Biochemistry:
Gespeichert in:
Hauptverfasser: | , , |
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Format: | Buch |
Sprache: | English |
Veröffentlicht: |
New York
Freeman [u.a.]
2012
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Ausgabe: | Internat. 7. ed. |
Schlagworte: | |
Online-Zugang: | Inhaltsverzeichnis |
Beschreibung: | Hier auch später erschienene, unveränderte Nachdrucke. - Erg. bildet: Student companion to accompany Biochemistry |
Beschreibung: | Getr. Zählung zahlr. Ill., graph. Darst. |
ISBN: | 9781429276351 1429276355 |
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245 | 1 | 0 | |a Biochemistry |c Jeremy M. Berg ; John L. Tymoczko ; Lubert Stryer |
250 | |a Internat. 7. ed. | ||
264 | 1 | |a New York |b Freeman [u.a.] |c 2012 | |
300 | |a Getr. Zählung |b zahlr. Ill., graph. Darst. | ||
336 | |b txt |2 rdacontent | ||
337 | |b n |2 rdamedia | ||
338 | |b nc |2 rdacarrier | ||
500 | |a Hier auch später erschienene, unveränderte Nachdrucke. - Erg. bildet: Student companion to accompany Biochemistry | ||
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Datensatz im Suchindex
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adam_text |
BRIEF CONTENTS
Part I THE MOLECULAR DESIGN OF LIFE
1
Biochemistry: An Evolving Science
1
2
Protein Composition and Structure
25
3
Exploring Proteins and Proteomes
67
4
DNA RNA
and the Flow of Genetic Information
113
5
Exploring Genes and Genomes
145
6
Exploring Evolution and Bioinformatics
181
7
Hemoglobin: Portrait of a Protein in Action
203
8
Enzymes: Basic Concepts and Kinetics
227
9
Catalytic Strategies
261
10
Regulatory Strategies
299
11
Carbohydrates
329
12
Lipids and Cell Membranes
357
13
Membrane Channels and Pumps
383
14
Signal-Transduction Pathways
415
Part I! TRANSDUCING AND STORING ENERGY
15
Metabolism: Basic Concepts and Design
443
16
Glycolysis and Gluconeogenesis
469
17
The Citric Acid Cycle
515
18
Oxidative Phosphorylation
543
19
The Light Reactions of Photosynthesis
585
20
The Calvin Cycle and the Pentose Phosphate
Pathway
609
21
Glycogen Metabolism
637
22
Fatty Acid Metabolism
663
23
Protein Turnover and
Amino
Acid Catabolism
697
Part I» SYNTHESIZING THE MOLECULES OF LIFE
24
The Biosynthesis of
Amino
Acids
729
25
Nucleotide Biosynthesis
761
26
The Biosynthesis of Membrane Lipids and
Steroids
787
27
The Integration of Metabolism
821
28 DNA
Replication, Repair, and Recombination
849
29
RNA
Synthesis and Processing
883
30
Protein Synthesis
921
31
The Control of Gene Expression in Prokaryotes
957
32
The Control of Gene Expression in Eukaryotes
973
Part IV RESPONDING TO ENVIRONMENTAL CHANGES
33
Sensory Systems
995
34
The Immune System
1017
35
Molecular Motors
1049
36
Drug Development
1073
CONTENTS
Preface
Part I THE MOLECULAR DESIGN OF LIFE
Chapter l Biochemistry: An Evolving Science
1.1
Biochemical Unity Underlies
Biological Diversity
1.2 DNA
Illustrates the Interplay Between
Form and Function
DNA
is constructed from four building blocks
Two single strands of
DNA
combine to form a
double helix
DMA structure explains heredity and the storage
of information
1.3
Concepts from Chemistry Explain the
Properties of Biological Molecules
The double helix can form from its component strands
Covalent and noncovalent bonds are important for the
structure and stability of biological molecules
The double helix is an expression of the rules
of chemistry
The laws of thermodynamics govern the behavior of
biochemical systems
Heat is released in the formation of the double helix
Acid base reactions are central in many biochemical
processes
Acid base reactions can disrupt the double helix
Buffers regulate
pH
in organisms and in the laboratory
1.4
The Genomic Revolution Is Transforming
Biochemistry and Medicine
The sequencing of the human genome is a landmark
in human history
Genome sequences encode proteins and patterns of
expression
Individuality depends on the interplay between genes
and environment
APPENDIX: Visualizing Molecular Structures I:
Small Molecules
4
4
6
6
10
11
12
1Л
14
15
17
17
18
19
21
Chapter
2
Protein Composition and Structure
25
2.1
Proteins Are Built from a Repertoire of
20
Amino
Acids
27
2.2
Primary Structure:
Amino
Acids Are Linked by
Peptide
Bonds to Form Polypeptide Chains
33
Proteins have unique
amino
acid sequences specified
by genes
35
Polypeptide chains are flexible yet conformationally
restricted
36
xvi Contents
2.3
Secondary Structure: Polypeptide Chains Can
Fold into Regular Structures Such As the Alpha
Helix, the Beta Sheet, and Turns and Loops
The alpha helix is a coiled structure stabilized
by intrachain hydrogen bonds
Beta sheets are stabilized by hydrogen bonding between
polypeptide strands
Polypeptide chains can change direction by
making reverse turns and loops
Fibrous proteins provide structural support for
cells and tissues
2.4
Tertiary Structure: Water-Soluble Proteins
Fold into Compact Structures with
Nonpolar
Cores
2.5
Quaternary Structure: Polypeptide Chains
Can Assemble into Multisubunit Structures
2.6
The
Amino
Acid Sequence of a Protein
Determines Its Three-Dimensional Structure
Amino
acids have different propensities for
forming alpha helices, beta sheets, and beta turns
Protein folding is a highly cooperative process
Proteins fold by progressive stabilization of
intermediates rather than by random search
Prediction of three-dimensional structure from
sequence remains a great challenge
Some proteins are inherently unstructured and
can exist in multiple conformations
Protein misfolding and aggregation are associated
with some neurological diseases
Protein modification and cleavage confer
new capabilities
APPENDIX: Visualizing Molecular Structures II: Proteins
38
38
40
42
43
45
48
49
50
52
52
54
54
55
57
60
Chapter
3
Exploring Proteins and Proteomes
67
The proteome is the functional representation of
the genome
68
3.1
The Purification of Proteins Is an Essential
First Step in Understanding Their Function
68
The assay: How do we recognize the protein
that we are looking for?
69
Proteins must be released from the cell to be purified
69
Proteins can be purified according to solubility, size,
charge, and binding affinity
70
Proteins can be separated by gel electrophoresis and
displayed
73
A protein purification scheme can be quantitatively
evaluated
77
Ultracentrifugation is valuable for separating
biomolecules and determining their masses
78
Protein purification can be made easier with the use
of
recombinam DX
A tedhnoloçv
80
3.2
Amino
Acid Sequences of Proteins Can
Be Determined Experimentally
Peptide
sequences can be determined by automated
Edman
degradation
Proteins can be specifically cleaved into small
peptides to facilitate analysis
Genomic and proteomic methods are complementary
3.3
Immunology Provides Important Techniques
with Which to Investigate Proteins
Antibodies to specific proteins can be generated
Monoclonal antibodies with virtually any
desired specificity can be readily prepared
Proteins can be detected and quantified by using an
enzyme-linked immunosorbent assay
Western blotting permits the detection of
proteins separated by gel electrophoresis
Fluorescent markers make the visualization of
proteins in the cell possible
3.4
Mass Spectrometry Is a Powerful Technique
for the Identification of Peptides and Proteins
The mass of a protein can be precisely determined
by mass spectrometry
Peptides can be sequenced by mass spectrometry
Individual proteins can be identified by
mass spectrometry
3.5
Peptides Can Be Synthesized by
Automated Solid-Phase Methods
3.6
Three-Dimensional Protein Structure
Can Be Determined by X-ray Crystallography
and NMR Spectroscopy
X-ray crystallography reveals three-dimensional
structure in atomic detail
Nuclear magnetic resonance spectroscopy can reveal
the structures of proteins in solution
81
82
84
86
86
86
Chapter
4
DNA, RNA,
and the Flow of
Information
90
91
92
93
93
95
96
97
100
100
103
113
4.1
A Nucleic Acid Consists of Four Kinds of
Bases Linked to a Sugar-Phosphate Backbone
114
RNA
and
DNA
differ in the sugar component and
one of the bases
114
Nucleotides are the monomeric units of nucleic acids
115
DNA
molecules are very long
117
4.2
A Pair of Nucleic Acid Chains with
Complementary Sequences Can Form a
Double-Helical Structure
117
The double helix is stabilized by hydrogen bonds and
van
der Waals
interactions
117
DNA
can assume a variety of structural forms
119
Z-DNA is a left-handed double helix in which
backbone phosphates zigzag
120
Contents xvii
Some
DNA
molecules are circular and supercoiled
Single-stranded nucleic acids can adopt
elaborate structures
4.3
The Double Helix Facilitates the Accurate
Transmission of Hereditary Information
Differences in
DNA
density established the validity
of the semiconservative-replication hypothesis
The double helix can be reversibly melted
4.4 DNA
Is Replicated by Polymerases
That Take Instructions from Templates
DNA polymerase
catalyzes phosphodiester-bridge
formation
The genes of some viruses are made of
RNA
4.5
Gene Expression Is the Transformation of
DNA
Information into Functional Molecules
Several kinds of
RNA
play key roles in gene expression
All cellular
RNA
is synthesized by
RNA
polymerases
RNA
polymerases take instructions from
DNA
templates
Transcription begins near promoter sites and ends at
terminator sites
Transfer RNAs are the adaptor molecules in protein
synthesis
4.6
Amino
Acids Are Encoded by Groups of
Three Bases Starting from a Fixed Point
Major features of the genetic code
Messenger
RNA
contains start and stop signals for
protein synthesis
The genetic code is nearly universal
4.7
Most Eukaryotic Genes Are Mosaics of
Introns
and Exons
RNA
processing generates mature
RNA
Many exons encode protein domains
121
121
122
123
124
125
125
126
127
127
128
130
130
131
132
1
ЗЛ
134
135
135
136
137
Chapter
5
Exploring Genes and Genomes
145
5.1
The Exploration of Genes Relies on
Key Tools
146
Restriction enzymes split
DNA
into specific fragments
147
Restriction fragments can be separated by gel
electrophoresis and visualized
147
DNA
can be sequenced by controlled termination of
replication
149
DNA
probes and genes can be synthesized by
automated solid-phase methods
150
Selected
DNA
sequences can be greatly amplified
by the polymerase chain reaction
151
PCR is a powerful technique in medical diagnostics.
