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Enzymatic Reaction Mechanisms [Hardback]

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, (both in the Department of Biochemistry, University of Wisconsin)
  • Formāts: Hardback, 848 pages, height x width x depth: 216x282x33 mm, weight: 3016 g, 122 halftones, 532 line illus., 401 2-color illus.
  • Izdošanas datums: 01-Mar-2007
  • Izdevniecība: Oxford University Press Inc
  • ISBN-10: 0195122585
  • ISBN-13: 9780195122589
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  • Formāts: Hardback, 848 pages, height x width x depth: 216x282x33 mm, weight: 3016 g, 122 halftones, 532 line illus., 401 2-color illus.
  • Izdošanas datums: 01-Mar-2007
  • Izdevniecība: Oxford University Press Inc
  • ISBN-10: 0195122585
  • ISBN-13: 9780195122589
Citas grāmatas par šo tēmu:
Frey and Hegemon (both: biochemistry, U. of Wisconsin-Madison) examine the chemical mechanisms of enzymatic catalysis. After reviewing the fundamentals of the science, they focus on specific types of enzymatic reactions, discussing the underlying chemistry and providing brief case studies exemplifying enzymes in that particular class of enzymes. Among these reactions and classes are isomerization, addition and elimination, nitrogen and sulfur tranferases, oxidoreductases, and complex enzymes. Touches of color appear throughout. Annotation ©2007 Book News, Inc., Portland, OR (booknews.com)

Books dealing with the mechanisms of enzymatic reactions were written a generation ago. They included volumes entitled Bioorganic Mechanisms, I and II by T.C. Bruice and S.J. Benkovic, published in 1965, the volume entitled Catalysis in Chemistry and Enzymology by W.P. Jencks in 1969, and the volume entitled Enzymatic Reaction Mechanisms by C.T. Walsh in 1979. The Walsh book was based on the course taught by W.P. Jencks and R.H. Abeles at Brandeis University in the 1960's and 1970's. By the late 1970's, much more could be included about the structures of enzymes and the kinetics and mechanisms of enzymatic reactions themselves, and less emphasis was placed on chemical models. Walshs book was widely used in courses on enzymatic mechanisms for many years. Much has happened in the field of mechanistic enzymology in the past 15 to 20 years. Walshs book is both out-of-date and out-of-focus in todays world of enzymatic mechanisms. There is no longer a single volume or a small collection of volumes to which students can be directed to obtain a clear understanding of the state of knowledge regarding the chemicals mechanisms by which enzymes catalyze biological reactions. There is no single volume to which medicinal chemists and biotechnologists can refer on the subject of enzymatic mechanisms. Practitioners in the field have recognized a need for a new book on enzymatic mechanisms for more than ten years, and several, including Walsh, have considered undertaking to modernize Walshs book. However, these good intentions have been abandoned for one reason or another. The great size of the knowledge base in mechanistic enzymology has been a deterrent. It seems too large a subject for a single author, and it is difficult for several authors to coordinate their work to mutual satisfaction. This text by Perry A. Frey and Adrian D. Hegeman accomplishes this feat, producing the long-awaited replacement for Walshs classic text.
Enzymes and Catalytic Mechanisms
1(68)
Catalysis and the Active Site
1(2)
Rate Enhancement in Enzymatic Catalysis
3(2)
Conformational Mobility in Catalysis
5(4)
Substrate-Induced Conformational Changes
5(1)
Catalysis of Multistep Reactions
6(1)
Structural Mobility in Enzymes
6(3)
Acid-Base Catalysis
9(7)
Acids and Bases
9(2)
Acid- and Base-Catalyzed Reactions
11(5)
Nucleophilic Catalysis
16(5)
Electrophilic Catalysis
21(9)
Catalysis of Enolization
21(2)
Imine Formation by Lysine
23(3)
Catalysis by Metal Ions
26(4)
Hydrogen Bonding
30(4)
Strong and Weak Hydrogen Bonds
30(2)
Hydrogen Bonding in Catalysis
32(2)
Binding Energy in Catalysis
34(19)
Binding and Activation Energy
34(2)
The Active Site as an Entropy Trap
36(4)
Dissecting the Binding Effect in Enzymatic Action
40(1)
Stabilization of the Transition State
41(5)
Binding the Near Attack Conformation
46(2)
Destabilization of Ground States
48(1)
Rate Enhancement through Binding of Remote Groups
48(5)
Characterization of Active Sites
53(9)
Competitive Inhibitors: Analogs of Substrates
53(1)
Group-Selective Chemical Modification
53(4)
Site-Directed Mutagenesis
57(2)
Affinity Labeling
59(3)
Why Are Enzymes Large Molecules?
