anchored
  • Section of a lipid bilayer
  • Membrane proteins can be integral, peripheral, or lipid-anchored
  • Structures of bases, nucleosides, or nucleotides
  • Structures of bases, nucleosides, or nucleotides
  • Structure of a compound
  • Structure of a compound
  • Structure of a compound
  • Structure of a dinucleotide
  • Process of D N A replication, highlighting the key components and their roles
  • Structure of a D N A double helix
  • Structure of 5-methylcytosine
  • Genetic sequence
  • Genetic sequence
  • Genetic sequence
  • Genetic sequence
  • Types of gene expression
  • Structure of isopropyl-beta-D-thiogalactoside (I P T G)
  • Process of D N A replication, focusing on the leading and lagging strands at the replication fork
  • Formation of thymine from 5-methylcytosine
  • Types of gene expression
  • Formation of an aminoacyl-A M P product from glycine and A T P
  • Reaction of aminoacyl-A M P and the terminal adenylate of t R N A to produce an aminoacyl-t R N A
  • t R N A molecule in its cloverleaf secondary structure
  • Structure of a prokaryotic ribosome
  • Translation process within a ribosome
  • Enzymatic steps involved in ubiquitination, a process where ubiquitin molecules are attached to a target protein
  • Transcription and translation processes
  • Transcription and translation processes
  • Chemical reaction involved in nucleotide activation
  • Chemical reaction involved in nucleotide activation
  • t R N A molecule in its cloverleaf secondary structure
  • Structure of a prokaryotic ribosome, labeled "70 S."
  • Translation process within a ribosome
  • Enzymatic steps involved in ubiquitination, a process where ubiquitin molecules are attached to a target protein
  • Transcription and translation processes
  • Transcription and translation processes
  • Gel electrophoresis result with four labeled lanes (1 through 4)
  • Modified cytidine nucleotide triphosphate
  • Modified cytidine nucleotide triphosphate
  • Modified cytidine nucleotide triphosphate
  • D N A sequence
  • Site-specific recombination in a species of ciliated protist
  • Two complementary D N A strands with partial sequences
  • Two complementary D N A strands with partial sequences
  • Two complementary D N A strands with partial sequences
  • Two complementary D N A strands with partial sequences
  • Constructed italics E. coli end italics plasmid lowercase p uppercase B uppercase R 322
  • Rectangular electrophoresis gel
  • Short tandem repeat (S T R) patterns across three loci for multiple individuals
  • Variable number tandem repeat (V N T R) patterns across multiple individuals
  • Gel electrophoresis result with four labeled lanes (1 through 4)
  • Two complementary D N A strands with partial sequences
  • Two complementary D N A strands with partial sequences
  • Two complementary D N A strands with partial sequences
  • Two complementary D N A strands with partial sequences
  • Two starting materials of aldol condensation
  • Structure of glucose 6-phosphate and the product of its isomerization by phosphohexose isomerase, fructose 6-phosphate
  • Forward reaction
  • Irreversible reaction
  • Irreversible reaction
  • Glycolysis pathway
  • Biochemical process of glycogen synthesis from glucose
  • Glycolysis pathway
  • Glycolysis pathway
  • Pathways of gluconeogenesis and glycolysis, starting from reactant and progressing toward product in gluconeogenesis
  • P F K-1 activity versus concentration of A T P
  • Structure of pyruvate and the product of a reaction catalyzed by lactate dehydrogenase, L- lactate
  • V subscript 0 over V subscript max over glucose concentration in millimolar
  • Interconnected pathways of glycolysis and gluconeogenesis
  • Pathways of gluconeogenesis and glycolysis, starting from pyruvate and progressing toward glucose in gluconeogenesis
  • Citric acid cycle
  • Structure of isocitrate
  • Structures of 5 compounds
  • Metabolic transformations labeled from (a) through (d)
  • Metabolic transformations labeled from (e) through (h)
  • Metabolic transformations labeled from (a) through (d)