forensics, and studies of
molecuîar évolution
152
The tools for
recombinant
DNA
technology
have been used to identify disease-causing
mutations
153
5.2
Recombinant
DNA
Technology Has
Revolutionized All Aspects of Biology
Restriction enzymes and
DNA
ligase
are key tools in
forming
recombinant
DNA
molecules
Plasmids and lambda phage are choice vectors for
DNA
cloning in bacteria
Bacterial and yeast artificial chromosomes
Specific genes can be cloned from digests of
genomicDNA
Complementary
DNA
prepared from mRNA can be
expressed in host cells
Proteins with new functions can be created through
directed changes in
DNA
Recombinant
methods enable the exploration of the
functional effects of disease-causing mutations
5.3
Complete Genomes Have Been
Sequenced and Analyzed
The genomes of organisms ranging from bacteria to
multicellular eukaryotes have been sequenced
The sequencing of the human genome has
been finished
Next-generation sequencing methods enable the rapid
determination of a whole genome sequence
Comparative genomics has become a powerful
research tool
5.4
Eukaryotic Genes Can Be
Quantitated
and
Manipulated with Considerable Precision
Gene-expression levels can be comprehensively
examined
New genes inserted into eukaryotic cells can be
efficiently expressed
Transgenic animals harbor and express genes
introduced into their germ lines
Gene disruption provides clues to gene function
RNA
interference provides an additional tool for
disrupting gene expression
Tumor-inducing plasmids can be used to introduce
new genes into plant cells
Human gene therapy holds great promise for medicine
Chapter
6
Exploring Evolution and
Bioinformatics
6.2
Statistical Analysis of Sequence
Alignments Can Detect Homoiogy
The statistical significance of alignments can be
estimated by shuffling
Distant
evolutionär}"
relationships can be detected
through the use of substitution matrices
Databases can be searched to identify homologous
sequences
154
154
155
157
157
160
162
163
163
164
165
166
166
167
167
169
170
170
171
172
173
181
6.1
Homologs Are Descended from a
Common Ancestor
182
Î83
185
186
189
xvi
і і
Contents
6.3
Examination of Three-Dimensional
Structure Enhances Our Understanding of
Evolutionary Relationships
190
Tertiary structure is more conserved than primary
structure
191
Knowledge of three-dimensional structures can
aid in the evaluation of sequence alignments
192
Repeated motifs can be detected by aligning
sequences with themselves
192
Convergent evolution illustrates common solutions
to biochemical challenges
193
Comparison of
RNA
sequences can be a source of
insight into
RNA
secondary structures
194
6.4
Evolutionary Trees Can Be Constructed
on the Basis of Sequence Information
195
6.5
Modern Techniques Make the Experimental
Exploration of Evolution Possible
196
Ancient
DNA
can sometimes be amplified
and sequenced
196
Molecular evolution can be examined experimentally
197
Additional globins are encoded in the human genome
219
APPENDIX: Binding Models Can Be Formulated in
Quantitative Terms: the Hill Plot and the Concerted Model
221
Chapter
7
Hemoglobin: Portrait of a
Protein in Action
203
7.1
Myoglobin and Hemoglobin Bind Oxygen
at Iron Atoms in
Heme
204
Changes in
heme
electronic structure upon oxygen
binding are the basis for functional imaging studies
205
The structure of myoglobin prevents the release of
reactive oxygen species
206
Human hemoglobin is an assembly of four
myoglobin-like subunits
207
7.2
Hemoglobin Binds Oxygen Cooperatively
207
Oxygen binding markedly changes the quaternary
structure of hemoglobin
209
Hemoglobin cooperativity can be potentially explained
by several models
210
Structural changes at the
heme
groups are
transmitted to the
otjßt-
αιβι
interface
212
2,3-Bisphosphoglycerate in red cells is crucial in
determining the oxygen affinity of hemoglobin
212
Carbon monoxide can disrupt oxygen transport by
hemoglobin
213
7.3
Hydrogen Ions and Carbon Dioxide Promote
the Release of Oxygen: The Bohr Effect
214
7.4
Mutations in Genes Encoding Hemoglobin
Subunits Can Result in Disease
216
Sickle-cell anemia results from the aggregation of
mutated deoxyhemoglobin molecules
217
Thalassemia is caused by an imbalanced production of
hemoglobin chains
218
The accumulation of free alpha-hemoglobin
chains is prevented
219
Chapter
8
Enzymes: Basic Concepts and
Kinetics
227
8.1
Enzymes Are Powerful and Highly
Specific Catalysts
228
Many enzymes require cofactors for activity
229
Enzymes can transform energy from one form
into another
229
8.2
Free Energy Is a Useful Thermodynamic
Function for Understanding Enzymes
230
The free-energy change provides information about
the spontaneity but not the rate of a reaction
230
The standard free-energy change of a reaction is
related to the equilibrium constant
231
Enzymes alter only the reaction rate and not the
reaction equilibrium
232
8.3
Enzymes Accelerate Reactions by Facilitating
the Formation of the Transition State
233
The formation of an enzyme—substrate complex is
the first step in enzymatic catalysis
234
The active sites of enzymes have some
common features
235
The binding energy between enzyme and substrate
is important for catalysis
237
8.4
The Michaelis-Menten Equation Describes
the Kinetic Properties of Many Enzymes
237
Kinetics is the study of reaction rates
237
The steady-state assumption facilitates a description
of enzyme kinetics
238
Variations in
Км
can have physiological consequences
240
Km and Vmax values can be determined by
several means
240
Км
and Vmax values are important enzyme
characteristics
241
^cat/^M
is a measure of catalytic efficiency
242
Most biochemical reactions include multiple substrates
243
Allosteric enzymes do not obey
Michaelis-Menten kinetics
245
8.5
Enzymes Can Be Inhibited by Specific
Molecules
246
Reversible inhibitors are kinetically distinguishable
247
Irreversible inhibitors can be used to map
the active site
249
Transition-state analogs are potent inhibitors
of enzymes
251
Catalytic antibodies demonstrate the importance of selective
binding of the transition state to enzymatic activity
251
Penicillin irreversibly inactivates a key enzyme in
bacterial cell-wall synthesis
252
Contents
χ ι χ
8.6
Enzymes Can Be Studied One Molecule
at a Time
APPENDIX: Enzymes are Classified on the Basis
of the Types of Reactions That They Catalyze
254
256
The altered conformation of myosin persists for a
substantial period of time
290
Myosins are a family of enzymes containing P-loop
structures
291
Chapter
9
Catalytic Strategies
A few basic catalytic principles are used by
many enzymes
262
9.1
Proteases Facilitate a Fundamentally
Difficult Reaction
263
Chymotrypsin possesses a highly reactive
serine
residue
263
Chymotrypsin action proceeds in two steps linked
by a covalently bound intermediate
264
Serine
is part of a catalytic triad that also includes
histidine and aspartate
265
Catalytic triads are found in other hydrolytic enzymes
268
The catalytic triad has been dissected by
site-directed mutagenesis
270
Cysteine, aspartyl,
and metalloproteases are other
major classes of peptide-cleaving enzymes
271
Protease inhibitors are important drugs
272
9.2
Carbonic Anhydrases Make a Fast
Reaction Faster
274
Carbonic anhydrase contains a bound zinc ion
essential for catalytic activity
275
Catalysis entails zinc activation of a water molecule
276
A proton shuttle facilitates rapid regeneration of
the active form of the enzyme
277
Convergent evolution has generated zinc-based
active sites in different carbonic anhydrases
279
9.3
Restriction Enzymes Catalyze Highly
Specific DNA-Cleavage Reactions
279
Cleavage is by in-line displacement of
3'
-oxygen
from phosphorus by magnesium-activated water
280
Restriction enzymes require magnesium for
catalytic activity
282
The complete catalytic apparatus is assembled
only within complexes of cognate
DNA
molecules,
ensuring specificity
283
Host-cell
DNA
is protected by the addition of methyl
groups to specific bases
285
Type II restriction enzymes have a catalytic core in
common and are probably related by horizontal
gene transfer
286
9.4
Myosins Harness Changes in Enzyme
Conformation to Couple ATP Hydrolysis to
Mechanical Work
287
ATP hydrolysis proceeds by the attack of water on
the gamma-phosphoryl group
287
Formation of the transition state for ATP hydrolysis
is associated with a substantial conformational change
288
Chapter
10
Regulatory Strategies
299
261
ЮЛ
Aspartate Transcarbamoylase Is Allosterically
Inhibited by the End Product of Its Pathway
Allosterically regulated enzymes do not follow
Michaelis-Menten kinetics
ATCase consists of separable catalytic and regulatory
subunits
Allosteric interactions in ATCase are mediated by large
changes in quaternary structure
Allosteric regulators modulate the
Τ
-to-
R
equilibrium
10.2
Isozymes Provide a Means of Regulation
Specific to Distinct Tissues and Developmental
Stages
10.3
Covalent Modification Is a Means of
Regulating Enzyme Activity
Kinases and phosphatases control the extent of protein
phosphorylation
Phosphorylation is a highly effective means of
regulating the activities of target proteins
Cyclic AMP activates protein kinase A by altering the
quaternary structure
ATP and the target protein bind to a deep cleft