62(7)
Sizes of Enzymatic Binding Domains
62(1)
Catalytic Antibodies
63(6)
Kinetics of Enzymatic Reactions
69(60)
Steady-State Kinetics
69(22)
One-Substrate Reactions
70(4)
Two-Substrate Reactions
74(15)
Three-Substrate Reactions
89(2)
Isotope Effects
91(10)
Classes of Isotope Effects
91(4)
Measurement of Isotope Effects
95(6)
Transient-Phase Kinetics
101(10)
Reaction Characteristics
101(1)
Transient Methods
102(9)
pH-Rate Profiles
111(6)
Profile Interpretation
111(1)
Measurements of pH-Rate Profiles
111(6)
Allosteric Regulation
117(12)
Theory
118(2)
Binding Equations for Cooperative Systems
120(3)
Aspartate Transcarbamoylase
123(6)
Coenzymes I: Organic Coenzymes
129(60)
Nicotinamide Coenzymes
129(12)
Structures and Functions of Nicotinamide Coenzymes
129(3)
Stereospecificity of Hydride Transfer
132(2)
NAD+ as a Coenzyme
134(7)
Thiamine Pyrophosphate
141(6)
Structure
141(1)
Reaction Mechanism
141(6)
α-Lipoamide
147(1)
Pyridoxal-5'-Phosphate
148(10)
Enzymatic Reactions Facilitated by Pyridoxal-5'-Phosphate
149(1)
Pyridoxal-5'-Phosphate-Stabilized Amino Acid Carbanions
149(2)
Mechanisms of Pyridoxal-5'-Phosphate-Dependent Reactions
151(7)
Flavin Coenzymes
158(5)
Structures of Flavin Coenzymes
158(1)
Mechanisms of Flavin Catalysis
159(4)
Biotin
163(2)
Structure and Role as a Carboxyl Carrier
163(1)
Chemistry of Biotin and N1-Carboxybiotin
164(1)
Mechanism of Biotin-Dependent Carboxylation
164(1)
Phosphopantetheine Coenzymes
165(2)
Structures of Phosphopantetheine Coenzymes
165(1)
Mechanism of Phosphopantetheine Action
165(2)
Folate Compounds
167(5)
Folate Compounds of One-Carbon Metabolism
168(2)
Enzymes in Tetrahydrofolate Metabolism
170(1)
Biological Importance of Folate
171(1)
Amino Acid--Based Coenzymes
172(17)
Pyruvoyl Decarboxylases
172(1)
Methylidene Imidazolinone--Dependent Deaminases
173(1)
Quinoproteins
174(15)
Coenzymes II: Metallic Coenzymes
189(64)
Vitamin B12 Coenzymes
190(11)
Chemistry of B12 Coenzymes
190(3)
Adenosylcobalamin-Dependent Enzymes
193(6)
Methylcobalamin-Dependent Enzymes
199(2)
Heme Coenzymes
201(9)
Chemistry of Oxygen and Heme
201(3)
Heme Enzymes
204(5)
Oxygen Binding and Electron Transfer
209(1)
Mononuclear Nonheme Iron
210(7)
Monooxygenases
210(7)
Dioxygenases
217(1)
Oxo-Fe2 Complexes
217(5)
Structures
218(1)
Reactions of Di-iron Enzymes
219(3)
Metallopterin Enzymes
222(5)
Molybdopterin and Tungstopterin
222(5)
Iron-Sulfur Centers
227(7)
Structures
227(3)
Catalytic Functions
230(4)
S-Adenosylmethionine and Iron-Sulfur Centers
234(3)
Catalytic Action of S-Adenosylmethionine and [ 4Fe--4S] Centers
234(2)
Stoichiometric Reactions of S-Adenosylmethionine and [ 4Fe--4S] Centers
236(1)
Divalent Metal Ions
237(3)
Electrostatic Activation of Coordinated Water
237(1)
Electrostatic Activation of Enolization
238(2)
Copper as a Cofactor
240(3)
Copper Proteins
240(1)
Other Copper Enzymes
241(2)
Nickel Coenzymes
243(4)
Nickel in Methanogenesis
243(2)
Other Nickel Coenzymes
245(2)
Long-Range Electron Transfer
247(6)
Biological Electron Transfer
247(1)
Marcus Theory
248(5)
Enzyme Inhibition
253(44)
Two-Substrate Analogs
254(1)
Inhibition and Binding
254(1)
PALA and Aspartate Transcarbamylase
254(1)
Suicide Inactivation
255(13)
Thymidylate Synthase
255(5)