  • Metabolic transformations labeled from (e) through (h)
  • Stepwise breakdown of isoleucine into propionyl-Co A and acetyl-Co A through six enzymatic steps
  • Stepwise breakdown of isoleucine into propionyl-Co A and acetyl-Co A through six enzymatic steps
  • Biosynthesis of proline from glutamate, showing a stepwise process through several intermediates
  • Structure of quinonoid intermediate
  • Structure of Schiff base intermediate (external aldimine)
  • Formation of glutamate and oxaloacetate by the enzyme transaminase
  • Biosynthesis of proline from glutamate, showing the stepwise enzymatic reactions and molecular intermediates involved
  • Structure of C-14 labeled orotate
  • Electron transport chain within the inner mitochondrial membrane, represented as an oval-shaped double membrane structure
  • Structures of [4- superscript 3 end superscript H] N A D H and [7- superscript 14 end superscript C] N A D H
  • Structures of ethylamine and phosphorylated ethanol
  • Structure of aspirin
  • Structure of urushiol
  • p H versus O H superscript minus equivalents
  • Stained S D S polyacrylamide gel showing the results of electrophoresis
  • Protein structure
  • Ramachandran plot
  • Ramachandran plot
  • Resonance structures
  • Binding of oxygen to fractional saturation
  • Fractional saturation against the p O subscript 2 in torr
  • p H dependence to activity in percent of maximal
  • Two sigmoid curves
  • d-glucose and d-mannose
  • Structure of alpha-d-glucosyl (1 to 6) d-mannosamine
  • Haworth structure of gentiobiose
  • Structure of a tetranucleotide
  • Structure of molecule A
  • Structure of molecule B
  • Structure of molecule C
  • Interaction between two nucleotides labeled d N a M-d T P T 3
  • Constructed plasmid labeled lowercase p uppercase S uppercase A uppercase P
  • Two D N A strands
  • Gel electrophoresis result with four labeled lanes (1 through 4)
  • Constructed plasmid labeled lowercase p uppercase S uppercase A uppercase P
  • Palmitoyl- C o A and trans-delta squared-enoyl- C o A
  • Structure of L-Leucine and D-Leucine
  • Structure of glucose and fructose
  • Structures of glycerol and glycerol 3-phosphate
  • Structures of glycylalanine, glycine, and alanine
  • Structures of glycerol and dihydroxyacetone
  • Structures of acetaldehyde and acetic acid
  • Structure of phosphoarginine
  • Reaction of Acetyl C o A
  • 4-carbon alkane chain
  • 3-carbon alkane chain
  • 5-carbon alkane chain
  • 5-carbon alkane chain
  • Hydrolysis Reaction
  • Enzymatic removal of the terminal glucose residue by glycogen phosphorylase
  • Metabolic pathway for the conversion of [C superscript 14] bicarbonate into glucose through a series of intermediates
  • Metabolic pathway for the conversion of [1-C superscript 14] pyruvate into glucose through a series of intermediates
  • Enzymatic removal of the terminal glucose residue by glycogen phosphorylase
  • Metabolic pathway for the conversion of [C superscript 14] bicarbonate into glucose through a series of intermediates
  • Metabolic pathway for the conversion of [1-C superscript 14] pyruvate into glucose through a series of intermediates
  • Citric acid cycle (Krebs cycle), showing the sequence of reactions involving acetyl-Co A and various intermediate metabolites
  • Citric acid cycle (Krebs cycle), showing the sequence of reactions involving acetyl-Co A and various intermediate metabolites
  • Formation of oxaloacetate
  • Multi-enzyme complex mechanism of pyruvate dehydrogenase (P D H), which catalyzes the conversion of pyruvate into acetyl-Co A
  • Structure of a compound
  • Citric acid cycle (Krebs cycle), showing the sequence of reactions involving acetyl-Co A and various intermediate metabolites
  • 2 minus H superscript 2 Acetyl- C o A
  • Oxygen concentration versus time with N A D H and Rotenone
  • Oxygen concentration versus time with N A D H, Rotenone, and Succinate
  • Oxygen concentration versus time with N A D H, Cyanide, and Succinate
  • Amino acid sequences of human oxytocin and human vasopressin
  • Back Cover page
  • Back Cover