in the catalytic subunit of protein kinase A
10.4
Many Enzymes Are Activated by Specific
Proteolytic Cleavage
Chymotrypsinogen is activated by specific cleavage
of a single
peptide
bond
Proteolytic activation of chymotrypsinogen leads
to the formation of a substrate-binding site
The generation of
trypsin
from trypsinogen leads
to the activation of other zymogens
Some proteolytic enzymes have specific inhibitors
Blood clotting is accomplished by a cascade of
zymogen activations
Fibrinogen is converted by thrombin into a
fibrin clot
Prothrombin is readied for activation by a vitamin
K-dependent modification
Hemophilia revealed an early step in clotting
The clotting process must be precisely regulated
Chapter
11
Carbohydrates
11.1
Monosaccharides Are the Simplest
Carbohydrates
Many common sugars exist in cyclic forms
Pyranose and furanose rings can assume different
conformations
300
301
301
302
305
306
307
308
310
311
312
312
313
314
315
316
317
318
320
321
321
329
330
332
334
xx Contents
Glucose
is a reducing sugar
Monosaccharides are joined to alcohols and
amines through glycosidic bonds
Phosphorylated sugars are key intermediates in
energy generation and biosyntheses
11.2
Monosaccharides Are Linked to Form
Complex Carbohydrates
Sucrose, lactose, and maltose are the common
disaccharides
Glycogen and starch are storage forms of glucose
Cellulose, a structural component of plants, is made
of chains of glucose
11.3
Carbohydrates Can Be Linked to Proteins
to Form Glycoproteins
Carbohydrates can be linked to proteins through
asparagine (N-linked) or through
serine
or
threonine (O-linked) residues
The glycoprotein erythropoietin is a vital hormone
Proteoglycans, composed of polysaccharides and
protein, have important structural roles
Proteoglycans are important components of cartilage
Mucins are glycoprotein components of mucus
Protein glycosylation takes place in the lumen of the
endoplasmic reticulum and in the Golgi complex
Specific enzymes are responsible for oligosaccharide
assembly
Blood groups are based on protein glycosylation
patterns
Errors in glycosylation can result in pathological
conditions
Oligosaccharides can be "sequenced"
11.4
Lectins Are Specific Carbohydrate-Binding
Proteins
Lectins promote interactions between cells
Lectins are organized into different classes
Influenza virus binds to sialic acid residues
Chapter
12
Lipids and Cell Membranes
335
336
336
337
337
338
338
339
340
340
341
342
343
343
345
345
346
346
347
348
348
349
357
Many common features underlie the diversity of
biological membranes
12.1
Fatty Acids Are Key Constituents of
Lipids
Fatty acid names are based on their parent hydrocarbons
Fatty acids vary in chain length and degree of
unsaturation
12.2
There Are Three Common Types of
Membrane Lipids
Phospholipids are the major class of membrane lipids
Membrane lipids can include carbohydrate moieties
Cholesterol is
a lipid
based on a steroid nucleus
Archaeal membranes are built from ether lipids with
branched chains
358
358
358
359
360
360
361
362
362
A membrane
lipid
is an amphipathic molecule
containing a hydrophilic and a hydrophobic moiety
12.3
Phospholipids and Glycolipids Readily
Form Bimolecular Sheets in Aqueous Media
Lipid
vesicles can be formed from phospholipids
Lipid bilayers
are highly impermeable to ions and
most polar molecules
12.4
Proteins Carry Out Most Membrane
Processes
Proteins associate with the
lipid
bilayer in a
variety of ways
Proteins interact with membranes in a variety
of ways
Some proteins associate with membranes through
covalently attached hydrophobic groups
Transmembrane
helices can be accurately
predicted from
amino
acid sequences
12.5
Lipids and Many Membrane Proteins
Diffuse Rapidly in the Plane of the
Membrane
The fluid mosaic model allows lateral movement
but not rotation through the membrane
Membrane fluidity is controlled by fatty acid
composition and cholesterol content
Lipid
rafts are highly dynamic complexes formed
between cholesterol and specific lipids
All biological membranes are asymmetric
12.6
Eukaryotic Cells Contain Compartments
Bounded by Internal Membranes
363
364
365
366
367
367
368
371
371
373
374
374
375
375
376
Chapter
13
Membrane Channels and Pumps
383
The expression of transporters largely defines the
metabolic activities of a given cell type
384
13.1
The Transport of Molecules Across a
Membrane May Be Active or Passive
384
Many molecules require protein transporters to
cross membranes
384
Free energy stored in concentration gradients can be
quantified
385
13.2
Two Families of Membrane Proteins
Use ATP Hydrolysis to Pump Ions and
Molecules Across Membranes
386
P-type ATPases couple phosphorylation and
conformational changes to pump calcium ions
across membranes
386
Digitalis specifically inhibits the Na+-K+ pump
by blocking its dephosphorylation
389
P-type ATPases are evolutionarily conserved and
play a wide range of roles
390
Multidrug resistance highlights a family of
membrane pumps with ATP-binding cassette
domains
390
Contents xxi
13.3
Lactose Permease
Is an Archetype of
Secondary Transporters That Use One
Concentration Gradient to Power the Formation
of Another
392
13.4
Specific Channels Can Rapidly Transport
Ions Across Membranes
394
Action potentials are mediated by transient changes
in Na+ and K+ permeability
394
Patch-clamp conductance measurements reveal
the activities of single channels
395
The structure of a potassium ion channel is an
archetype for many ion-channel structures
395
The structure of the potassium ion channel reveals
the basis of ion specificity
396
The structure of the potassium ion channel explains
its rapid rate of transport
399
Voltage gating requires substantial conformational
changes in specific ion-channel domains
399
A channel can be activated by occlusion of the pore:
the ball-and-chain model
400
The acetylcholine receptor is an archetype for
ligand-gated ion channels
401
Action potentials integrate the activities of several ion
channels working in concert
402
Disruption of ion channels by mutations or
chemicals can be potentially life threatening
404
13.5
Gap Junctions Allow Ions and Small
Molecules to Flow Between Communicating Cells
405
13.6
Specific Channels Increase the Permeability
of Some Membranes to Water
406
Insulin binding results in the cross-phosphorylation
and activation of the insulin receptor
426
The activated insulin-receptor kinase initiates a
kinase cascade
426
Insulin signaling is terminated by the action of
phosphatases
429
14.3
EGF Signaling: Signal-Transduction
Pathways Are Poised to Respond
429
EGF binding results in the dimerization of the
EGF receptor
429
The EGF receptor undergoes phosphorylation of
its carboxyl-terminal tail
431
EGF signaling leads to the activation of
Ras, a
small
G
protein
431
Activated
Ras
initiates a protein kinase cascade
432
EGF signaling is terminated by protein phosphatases
and the intrinsic GTPase activity of
Ras
432
14.4
Many Elements Recur with Variation
in Different Signal-Transduction
Pathways
433
14.5
Defects in Signal-Transduction
Pathways Can Lead to Cancer and Other
Diseases
434
Monoclonal antibodies can be used to inhibit
signal-transduction pathways activated in tumors
434
Protein kinase inhibitors can be effective anticancer
drugs
435
Cholera and whooping cough are due to altered
G
-protein activity
435
Chapter
14
Signal-Transduction Pathways
415
Signal transduction depends on molecular circuits
416
14.1
Heterotrimeric
G
Proteins Transmit
Signals and Reset Themselves
417
Ligand binding to 7TM receptors leads to the
activation of heterotrimeric
G
proteins
419
Activated
G
proteins transmit signals by binding
to other proteins
420
Cyclic AMP stimulates the phosphorylation of many
target proteins by activating protein kinase A
420
G
proteins spontaneously reset themselves through
GTP hydrolysis
421
Some 7T\
f
receptors activate the phosphoinositide cascade
422
Calcium ion is a widely used second messenger
423
Calcium ion often activates the regulatory protein
calmodulin
424
14.2
Insulin Signaling: Phosphorylation
Cascades Are Central to Many
Signal-Transduction Processes
425
The insulin receptor is a dimer that closes around
a bound insulin molecule
426
Part
И
TRANSDUCING AND
STORING ENERGY
Chapter
15
Metabolism: Basic Concepts
and Design
443
15.1
Metabolism Is Composed of Many
Coupled, Interconnecting Reactions
444
Metabolism consists of energy-yielding and
energy-requiring reactions
444
A thermodynamicaily unfavorable reaction can be
driven by a favorable reaction
445
15.2
ATP is the Universal Currency of Free
Energy in Biological Systems
446
ATP hydrolysis is exergonic
446
ATP hydrolysis drives metabolism by shifting the
equilibrium of coupled reactions
447
The high phosphoryl potential of ATP results
from structural differences between ATP and its
hydrolysis products
449
Phosphoryl-transfer potential is an important form
of cellular energy transformation
450
xxii Contents
15.3
The Oxidation of Carbon Fuels Is an
Important Source of Cellular Energy
Compounds with high phosphoryl-transfer potential
can couple carbon oxidation to ATP synthesis
Ion gradients across membranes provide an
important form of cellular energy that can be
coupled to ATP synthesis