β-Hydroxydecanoyl Thioester Dehydratase
260(2)
γ-Aminobutyrate Aminotransferase
262(6)
Kinetics of Slow-Binding and Tight-Binding Inhibition
268(2)
Slow Binding
268(1)
Tight Binding
269(1)
Slow-Binding Inhibition
270(10)
Dihydrofolate Reductase
271(3)
Prostaglandin H Synthase
274(6)
Tight-Binding Inhibition
280(17)
HMG-CoA Reductase
280(5)
Alanine Racemase
285(4)
5-Enolpyruvoylshikimate-3-Phosphate Synthase
289(2)
Acetylcholinesterase
291(6)
Acyl Group Transfer: Proteases and Esterases
297(36)
Chemistry of Acyl Transfer
297(3)
Serine Proteases
300(14)
Chymotrypsin
301(10)
Subtilisin
311(3)
Cysteine Proteases
314(3)
Papain
315(2)
Caspases
317(1)
Aspartic Proteases
317(6)
Molecular Properties
318(2)
Mechanism of Action
320(3)
Metalloproteases
323(5)
Carboxypeptidase A
324(3)
Thermolysin
327(1)
Esterases
328(5)
Structure and Function
328(1)
Phospholipase A2
329(4)
Isomerization
333(54)
Aldose and Ketose Isomerases
333(8)
Chemistry
333(1)
Phosphoglucose Isomerase
334(1)
Triosephosphate Isomerase
335(6)
Xylose Isomerase
341(1)
Phosphomutases
341(5)
α-Phosphoglucomutase
341(2)
β-Phosphoglucomutase
343(1)
Phosphoglycerate Mutases
343(3)
Racemases and Epimerases
346(18)
Proline Racemase
346(4)
Glutamate Racemase
350(2)
Mandelate Racemase
352(3)
UDP-Galactose 4-Epimerase
355(5)
Ribulose-5-P 4-Epimerase
360(1)
UDP-N-Acetylglucosamine-2-Epimerase
361(3)
Chorismate Mutase
364(2)
Δ5-3-Ketosteroid Isomerase
366(2)
Radical Isomerizations
368(11)
Glutamate Mutase
369(2)
Methylmalonyl CoA Mutase
371(5)
Lysine 2,3-Aminomutase
376(3)
Newer Isomerases
379(8)
UDP-Galactopyranose Mutase
379(1)
Pseudouridine Synthase
379(8)
Decarboxylation and Carboxylation
387(46)
Chemistry of Decarboxylation and Carboxylation
387(1)
Decarboxylases
388(30)
Pyruvate Decarboxylase
389(5)
Amino Acid Decarboxylases
394(9)
Acetoacetate Decarboxylase
403(2)
Mevalonate Pyrophosphate Decarboxylase
405(2)
Radical-Based Decarboxylases
407(7)
Orotidine Monophosphate Decarboxylase
414(4)
Carboxylases
418(15)
Ribulose-1,5-Bisphosphate Carboxylase
419(6)
Phosphoenolpyruvate Carboxylase
425(1)
Vitamin K--Dependent Carboxylase
426(7)
Addition and Elimination
433(43)
α,β-Elimination/Addition Reactions
433(23)
Cofactor-Independent α,β-Elimination/Addition Reactions
434(6)
Cofactor-Dependent α,β-Elimination/Addition Reactions
440(16)
β,α-Elimination/Addition Reactions
456(6)
Methylidene Imidazolone--Dependent Elimination and Addition
456(6)
Carbonic Anhydrase
462(3)
Isomerization and Elimination
465(11)
Catalytic Process
465(1)
Coenzyme B12--Dependent Elimination
466(10)
Phosphotransfer and Nucleotidyltransfer
476(71)
Chemistry of Phosphoryl Group Transfer
476(11)
Phosphomonoesters
476(7)
Phosphodiesters
483(1)
Phosphotriesters
483(1)
Five-Member Ring Phosphoesters
484(3)
Enzymatic Phosphoryl Group Transfer
487(34)
Single and Double Displacements
487(2)
Phosphotransferases
489(13)
Protein Phosphorylation: Protein Kinase A
502(7)
Phosphomonoesterases
509(12)
Enzymatic Nucleotidyl Group Transfer
521(26)
Nucleotidyltransferases
521(18)
Phosphodiesterases
539(8)
ATP-Dependent Synthetases and Ligases
547(22)
Ligation and the Energy of ATP
547(1)
Activation by Phosphorylation
548(11)
Glutamine Synthetase
548(6)
Carbamoyl Phosphate Synthetase
554(5)
Activation by Adenylylation
