Produktbild: Lehninger Biochemistry: Core Concepts and Applications

Lehninger Biochemistry: Core Concepts and Applications

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Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

15.04.2025

Verlag

Macmillan Learning

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720

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27,4/21,5/2,5 cm

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1448 g

Sprache

Englisch

ISBN

978-1-319-58996-7

Beschreibung

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

15.04.2025

Verlag

Macmillan Learning

Seitenzahl

720

Maße (L/B/H)

27,4/21,5/2,5 cm

Gewicht

1448 g

Sprache

Englisch

ISBN

978-1-319-58996-7

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Libri GmbH
Europaallee 1
36244 Bad Hersfeld
DE

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  • Produktbild: Lehninger Biochemistry: Core Concepts and Applications
  • 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 the 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


    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
    • Phosphate and Bicarbonate Are Important Biological Buffer Systems Untreated Diabetes Produces Life-Threatening Acidosis

    Chapter 3: Amino Acids, Peptides, and Proteins

    3.1 Amino Acids

    • What is an Amino Acid?
    • The Amino Acid Residues 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

    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 ¿ Helix Maximizes the Use of Polypeptide Hydrogen Bonds
    • The ß 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 b-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

    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 Protein to a Ligand: 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 Protein to a Ligand: 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

    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

    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

    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

    Chapter 8: Lipids, Membranes, and Membrane Proteins

    8.1 Membrane Lipids

    • Fatty Acids are the Hydrocarbon Chain of Membrane Lipids
    • Fatty Acid Composition of Lipids Impacts Health
    • Structural Elements Determine Membrane Classes
    • Membranes 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 in 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 Phosphoryl- Group Transfer from ATP
    • Ion Channels Allow Rapid Movement of Ions Across Membranes

    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?

    Chapter 10: Biological Information Part 1: DNA and RNA Metabolism

    10.1 DNA Replication

    • DNA Replication Follows a Set of Rules
    • DNA Polymerases Synthesizes 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 Synthesizes RNA
    • RNA Replication Requires Many Enzymes and Protein Factors
    • RNA Syntheses 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

    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

    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 Copying the RNA to DNA with Reverse Transcriptase

    12.2 Altering Genomic Information

    • Joining DNA Segments from Different Sources Yields Recombinant DNA Segments Can be Joined Without Using Restriction Enzymes
    • Cloned DNA Can be Altered to Study Genes and Proteins
    • CRISPR/Cas Systems Allows 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

    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 High Energy Phosphodiester 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 Adenyl 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

    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 3-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 Anaerobic 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

    Chapter 15: Carbohydrate Metabolism Part 2: Gluconeogenesis and Glycogen Degradation

    15.1 Gluconeogenesis

    • Gluconeogenesis and Glycolysis Share Many But Not All Steps and Enzymes
    • Glycolysis 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 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

    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 Multi-stage 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 Non-canonical Citric Acid Cycle
    • Vitamin Deficiencies Result in Disease
    • Amino Acid Substitutions in Isocitrate Dehydrogenase Facilitate Tumor Growth

    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
    • Regulation of Fatty Acid Oxidation By Compartmentalization
    • Ketone Body are Formed in the Liver and Exported to Other Tissues
    • Ketone Bodies Are Overproduced in Diabetes and Starvation

    Chapter 18: Amino Acid Catabolism and Anabolism

    18.1 The Worldwide Nitrogen Web and its Many Interfaces With Living Systems

    • The 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
    • 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

    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
    • Chemiosmotic Coupling Allows Nonintegral Stoichiometries of 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

    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 Feeding
    • The Liver Produces Ketone Bodies to Fuel Perip