Energy from foodstuffs is extracted in three stages
15.4
Metabolic Pathways Contain Many
Recurring Motifs
Activated carriers exemplify the modular design and
economy of metabolism
Many activated carriers are derived from vitamins
Key reactions are reiterated throughout metabolism
Metabolic processes are regulated in three
principal ways
Aspects of metabolism may have evolved from an
RNA
world
451
452
453
453
454
454
457
459
461
463
Chapter
16
Glycolysis and Gluconeogenesis
469
Glucose is generated from dietary carbohydrates
470
Glucose is an important fuel for most organisms
471
Î6.Ï
Glycolysis Is an Energy-Conversion
Pathway in Many Organisms
471
Hcxokinase traps glucose in the cell and begins
glycolysis
471
Fructose 1,6-bisphosphate is generated from glucose
6-phosphate
473
The six-carbon sugar is cleaved into two
three-carbon fragments
474
Mechanism:
Triose
phosphate isomerase salvages a
three-carbon fragment
475
The oxidation of an aldehyde to an acid powers
the formation of a compound with high
phosphoryl-transfer potential
476
Mechanism: Phosphorylation is coupled to the
oxidation of glyceraldehyde 3-phosphate by a
thioester intermediate
478
ATP is formed by phosphoryl transfer from
l^-bisphosphoglycerate
479
Additional ATP is generated with the formation of
pyruvate
480
Two ATP molecules are formed in the conversion
of glucose into pyruvate
481
NAD* is regenerated from the metabolism
of pyruvate
482
Fermentations provide usable energy in the absence
ofoxygen
484
The binding site for NAD* is similar in many
dehydrogenases
485
Fructose and
galactose
are converted into glycolytic
intermediates
485
Many adults are intolerant of milk because they
are deficient in lactase
Galactose
is highly toxic if the
transferase
is missing
16.2
The Glycolytic Pathway Is Tightly
Controlled
Glycolysis in muscle is regulated to meet the need
for ATP
The regulation of glycolysis in the liver illustrates
the biochemical versatility of the liver
A family of transporters enables glucose to enter
and leave animal cells
Cancer and exercise training affect glycolysis in a
similar fashion
16.3
Glucose Can Be Synthesized from
Noncarbohydrate Precursors
Gluconeogenesis is not a reversal of glycolysis
The conversion of pyruvate into phosphoenolpyruvate
begins with the formation of oxaloacetate
Oxaloacetate is shuttled into the cytoplasm and
converted into phosphoenolpyruvate
The conversion of fructose 1,6-bisphosphate into
fructose 6-phosphate and
orthophosphate
is an
irreversible step
The generation of free glucose is an important
control point
Six high-transfer-potential phosphoryl groups are
spent in synthesizing glucose from pyruvate
16.4
Gluconeogenesis and Glycolysis Are
Reciprocally Regulated
Energy charge determines whether glycolysis or
gluconeogenesis will be most active
The balance between glycolysis and gluconeogenesis
in the liver is sensitive to blood-glucose concentration
Substrate cycles amplify metabolic signals and
produce heat
Lactate
and
alaninę
formed by contracting muscle
are used by other organs
Glycolysis and gluconeogenesis are evolutionarily
intertwined
Chapter
17
The Citric Acid Cycle
487
488
488
489
490
493
494
495
497
498
499
500
500
501
502
502
503
505
505
507
515
The citric acid cycle harvests high-energy electrons
516
17.1
Pyruvate Dehydrogenase Links Glycolysis
to the Citric Acid Cycle
517
Mechanism: The synthesis of
acetyl
coenzyme a from
pyruvate requires three enzymes and five coenzymes
518
Flexible linkages allow lipoamide to move between
different active sites
520
17.2
The Citric Acid Cycle Oxidizes
Two-Carbon Units
521
Citrate synthase forms citrate from oxaloacetate and
acetyl
coenzyme A
522
Contents xxiii
Mechanism: The mechanism of citrate synthase
prevents undesirable reactions
522
Citrate is isomerized into
isocitrate
524
Isocitrate
is oxidized and decarboxylated to
alpha-ketoglutarate
524
Succinyl coenzyme A is formed by the oxidative
decarboxylation of alpha-ketoglutarate
525
A compound with high phosphoryl-transfer potential
is generated from succinyl coenzyme A
525
Mechanism: Succinyl coenzyme A synthetase
transforms types of biochemical energy
526
Oxaloacetate is regenerated by the oxidation
of succinate
527
The citric acid cycle produces high-transfer-potential
electrons, ATP, and CCb
528
17.3
Entry to the Citric Acid Cycle and
Metabolism Through It Are Controlled
530
The pyruvate dehydrogenase complex is regulated
allosterically and by reversible phosphoryiation
531
The citric acid cycle is controlled at several points
532
Defects in the citric acid cycle contribute to the
development of cancer
533
Τ
7.4
The Citric Acid Cycle Is a Source of
Biosynthetic Precursors
534
The citric acid cycle must be capable of being
rapidly replenished
534
The disruption of pyruvate metabolism is the cause
of beriberi and poisoning by mercury and arsenic
535
The citric acid cycle may have evolved from
preexisting pathways
536
17.5
The Glyoxylate Cycle Enables Plants
and Bacteria to Grow on Acetate
536
543
Chapter
18
Oxidative Phosphoryiation
18.1
Eukaryotic Oxidative Phosphoryiation
Takes Place in Mitochondria
544
Mitochondria are bounded by a double membrane
544
Mitochondria are the result of an
endosymbiotic event
545
18.2
Oxidative Phosphoryiation Depends on
Electron Transfer
546
The electron-transfer potential of an electron is
measured as
redox
potential
546
A 1.14-volt potential difference between XADH and
molecular oxygen drives electron transport through
the chain and favors the formation of a proton
gradient
548
18.3
The Respiratory Chain Consists of
Four Complexes: Three Proton Pumps and
a Physical Link to the Citric Acid Cycle
549
The high-potential electrons of XADH enter the
respiratory chain at XADH-Qoxidoreductase
551
Ubiquinol is the entry point for electrons from FADH?
of flavoproteins
Electrons flow from ubiquinol to cytochrome
с
through Q- cytochrome
с
oxidoreductase
The Qcycle funnels electrons from a two-electron
carrier to a one-electron carrier and pumps protons
Gytochrome
с
oxidase
catalyzes the reduction of
molecular oxygen to water
Toxic derivatives of molecular oxygen such as
superoxide
radical are scavenged by protective enzymes
Electrons can be transferred between groups that are
not in contact
The conformation of cytochrome
с
has remained
essentially constant for more than a billion years
18.4
A Proton Gradient Powers the
Synthesis of ATP
ATP synthase is composed of a proton-conducting
unit and a catalytic unit
Proton flow through ATP synthase leads to the release
of tightly bound ATP: The binding-change mechanism
Rotational catalysis is the world's smallest molecular motor
Proton flow around the
с
ring powers ATP synthesis
ATP synthase and
G
proteins have several common
features
18.5
Many Shuttles Allow Movement Across
Mitochondrial Membranes
Electrons from cytoplasmic KADH enter
mitochondria by shuttles
The entry of
AL) P
into mitochondria is coupled to
the exit of ATP by ATP-ADP translocase
Mitochondrial transporters for metabolites have a
common tripartite structure
18.6
The Regulation of Cellular Respiration Is
Governed Primarily by the Need for ATP
The complete oxidation of glucose yields about
30
molecules of ATP
The rate of oxidative phosphoryiation is determined
by the need for ATP
Regulated uncoupling leads to the generation of heat
Oxidative phosphoryiation can be inhibited at many stages
Mitochondrial diseases are being discovered
Mitochondria play a key role in apoptosis
Power transmission by proton gradients is a central
motif of bioenergetics
Chapter
19
The Light Reactions of
Photosynthesis
553
553
554
555
558
560
561
561
563
564
565
566
568
568
569
570
571
572
572
573
574
576
576
577
585
Photosynthesis converts light energy into chemical energy
586
19.1
Photosynthesis Takes Place in Chforoplasts
587
The primary events of photosynthesis take place in
thylakoid membranes
587
Chloroplaste
arose from an endosymbiotic event
588
xxiv Contents
19.2 Light
Absorption by
Chlorophyll
Induces
Electron Transfer
A special pair of chlorophylls initiate charge separation
Cyclic electron flow reduces the cytochrome of the
reaction center
19.3
Two
Photosystems
Generate a Proton
Gradient and NADPH in Oxygenic
Photosynthesis
Photosystem
II transfers electrons from water to
plastoquinone and generates a proton gradient
Cytochrome bf links photosystem II to photosystem I
Photosystem
I uses light energy to generate reduced
ferredoxin, a powerful reductant
Ferredoxin-NADP4"
reducíase
converts NADP4"
into NADPH
19.4
A Proton Gradient Across the Thylakoid
Membrane Drives ATP Synthesis
The ATP synthase of chloroplasts closely resembles
those of mitochondria and prokaryotes
Cyclic electron flow through photosystem I leads to
the production of ATP instead of NADPH
The absorption of eight photons yields one Cb, two
NADPH, and three ATP molecules
19.5
Accessory Pigments Funnel Energy into
Reaction Centers
Resonance energy transfer allows energy to move
from the site of initial absorbance to the reaction
center
Light-harvesting complexes contain additional
chlorophylls and carotinoids
The components of photosynthesis are highly organized
Many herbicides inhibit the light reactions of
photosynthesis
19.6