559(10)
DNA Ligase
559(2)
Aminoacyl-tRNA Synthetases
561(5)
Ubiquitin
566(3)
Glycosyl Group Transferases
569(28)
Chemical Mechanisms
570(5)
Chemistry of Glycoside Hydrolysis
570(3)
Enzymatic Glycosyl Transfer
573(2)
Glycosyltransferases
575(12)
Sucrose Phosphorylase
575(2)
Glycogen Phosphorylase
577(7)
Purine Nucleoside Phosphorylase
584(3)
Glycosidases
587(10)
Families and Structures
587(2)
Lysozyme
589(6)
T4 Lysozyme
595(2)
Nitrogen and Sulfur Transferases
597(20)
Nitrogen Transfer
597(12)
Aspartate Aminotransferase
597(5)
Tyrosine 2,3-Aminomutase
602(2)
Amidotransfer
604(3)
Glutamine: PRPP Amidotransferase
607(2)
Sulfur Transfer
609(8)
Biotin Synthase
611(1)
Lipoyl Synthase
612(5)
Carbon-Carbon Condensation and Cleavage
617(38)
Chemistry
617(2)
Enolization of Acetyl CoA
619(11)
Acetyl CoA in Ester Condensations
619(1)
Citrate Synthase
620(7)
Thiolases
627(3)
Carbanionic Mechanisms
630(15)
Transaldolase
631(3)
Transketolase
634(5)
Serine Hydroxymethyltransferase
639(6)
Carbocationic Mechanisms
645(10)
Farnesyl Pyrophosphate Synthase
645(3)
Squalene Synthase
648(7)
Alkyltransferases
655(24)
Chemistry of Alkylation
655(2)
Biological Alkylations
655(1)
Alkylation Mechanisms
656(1)
Enzymatic Alkylation
657(22)
Protein Farnesyltransferase
657(4)
Catechol O-Methyltransferase
661(4)
S-Adenosylmethionine Synthetase
665(5)
Methionine Synthases
670(9)
Oxidoreductases
679(31)
Pyridine Nucleotide--Dependent Dehydrogenases
680(14)
Alcohol Dehydrogenase
680(6)
Lactate Dehydrogenase
686(1)
Short-Chain Alcohol Dehydrogenases
687(3)
Glyceraldehyde-3-P Dehydrogenase
690(3)
Glutamate Dehydrogenase
693(1)
Disulfide Oxidoreductases
694(4)
Dihydrolipoyl Dehydrogenase
694(4)
Ribonucleotide Reductases
698(12)
Classes of Ribonucleotide Reductases
700(5)
Structural Relationships of Ribonucleotide Reductases
705(5)
Oxidases and Oxygenases
710(39)
Oxidases
710(12)
D-Amino Acid Oxidase
710(6)
Monoamine Oxidases
716(2)
Isopenicillin-N Synthase
718(3)
Urate Oxidase
721(1)
Monooxygenases
722(19)
Lactate Monooxygenase
722(1)
Cytochrome P450 Monooxygenases
722(5)
Iron-Methane Monooxygenase
727(5)
α-Ketoglutarate--Dependent Oxygenases
732(3)
Dopamine β-Monooxygenase
735(2)
Copper-Methane Monooxygenase
737(1)
Nitric Oxide Synthase
738(3)
Dioxygenases
741(8)
Intradiol Dioxygenases
741(3)
Extradiol Dioxygenases
744(5)
Complex Enzymes
749(54)
Multienzyme Complexes
750(7)
α-Ketoacid Dehydrogenase Complexes
750(1)
Pyruvate Dehydrogenase Complex
750(7)
Fatty Acid Synthesis
757(6)
Acetyl CoA Carboxylase
757(4)
Fatty Acid Synthases
761(2)
Modular Enzymes
763(5)
Polyketide Synthases
763(4)
Nonribosomal Polypeptide Synthetases
767(1)
Ribosomal Protein Synthesis
768(9)
RNA Polymerase
768(2)
The Ribosome
770(7)
Energy-Coupling Enzymes
777(26)
Nitrogenase
777(5)
Cytochrome c Oxidase
782(4)
ATP Synthase
786(6)
Myosin and Muscle Contraction
792(11)
Appendices
803(6)
Appendix A: Haldane Relationships for Some Kinetic Mechanisms
803(1)
Appendix B: Inhibition Patterns for Three-Substrate Kinetic Mechanisms
804(1)
Appendix C: Equations for Number of Occupied Sites in the Binding of a Ligand to a Multisite Macromolecule
804(1)
Appendix D: Derivation of Steady-State Kinetic Equations by the King-Altman Method
805(4)
Index 809