The Ability to Convert Light into Chemical
Energy Is Ancient
Chapter
20
The Calvin Cycle and Pentose
Phosphate Pathway
588
589
592
592
592
595
595
596
597
598
599
600
601
601
602
603
604
604
609
20.1
The Calvin Cycle Synthesizes Hexoses
from Carbon Dioxide and Water
610
Carbon dioxide reacts with ribulose
1
,5-bisphosphate
to form two molecules of 3-phosphogrycerate
611
Rubisco activity depends on magnesium and
carbamate
612
Rubisco also catalyzes a wasteful oxygenase reaction:
Catalytic imperfection
613
Hexose phosphates are made from phosphoglycerate,
and ribulose
1
,5-bisphosphate is regenerated
614
Three ATP and two NADPH molecules are used to
bring carbon dioxide to the level of a hexose
617
Starch and sucrose are the major carbohydrate
stores in plants
617
20.2
The Activity of the Calvin Cycle Depends
on Environmental Conditions
Rubisco is activated by light-driven changes in proton
and magnesium ion concentrations
Thioredoxin plays a key role in regulating the
Calvin cycle
The C4 pathway of tropical plants accelerates
photosynthesis by concentrating carbon dioxide
Crassulacean acid metabolism permits growth in
arid ecosystems
20.3
The Pentose Phosphate Pathway
Generates NADPH and Synthesizes
Five-Carbon Sugars
Two molecules of NADPH are generated in the
conversion of glucose 6-phosphate into ribulose
5
-phosphate
The pentose phosphate pathway and glycolysis are
linked by transketolase and transaldolase
Mechanism: Transketolase and transaldolase stabilize
carbanionic intermediates by different mechanisms
20.4
The Metabolism of Glucose 6-phosphate
by the Pentose Phosphate Pathway Is
Coordinated with Glycolysis
The rate of the pentose phosphate pathway is controlled
bythelevelofNADP+
The flow of glucose 6-phosphate depends on the
need for NADPH, ribose
5
-phosphate, and ATP
Through the looking-glass: The Calvin cycle and the
pentose phosphate pathway are mirror images
20.5
Glucose 6-phosphate Dehydrogenase
Plays a Key Role in Protection Against Reactive
Oxygen Species
Glucose 6-phosphate dehydrogenase deficiency causes
a drug-induced hemolytic anemia
A deficiency of glucose 6-phosphate dehydrogenase
confers an evolutionary advantage in some
circumstances
Chapter
21
Glycogen Metabolism
617
618
618
619
620
621
621
621
624
626
626
627
629
629
629
631
637
Glycogen metabolism is the regulated release and
storage of glucose
638
21.1
Glycogen Breakdown Requires the
Interplay of Several Enzymes
639
Phosphorylase catalyzes the phosphorolytic cleavage
of glycogen to release glucose
1
-phosphate
639
Mechanism: Pyridoxal phosphate participates in the
phosphorolytic cleavage of glycogen
640
A debranching enzyme also is needed for the
breakdown of glycogen
641
Phosphoglucomutase converts glucose
1
-phosphate
into glucose 6-phosphate
642
The liver contains glucose 6-phosphatase, a
hydrolytic enzyme absent from muscle
643
Contents xxv
21.2 Phosphorylase
Is Regulated by
Allosteric
Interactions
and Reversible Phosphorylation 643
Muscle
phosphorylase
is regulated by the intracellular
energy charge
643
Liver phosphorylase produces glucose for use by other
tissues
645
Phosphorylase kinase is activated by phosphorylation
and calcium ions
645
21.3
Epinephrine and Glucagon Signal the
Need for Glycogen Breakdown
646
G
proteins transmit the signal for the initiation of
glycogen breakdown
646
Glycogen breakdown must be rapidly turned off
when necessary
648
The regulation of glycogen phosphorylase became
more sophisticated as the enzyme evolved
649
21.4
Glycogen Is Synthesized and Degraded
by Different Pathways
649
UDP-glucose is an activated form of glucose
649
Glycogen synthase catalyzes the transfer of glucose
from UDP-glucose to a growing chain
650
A branching enzyme forms
α
-1,6
linkages
651
Glycogen synthase is the key regulatory enzyme in
glycogen synthesis
651
Glycogen is an efficient storage form of glucose
651
21.5
Glycogen Breakdown and Synthesis Are
Reciprocally Regulated
652
Protein phosphatase
1
reverses the regulatory effects
of kinases on glycogen metabolism
653
Insulin stimulates glycogen synthesis by inactivating
glycogen synthase kinase
654
Glycogen metabolism in the liver regulates the
blood-glucose level
655
A biochemical understanding of glycogen-storage
diseases is possible
656
The complete oxidation of palmitate yields
106
molecules of ATP
671
Chapter
22
Fatty Acid Metabolism
663
Fatty acid degradation and synthesis mirror each
other in their chemical reactions
664
22.1
Triacylglycerols Are Highly Concentrated
Energy Stores
665
Dietary lipids are digested by pancreatic lipases
665
Dietary lipids are transported in chylomicrons
666
22.2
The Use of Fatty Acids As Fuel Requires
Three Stages of Processing
667
Triacylglycerols are hydrolyzed by hormone-stimulated
lipases
667
Fatty acids are linked to coenzyme A before they
are oxidized
668
Carnitine carries long-chain activated fatty acids
into the mitochondrial matrix
669
Acetyl
CoA, NADH, and FADFb are generated in
each round of fatty acid oxidation
670
22.3
Unsaturated and Odd-Chain Fatty Acids
Require Additional Steps for Degradation
672
An isomerase and a reductase are required for
the oxidation of unsaturated fatty acids
672
Odd-chain fatty acids yield propionyl CoA in the
final thiolysis step
673
Vitamin B12 contains a corrin ring and a cobalt atom
674
Mechanism: Methylmalonyl CoA
mutase
catalyzes a
rearrangement to form succinyl CoA
675
Fatty acids are also oxidized in peroxisomes
676
Ketone
bodies are formed from
acetyl CoA
when
fat breakdown predominates
677
Ketone
bodies are a major fuel in some tissues
678
Animals cannot convert fatty acids into glucose
680
22.4
Fatty Acids Are Synthesized by Fatty
Acid Synthase
680
Fatty acids are synthesized and degraded by different
pathways
680
The formation of malonyl CoA is the committed step
in fatty acid synthesis
681
Intermediates in fatty acid synthesis are attached to
an acyl carrier protein
681
Fatty acid synthesis consists of a series of condensation,
reduction, dehydration, and reduction reactions
682
Fatty acids are synthesized by a multifunctional
enzyme complex in animals
683
The synthesis of palmitate requires
8
molecules of
acetyl
CoA,
14
molecules of NADPH, and
7
molecules of ATP
685
Citrate carries
acetyl
groups from mitochondria to
the cytoplasm for fatty acid synthesis
686
Several sources supply NADPH for fatty acid synthesis
686
Fatty acid synthase inhibitors may be useful drugs
687
22.5
The Elongation and Unsaturation of
Fatty Acids Are Accomplished by Accessory
Enzyme Systems
687
Membrane-bound enzymes generate unsaturated fatty acids
688
Eicosanoid hormones are derived from polyunsaturated
fatty acids
688
22.6
Acetyl CoA
Carboxylase Plays a Key Role
in Controlling Fatty Acid Metabolism
690
Acetyl CoA
carboxylase is regulated by conditions in
the cell
690
Acetyl CoA
carboxylase is regulated by a variety of
hormones
690
Chapter
23
Protein Turnover and
Amino
Acid Catabolism
697
23.1
Proteins Are Degraded to
Amino
Acids
698
The digestion of dietary proteins begins in the
stomach and is completed in the intestine
698
Cellular proteins are degraded at different rates
699
xxvi Contents
701
701
23.2 Protein
Turnover
Is Tightly Regulated
699
Ubiquitin tags proteins for destruction
699
The proteasome digests the ubiquitin-tagged
proteins
The ubiquitin pathway and the proteasome
have prokaryotic counterparts
Protein degradation can be used to regulate
biological function
"02
23.3
The First Step in
Amino
Acid Degradation
Is the Removal of Nitrogen
704
Alpha-amino groups are converted into
ammonium ions by the oxidative deamination
of
glutamate
704
Mechanism: Pyridoxal phosphate forms Schiff-base
intermediates in aminotransferases
705
Aspartate aminotransferase is an archetypal
pyridoxal-dependent transaminase
706
Pyridoxal phosphate enzymes catalyze a wide array
of reactions
707
Serine
and threonine can be directly
deaminated
708
Peripheral tissues transport nitrogen to the
liver
708
23.4
Ammonium Ion Is Converted into Urea
in Most Terrestrial Vertebrates
709
The urea cycle begins with the formation of
carbamoyl phosphate
709
The urea cycle is linked to gluconeogenesis
711
Urea-cycle enzymes are evolutionarily related to
enzymes in other metabolic pathways
712
Inherited defects of the urea cycle cause
hyperammonemia and can lead to brain damage
712
Urea is not the only means of disposing of
excess nitrogen
713
23.5
Carbon Atoms of Degraded
Amino
Acids Emerge As Major Metabolic
Intermediates
714
Pyruvate is an entry point into metabolism for a
number of
amino
acids
715
Oxaloacetate is an entry point into metabolism for
aspartate and asparagine
716
Alpha-ketoglutarate is an entry point into metabolism
for five-carbon
amino
acids
716
Succinyl coenzyme A is a point of entry for several
nonpolar
amino
acids
717
Methionine degradation requires the formation of a
key methyl donor, S-adenosylmethionine
717
The branched-chain
amino
acids yield
acetyl
GoA,
acetoacetate, or propionyl CoA
717
Oxygenases are required for the degradation of
aromatic
amino
acids
719
23.6
Inborn Errors of Metabolism Can
Disrupt
Amino
Acid Degradation
72
Ì
Part ill SYNTHESIZING THE MOLECULES
OF LIFE
Chapter
24
The Biosynthesis of
Amino
Acids
729
Amino
acid synthesis requires solutions to three
key biochemical problems
7Л0
24.1
Nitrogen Fixation: Microorganisms Use
ATP and a Powerful Reductant to Reduce
Atmospheric Nitrogen to Ammonia
730
The iron-molybdenum cofactor of nitrogenase binds
and reduces atmospheric nitrogen
7
Л
1
Ammonium ion is assimilated into an
amino
acid
through
glutamate
and
glutaminę
7ЛЛ
24.2
Amino
Acids Are Made from Intermediates
of the Citric Acid Cycle and Other Major
Pathways
735
Human beings can synthesize some
amino
acids but
must obtain others from the diet
735
Aspartate,
alaninę,
and
glutamate
are formed by the
addition of an
amino
group to an alpha-ketoacid
736
A common step determines the chirality of all
amino
acids
737
The formation of asparagine from aspartate requires
an adenylated intermediate
737
Glutamate
is the precursor of
glutaminę,
proline,
and
arginine
738
S-Phosphoglycerate is the precursor of
serine,
cysteine,
and
glycine
738
Tetrahydrofolate carries activated one-carbon units
at several oxidation levels
739
S-Adenosylmethionine is the major donor of
methyl groups
740
Cysteine
is synthesized from
serine
and
homocysteine
742
High homocysteine levels correlate with
vascular disease
743
Shikimate and chorismate are intermediates in the
biosynthesis of aromatic
amino
acids
743
Tryptophan synthase illustrates substrate channeling
in enzymatic catalysis
746
24.3
Feedback Inhibition Regulates
Amino
Acid Biosynthesis
747
Branched pathways require sophisticated
regulation
747
An enzymatic cascade modulates the activity of
glutaminę
synthetase
749
24.4
Amino
Acids Are Precursors of Many
Biomolecules
750
Glutathione, a gamma-glutamyl
peptide,
serves as
a sulfhy dryl buffer and an
antioxidant
751
Nitric oxide, a short-lived signal molecule, is formed
from
arginine
751
Contents xxvii
Porphyrins
are synthesized from
glycine
and succinyl
coenzyme A
752
Porphyrins accumulate in some inherited disorders of
porphyrin
metabolism
754
Chapter
25
Nucleotide Biosynthesis
761
Nucleotides can be synthesized by
de novo
or
salvage pathways
762
25.1
The Pyrimidine Ring Is Assembled
de
Novo
or Recovered by Salvage Pathways
763
Bicarbonate and other oxygenated carbon compounds
are activated by phosphorylation
763
The side chain of
glutaminę
can be hydrolyzed to
generate ammonia
763
Intermediates can move between active sites by
channeling
763
Orotate
acquires a ribose ring from PRPP to
form a pyrimidine nucleotide and is converted
into uridylate
764
Nucleotide mono-,
di-,
and triphosphates are
interconvertible
765
GTP is formed by aminationof UTP
765
Salvage pathways recycle pyrimidine bases
766
25.2
Purine
Bases Can Be Synthesized
de
Novo
or Recycled by Salvage Pathways
766
The
purine
ring system is assembled on ribose
phosphate
766
The
purine
ring is assembled by successive steps of
activation by phosphorylation followed by
displacement
767
AMP and GMP are formed from IMP
769
Enzymes of the
purine
synthesis pathway associate
with one another in vivo
770
Salvage pathways economize intracellular energy
expenditure
770
25.3
Deoxyribonucleotides Are Synthesized
by the Reduction of Ribonucleotides Through
a Radical Mechanism
771
Mechanism: A tyrosyl radical is critical to the action
of ribonucleotide
reducíase
771
Stable radicals other than tyrosyl radical are
employed by other ribonucleotide reductases
773
Thymidylate is formed by the methylation of
deoxyuridylate
774
Dihydrofolate
reducíase
catalyzes the regeneration
of ietrahydrofolate, a one-carbon carrier
775
Several valuable aniicancer drugs block the synthesis
of thymidylaie
775
25.4
Key Steps in Nucleotide Biosynthesis Are
Regulated by Feedback Inhibition
776
Pyrimidine biosynthesis is regulated by aspartaie
transcarbamoylase
777
The synthesis of
purine
nucleotides is controlled by
feedback inhibition at several sites
The synthesis of deoxyribonucleotides is
controlled by the regulation of ribonucleotide
reducíase
25.5
Disruptions in Nucleotide Metabolism
Can Cause Pathological Conditions
The loss of adenosine deaminase activity results
in severe combined immunodeficiency
Gout is induced by high serum levels of
urate
Lesch—Nyhan syndrome is a dramatic consequence
of mutations in a salvage-pathway enzyme
Folk acid deficiency promotes birth defects such
as
spina bifida
Chapter
26
The Biosynthesis of Membrane
Lipids and Steroids
III
778
778
778
779
780
781
787
26.1
Phosphatidate Is a Common Intermediate
in the Synthesis of Phospholipids and
Triacylglycerols
788
The synthesis of phospholipids requires an activated
intermediate
789
Sphingolipids are synthesized from ceramide
791
Gangliosides are carbohydrate-rich sphingolipids
that contain acidic sugars
792
Sphingolipids confer diversity on
lipid
structure and
function
793
Respiratory distress syndrome and
Тау
-Sachs disease
result from the disruption of
lipid
metabolism
793
Phosphatiditic acid phosphatase is a key regulatory
enzyme in
lipid
metabolism
794
26.2
Cholesterol Is Synthesized from
Acetyl
Coenzyme A in Three Stages
795
The synthesis of mevalonate, which is activated as
isopentenyl
pyrophosphate,
initiates the synthesis of
cholesterol
795
Squalene
(С30)
is synthesized from six molecules of
isopentenyl
pyrophosphate (C5)
796
Squalene cyclizes to form cholesterol
797
26.3
The Complex Regulation of
Cholesterol Biosynthesis Takes Place at
Several Levels
798
Lipoproteins transport cholesterol and triacylglycerols
throughout the organism
801
The blood levels of certain lipoproteins can serve
diagnostic purposes
802
Low-density lipoproteins play a central role in
cholesterol metabolism
803
The absence of the LDL receptor leads to
hypercholesterolemia and atherosclerosis
804
Mutations in the LDL receptor prevent LDL release
and result in receptor destruction
805
xxvi
ïi
Contents
HDL appears to protect against arteriosclerosis
The clinical management of cholesterol levels can be
understood at a biochemical level
26.4
Important Derivatives of Cholesterol
Include Bile Salts and Steroid Hormones
Letters identify the steroid rings and numbers
identify the carbon atoms
Steroids are hydroxylated by cytochrome P450
monooxygenases that use NADPH and
СЪ
The cytochrome P450 system is widespread and
performs a protective function
Pregnenolone, a precursor of many other steroids, is
formed from cholesterol by cleavage of its side chain
Progesterone and corticosteroids are synthesized from
pregnenolone
Androgens and estrogens are synthesized from
pregnenolone
Vitamin
D
is derived from cholesterol by the
ring-splitting activity of light
806
807
807
809
809
810
811
811
812
813
Chapter
27
The Integration of Metabolism
821
27.1
Caloric Homeostasis Is a Means of
Regulating Body Weight
822
27.2
The Brain Plays a Key Role in Caloric
Homeostasis
824
Signals from the gastrointestinal tract induce feelings
of satiety
824
Leptin and insulin regulate long-term control
over caloric homeostasis
825
Leptin is one of several hormones secreted by
adipose tissue
826
Leptin resistance may be a contributing factor
to obesity
827
Dieting is used to combat obesity
827
27.3
Diabetes Is a Common Metabolic Disease
Often Resulting from Obesity
828
Insulin initiates a complex signal-transduction
pathway in muscle
828
Metabolic syndrome often precedes type
2
diabetes
830
Excess fatty acids in muscle modify metabolism
830
Insulin resistance in muscle facilitates pancreatic failure
831
Metabolic derangements in type
1
diabetes result from
insulin insufficiency and glucagon excess
832
27.4
Exercise Beneficially Alters the
Biochemistry of Cells
833
Mitochondrial biogenesis is stimulated by muscular activity
834
Fuel choice during exercise is determined by the
intensity and duration of activity
835
27.5
Food Intake and Starvation Induce
Metabolic Changes
836
The starved-fed cycle is the physiological response
to a fast
837
Metabolic adaptations in prolonged starvation
minimize protein degradation
27.6
Ethanol
Alters Energy Metabolism in
the Liver
Ethanol
metabolism leads to an excess of NADH
Excess
ethanol
consumption disrupts vitamin
metabolism
Chapter
28 DNA
Replication, Repair, and
Recombination
838
840
840
842
849
28.1 DNA
Replication Proceeds by the
Polymerization of Deoxyribonucleoside
Triphosphates Along a Template
850
DNA
polymerases require a template and a primer
850
AU DNA
polymerases have structural features in
common
851
Two bound metal ions participate in the
polymerase reaction
851
The specificity of replication is dictated by
complementarity of shape between bases
852
An
RNA
primer synthesized by
primase
enables
DNA
synthesis to begin
853
One strand of
DNA
is made continuously, whereas
the other strand is synthesized in fragments
853
DNA
ligase
joins ends of
DNA in
duplex regions
854
The separation of
DNA
strands requires specific
helicases
and ATP hydrolysis
854
28.2 DNA
Unwinding and Supercoiling Are
Controlled by Topoisomerases
855
The linking number of
DNA,
a topological property,
determines the degree of supercoiling
856
Topoisomerases prepare the double helix for
unwinding
858
Type I topoisomerases relax supercoiled structures
858
Type II topoisomerases can introduce negative
supercoils through coupling to ATP hydrolysis
859
28.3 DNA
Replication Is Highly Coordinated
861
DNA
replication requires highly
processive
polymerases
861
The leading and lagging strands are synthesized
in a coordinated fashion
862
DNA
replication in Escherickia
coli
begins at a
unique site
864
DNA
synthesis in eukaryotes is initiated at multiple sites
865
Telomeres are unique structures at the ends of
linear chromosomes
866
Telomeres are replicated by telomerase, a specialized
polymerase that carries its own
RNA
template
867
28.4
Many Types of
DNA
Damage Can Be
Repaired 867
Errors can arise in
DNA
replication
867
Bases can be damaged by oxidizing agents, alkylating
agents, and light 868
Contents xxix
DNA
damage
can be detected and repaired by a
variety of systems
The presence of thymine instead of uracil in
DNA
permits the repair of deaminated cytosine
Some genetic diseases are caused by the expansion
of repeats of three nucleotides
Many cancers are caused by the defective repair
of
DNA
Many potential carcinogens can be detected by their
mutagenic action on bacteria
28.5 DNA
Recombination Plays Important Roles
in Replication, Repair, and Other Processes
RecA can initiate recombination by promoting strand
invasion
Some recombination reactions proceed through
Holliday-junction intermediates
RNA
synthesis comprises three stages: Initiation,
elongation, and termination
29.1
RNA Polymerases
Catalyze Transcription
RNA
chains are formed
de novo
and grow in the
б'-Їо-З'
direction
RNA
polymerases backtrack and correct errors
RNA polymerase
binds to promoter sites on the
DNA
template to initiate transcription
Sigma subunits of
RNA
polymerase recognize
promoter sites
RNA
polymerases must unwind the template
double helix for transcription to take place
Elongation takes place at transcription bubbles
that move along the
DNA
template
Sequences within the newly transcribed
RNA
signal
termination
Some messenger RNAs directly sense metabolite
concentrations
The rho protein helps to terminate the transcription
of some genes
Some antibiotics inhibit transcription
Precursors of transfer and ribosomal
RNA
are
cleaved and chemically modified after transcription
in prokaryotes
29.2
Transcription in Eukaryotes Is Highly
Regulated
Three types of
RNA
polymerase synthesize
RNA
in
eukaryotic cells
Three common elements can be found in the
RNA
polymerase II promoter region
The TFIID protein complex initiates the assembly of
the active transcription complex
Multiple transcription factors interact with eukaryotic
promoters
869
871
872
872
873
874
874
875
Chapter
29
RNA
Synthesis and Processing
883
884
885
890
890
891
892
892
893
895
896
897
898
899
900
Enhancer sequences can stimulate transcription at
start sites thousands of bases away
29.3
The Transcription Products of Eukaryotic
Polymerases Are Processed
RNA
polymerase I produces three ribosomal RNAs
RNA
polymerase III produces transfer
RNA
The product of
RNA
polymerase II, the pre-mRNA
transcript, acquires a
5'
cap and a
3'
poly(A) tail
Small regulatory RNAs are cleaved from larger
precursors
RNA
editing changes the proteins encoded by mRNA
Sequences at the ends of
introns
specify splice sites
in mRNA precursors
Splicing consists of two sequential transesterification
reactions
Small nuclear RNAs in spliceosomes catalyze the
splicing of mRNA precursors
Transcription and processing of mRNA are coupled
Mutations that affect pre-mRNA splicing cause disease
Most human pre-mRNAS can be spliced in alternative
ways to yield different proteins
29.4
The Discovery of Catalytic
RNA
Was
Revealing in Regard to Both Mechanism and
Evolution
Chapter
30
Protein Synthesis
900
901
901
902
902
904
904
905
906
907
909
909
910
911
921
30.1
Protein Synthesis Requires the Translation
of Nucleotide Sequences into
Amino
Acid
Sequences
The synthesis of long proteins requires a low error
frequency
Transfer
RNA
molecules have a common design
Some transfer
RNA
molecules recognize more than
one codon because of wobble in base-pairing
30.2
Aminoacyl Transfer
RNA Synthetases
Read the Genetic Code
Amino
acids are first activated by adenylation
Aminoacyl-tRNA synthetases have highly discriminating
amino
acid activation sites
Proofreading by aminoacyl-tRNA synthetases increases
the fidelity of protein synthesis
Synthetases recognize various features of transfer
RNA
molecules
Aminoacyl-tRNA synthetases can be divided into two
classes
30.3
The Ribosome Is the Site of Protein
Synthesis
Ribosomal RNAs (5S, 16S, and 23S rRNA) play a central
role in protein synthesis
Ribosomes have three tRNA-binding sites that bridge
the 30s and 50s subunits
922
922
923
925
927
927
928
929
930
931
931
932
934
xxx Contents
The start signal is usually
AUG
preceded by several
bases that pair with
1
6S rRN A
Bacterial protein synthesis is initiated by
formylmethionyl transfer
RNA
Formylmethionyl-tRNAf is placed in the
Ρ
site of
the ribosome in the formation of the
70S
initiation complex
Elongation factors deliver aminoacyl-tRNA to the
ribosome
Peptidyl
transferase
catalyzes peptide-bond
synthesis
The formation of
a
peptide
bond is followed by the
GTP-driven
translocation
of tRNAs and mRNA
Protein synthesis is terminated by release factors
that read stop
codons
30.4
Eukaryotic Protein Synthesis Differs
from Prokaryotic Protein Synthesis Primarily
in Translation Initiation
Mutations in initiation factor
2
cause a curious
pathological condition
30.5
A Variety of Antibiotics and Toxins Can
Inhibit Protein Synthesis
Some antibiotics inhibit protein synthesis
Diphtheria toxin blocks protein synthesis in eukaryotes
by inhibiting
translocation
Ricin
fatally modifies 28S ribosomal
RNA
30.6
Ribosomes Bound to the Endoplasmic
Reticulum Manufacture Secretory and
Membrane Proteins
Signal sequences mark proteins for
translocation
across
the endoplasmic reticulum membrane
Transport vesicles carry cargo proteins to their final
destination
Chapter
31
The Control of Gene Expression
in Prokaryotes
934
935
936
936
937
938
940
941
942
943
943
944
945
945
945
947
957
31.1
Many DNA-Binding Proteins Recognize
Specific
DNA
Sequences
958
The helix-turn-helix motif is common to many
prokaryotic DNA-binding proteins
959
31.2
Prokaryotic DNA-Binding Proteins Bind
Specifically to Regulatory Sites in
Opérons
959
An
operan
consists of regulatory elements and
protein-encoding genes
960
The lac
repressor
protein in the absence of lactose
binds to the operator and blocks transcription
961
Ligand binding can induce structural changes in
regulatory proteins
962
The operon is a common regulatory unit in
prokaryotes
962
Transcription can be stimulated by proteins that
contact
RNA polymerase
963
31.3
Regulatory Circuits Can Result in Switching
Between Patterns of Gene Expression
Lambda
repressor
regulates its own expression
A circuit based on lambda
repressor
and Cro form
a genetic switch
Many prokaryotic cells release chemical signals that
regulate gene expression in other cells
Biofilms
are complex communities of prokaryotes
31.4
Gene Expression Can Be Controlled at
Posttranscriptional Levels
Attenuation is a prokaryotic mechanism for regulating
transcription through the modulation of nascent
RNA
secondary structure
Chapter
32
The Control of Gene Expression
in Eukaryotes
32.2
Transcription Factors Bind
DNA
and
Regulate Transcription Initiation
A range of DNA-binding structures are employed
by eukaryotic DNA-binding proteins
Activation domains interact with other proteins
Multiple transcription factors interact with eukaryotic
regulatory regions
Enhancers can stimulate transcription in specific
cell types
Induced pluripotent stem cells can be generated by
introducing four transcription factors into
differentiated cells
32.3
The Control of Gene Expression Can
Require Chromatin Remodeling
The methylation of
DNA
can alter patterns of gene
expression
Steroids and related hydrophobic molecules pass
through membranes and bind to DNA-binding receptors
Nuclear hormone receptors regulate transcription by
recruiting coactivators to the transcription complex
Steroid-hormone receptors are targets for drugs
Chromatin structure is modulated through covalent
modifications of histone tails
Histone deacetylases contribute to transcriptional
repression
32.4
Eukaryotic Gene Expression Can Be
Controlled at Posttranscriptional Levels
Genes associated with iron metabolism are
translationally regulated in animals
Small RNAs regulate the expression of many
eukaryotic genes
964
964
965
965
966
967
967
973
32.1
Eukaryotic
DNA
Is Organized into
Chromatin
Nucleosomes are complexes of
DNA
and histones
DNA
wraps around histone octamers to form
nucleosomes
974
975
975
977
977
978
979
979
980
980
981
982
982
984
985
986
987
987
989
Contents xxxi
Part IV RESPONDING TO
ENVIRONMENTAL CHANGES
Chapter
33
Sensory Systems
995
33.1
A Wide Variety of Organic Compounds
Are Detected by
Olfaction
996
Olfaction
is mediated by an enormous family of
seven-transmembrane-helix receptors
996
Odorants
are decoded by a combinatorial mechanism
998
33.2
Taste Is a Combination of Senses That
Function by Different Mechanisms
1000
Sequencing of the human genome led to the
discovery of a large family of 7TM bitter receptors
1001
A heterodimeric 7TM receptor responds to sweet
compounds
1002
Umami,
the taste of
glutamate
and aspartate, is
mediated by a heterodimeric receptor related to
the sweet receptor
1003
Salty tastes are detected primarily by the passage of
sodium ions through channels
1003
Sour tastes arise from the effects of hydrogen
ions (acids) on channels
1003
33.3
Photoreceptor Molecules in the Eye
Detect Visible Light
1004
Rhodopsin, a specialized 7TM receptor, absorbs
visible light
1004
Light absorption induces a specific isomerization of
bound ll-ds-retinal
1005
Light-induced lowering of the calcium level
coordinates recovery
1006
Color vision is mediated by three cone receptors
that are homologs of rhodopsin
1007
Rearrangements in the genes for the green and
red pigments lead to "color blindness"
1008
33.4
Hearing Depends on the Speedy
Detection of Mechanical Stimuli
1009
Hair cells use a connected bundle of stereocilia to
detect tiny motions
1009
Mechanosensory channels have been identified in
Drosophila
and vertebrates
1010
33.5
Touch Includes the Sensing of Pressure,
Temperature, and Other Factors
1011
Studies of capsaicin reveal a receptor for sensing
high temperatures and other painful stimuli
1011
More sensory systems remain to be studied
1012
Chapter
34
The Immune System
34.1
Antibodies Possess Distinct
Antigen-Binding and Effector Units
34.2
Antibodies Bind Specific Molecules
Through
Hypervariable
Loops
The immunoglobulin fold consists of a beta-sandwich
framework with
hypervariable
loops
X-ray analyses have revealed how antibodies
bind antigens
Large antigens bind antibodies with numerous
interactions
34.3
Diversity Is Generated by Gene
Rearrangements
J
(joining) genes and
D
(diversity) genes increase
antibody diversity
More than
10
antibodies can be formed by
combinatorial association and somatic mutation
The oligomerization of antibodies expressed on the
surfaces of immature
В
cells triggers antibody secretion
Different classes of antibodies are formed by
the hopping of Vh genes
34.4
Major-Histocompatibility-Complex
Proteins Present
Peptide
Antigens on Cell
Surfaces for Recognition by
Т
-Cell
Receptors
Peptides presented by MHC proteins occupy a deep
groove flanked by alpha helices
Т
-cell
receptors are antibody-like proteins
containing variable and constant regions
GD8 on cytotoxic
T
cells acts in concert with
T
-cell receptors
Helper
T
cells stimulate cells that display foreign
peptides bound to class II MHC proteins
Helper
T
cells rely on the
Т
-cell
receptor and CD4 to
recognize foreign peptides on antigen-presenting cells
MHC proteins are highly diverse
Human immunodeficiency viruses subvert the
immune system by destroying helper
T
cells
34.5
The Immune System Contributes to the
Prevention and the Development of Human
Diseases
T
cells are subjected to positive and negative
selection in the
thymus
Autoimmune diseases result from the generation
of immune responses against self-antigens
The immune system plays a role in cancer prevention
Vaccines are a powerful means to prevent and
eradicate disease
Innate immunity is an evolutionarily ancient
defense system
1018
The adaptive immune system responds by using
the principles of evolution
1019
1017
chapter
35
Molecular Motors
1021
1023
1024
1024
1026
1027
1027
1028
1029
1030
1031
1032
1034
1034
1036
1036
1038
1039
1040
1040
1041
1041
1042
1049
35.1
Most Molecular-Motor Proteins Are
Members of the P-Loop NTPase Superfamily
1050
Molecular motors are generally oligomeric proteins
with an ATPase core and an extended structure
1050
xxxii Contents
ATP
binding
and hydrolysis induce changes in the
conformation and binding affinity of motor proteins
35.2
Myosins Move Along Actin Filaments
Actin is a polar, self-assembling, dynamic polymer
Myosin head domains bind to actin filaments
Motions of single motor protems can be directly
observed
Phosphate release triggers the myosin power stroke
Muscle is a complex of myosin and actin
The length of the lever arm determines motor
velocity
35.3
Kinesin and Dynein Move Along
Microtubules
Microtubules are hollow cylindrical polymers
Kinesin motion is highly
processive
35.4
A Rotary Motor Drives Bacterial Motion
Bacteria swim by rotating their
flagella
Proton flow drives bacterial
flagellar
rotation
Bacterial chemotaxis depends on reversal of the
direction of
flagellar
rotation
Chapter
36
Drug Development
1052
1054
1054
1056
1056
1057
1057
1060
1060
1060
1062
1064
1064
1064
1066
1073
36.1
The Development of Drugs Presents
Huge Challenges
1074
Drug candidates must be potent modulators of
their targets
1074
Drugs must have suitable properties to reach their
targets
1075
Toxicity
can limit drug effectiveness
1080
36.2
Drug Candidates Can Be Discovered
by Serendipity, Screening, or Design
1081
Serendipitous observations can drive drug
development
1081
Screening libraries of compounds can yield drugs
or drug leads
1083
Drugs can be designed on the basis of
three-dimensional structural information
about their targets
1086
36.3
Analyses of Genomes Hold Great
Promise for Drug Discovery
1089
Potential targets can be identified in the human
proteome
1089
Animal models can be developed to test the
validity of potential drug targets
1090
Potential targets can be identified in the genomes
of pathogens
1090
Genetic differences influence individual responses
to drags
1091
36.4
The Development of Drugs Proceeds
Through Several Stages
1092
Clinical trials are time consuming and expensive
1092
The evolution of drug resistance can limit
the utility of drugs for infectious agents
and cancer
1094
Answers to Problems
Al
Index Bl |
any_adam_object | 1 |
author | Berg, Jeremy M. 1958- Tymoczko, John L. 1948-2019 Stryer, Lubert 1938-2024 |
author_GND | (DE-588)12460109X (DE-588)124601103 (DE-588)124601197 |
author_facet | Berg, Jeremy M. 1958- Tymoczko, John L. 1948-2019 Stryer, Lubert 1938-2024 |
author_role | aut aut aut |
author_sort | Berg, Jeremy M. 1958- |
author_variant | j m b jm jmb j l t jl jlt l s ls |
building | Verbundindex |
bvnumber | BV037261037 |
classification_rvk | WD 4000 WD 4010 |
classification_tum | CHE 800f |
ctrlnum | (OCoLC)706901557 (DE-599)BVBBV037261037 |
dewey-full | 572 |
dewey-hundreds | 500 - Natural sciences and mathematics |
dewey-ones | 572 - Biochemistry |
dewey-raw | 572 |
dewey-search | 572 |
dewey-sort | 3572 |
dewey-tens | 570 - Biology |
discipline | Biologie Chemie |
edition | Internat. 7. ed. |
format | Book |
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genre | 1\p (DE-588)4151278-9 Einführung gnd-content 2\p (DE-588)4123623-3 Lehrbuch gnd-content |
genre_facet | Einführung Lehrbuch |
id | DE-604.BV037261037 |
illustrated | Illustrated |
indexdate | 2024-08-06T00:21:50Z |
institution | BVB |
isbn | 9781429276351 1429276355 |
language | English |
oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-021174175 |
oclc_num | 706901557 |
open_access_boolean | |
owner | DE-355 DE-BY-UBR DE-20 DE-11 DE-19 DE-BY-UBM DE-29T DE-1028 DE-83 DE-898 DE-BY-UBR DE-91G DE-BY-TUM DE-634 |
owner_facet | DE-355 DE-BY-UBR DE-20 DE-11 DE-19 DE-BY-UBM DE-29T DE-1028 DE-83 DE-898 DE-BY-UBR DE-91G DE-BY-TUM DE-634 |
physical | Getr. Zählung zahlr. Ill., graph. Darst. |
publishDate | 2012 |
publishDateSearch | 2012 |
publishDateSort | 2012 |
publisher | Freeman [u.a.] |
record_format | marc |
spelling | Berg, Jeremy M. 1958- Verfasser (DE-588)12460109X aut Biochemistry Jeremy M. Berg ; John L. Tymoczko ; Lubert Stryer Internat. 7. ed. New York Freeman [u.a.] 2012 Getr. Zählung zahlr. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Hier auch später erschienene, unveränderte Nachdrucke. - Erg. bildet: Student companion to accompany Biochemistry Physiologische Chemie (DE-588)4076124-1 gnd rswk-swf Biochemie (DE-588)4006777-4 gnd rswk-swf 1\p (DE-588)4151278-9 Einführung gnd-content 2\p (DE-588)4123623-3 Lehrbuch gnd-content Biochemie (DE-588)4006777-4 s DE-604 Physiologische Chemie (DE-588)4076124-1 s 3\p DE-604 Tymoczko, John L. 1948-2019 Verfasser (DE-588)124601103 aut Stryer, Lubert 1938-2024 Verfasser (DE-588)124601197 aut Digitalisierung UB Regensburg application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=021174175&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis 1\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk 2\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk 3\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk |
spellingShingle | Berg, Jeremy M. 1958- Tymoczko, John L. 1948-2019 Stryer, Lubert 1938-2024 Biochemistry Physiologische Chemie (DE-588)4076124-1 gnd Biochemie (DE-588)4006777-4 gnd |
subject_GND | (DE-588)4076124-1 (DE-588)4006777-4 (DE-588)4151278-9 (DE-588)4123623-3 |
title | Biochemistry |
title_auth | Biochemistry |
title_exact_search | Biochemistry |
title_full | Biochemistry Jeremy M. Berg ; John L. Tymoczko ; Lubert Stryer |
title_fullStr | Biochemistry Jeremy M. Berg ; John L. Tymoczko ; Lubert Stryer |
title_full_unstemmed | Biochemistry Jeremy M. Berg ; John L. Tymoczko ; Lubert Stryer |
title_short | Biochemistry |
title_sort | biochemistry |
topic | Physiologische Chemie (DE-588)4076124-1 gnd Biochemie (DE-588)4006777-4 gnd |
topic_facet | Physiologische Chemie Biochemie Einführung Lehrbuch |
url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=021174175&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
work_keys_str_mv | AT bergjeremym biochemistry AT tymoczkojohnl biochemistry AT stryerlubert biochemistry |