Introduction to Enzyme and Coenzyme Chemistry, 3rd Edition

Klappentext Enzymes are giant macromolecules which catalyse biochemical reactions. They are remarkable in many ways. Their three-dimensional structures are highly complex, yet they are formed by spontaneous folding of a linear polypeptide chain. Their catalytic properties are far more impressive than synthetic catalysts which operate under more extreme conditions. Each enzyme catalyses a single chemical reaction on a particular chemical substrate with very high enantioselectivity and enantiospecificity at rates which approach "catalytic perfection". Living cells are capable of carrying out a huge repertoire of enzyme-catalysed chemical reactions, some of which have little or no precedent in organic chemistry.The popular textbook Introduction to Enzyme and Coenzyme Chemistry has been thoroughly updated to include information on the most recent advances in our understanding of enzyme action, with additional recent examples from the literature used to illustrate key points. A major new feature is the inclusion of two-colour figures, and the addition of over 40 new figures of the active sites of enzymes discussed in the text, in order to illustrate the interplay between enzyme structure and function.This new edition provides a concise but comprehensive account from the perspective of organic chemistry, what enzymes are, how they work, and how they catalyse many of the major classes of enzymatic reactions, and will continue to prove invaluable to both undergraduate and postgraduate students of organic, bio-organic and medicinal chemistry, chemical biology, biochemistry and biotechnology. Zusammenfassung Enzymes are giant macromolecules which catalyse biochemical reactions. They are remarkable in many ways. Their three-dimensional structures are highly complex, yet they are formed by spontaneous folding of a linear polypeptide chain. Inhaltsverzeichnis Preface ixRepresentation of Protein Three-Dimensional Structures x1 From Jack Beans to Designer Genes 11.1 Introduction 11.2 The discovery of enzymes 11.3 The discovery of coenzymes 31.4 The commercial importance of enzymes in biosynthesis and biotechnology 31.5 The importance of enzymes as targets for drug discovery 62 All Enzymes Are Proteins 72.1 Introduction 72.2 The structures of the L-alpha-amino acids 72.3 The primary structure of polypeptides 92.4 Alignment of amino acid sequences 112.5 Secondary structures found in proteins 122.6 The folded tertiary structure of proteins 152.7 Enzyme structure and function 172.8 Metallo-enzymes 202.9 Membrane-associated enzymes 212.10 Glycoproteins 233 Enzymes Are Wonderful Catalysts 263.1 Introduction 263.2 A thermodynamic model of catalysis 283.3 Proximity effects 303.4 The importance of transition state stabilisation 323.5 Acid/base catalysis in enzymatic reactions 363.6 Nucleophilic catalysis in enzymatic reactions 403.7 The use of strain energy in enzyme catalysis 443.8 Desolvation of substrate and active site nucleophiles 453.9 Catalytic perfection 463.10 The involvement of protein dynamics in enzyme catalysis 474 Methods for Studying Enzymatic Reactions 504.1 Introduction 504.2 Enzyme purification 504.3 Enzyme kinetics 524.4 The stereochemical course of an enzymatic reaction 594.5 The existence of intermediates in enzymatic reactions 644.6 Analysis of transition states in enzymatic reactions 684.7 Determination of active site catalytic groups 715 Hydrolytic and Group Transfer Enzymes 775.1 Introduction 775.2 The peptidases 79CASE STUDY: HIV-1 protease 905.3 Esterases and lipases 925.4 Acyl transfer reactions in biosynthesis (coenzyme A) 935.5 Enzymatic phosphoryl transfer reactions 955.6 Adenosine 5'-triphosphate (ATP) 1015.7 Enzymatic glycosyl transfer reactions 1025.8 Methyl group transfer: use of S-adenosyl methionine and tetrahydrofolatecoenzymes for one-carbon transfers 1076 Enzymatic Redox Chemistry...

List of contents

Preface ix
 
Representation of Protein Three-Dimensional Structures x
 
1 From Jack Beans to Designer Genes 1
 
1.1 Introduction 1
 
1.2 The discovery of enzymes 1
 
1.3 The discovery of coenzymes 3
 
1.4 The commercial importance of enzymes in biosynthesis and biotechnology 3
 
1.5 The importance of enzymes as targets for drug discovery 6
 
2 All Enzymes Are Proteins 7
 
2.1 Introduction 7
 
2.2 The structures of the L-alpha-amino acids 7
 
2.3 The primary structure of polypeptides 9
 
2.4 Alignment of amino acid sequences 11
 
2.5 Secondary structures found in proteins 12
 
2.6 The folded tertiary structure of proteins 15
 
2.7 Enzyme structure and function 17
 
2.8 Metallo-enzymes 20
 
2.9 Membrane-associated enzymes 21
 
2.10 Glycoproteins 23
 
3 Enzymes Are Wonderful Catalysts 26
 
3.1 Introduction 26
 
3.2 A thermodynamic model of catalysis 28
 
3.3 Proximity effects 30
 
3.4 The importance of transition state stabilisation 32
 
3.5 Acid/base catalysis in enzymatic reactions 36
 
3.6 Nucleophilic catalysis in enzymatic reactions 40
 
3.7 The use of strain energy in enzyme catalysis 44
 
3.8 Desolvation of substrate and active site nucleophiles 45
 
3.9 Catalytic perfection 46
 
3.10 The involvement of protein dynamics in enzyme catalysis 47
 
4 Methods for Studying Enzymatic Reactions 50
 
4.1 Introduction 50
 
4.2 Enzyme purification 50
 
4.3 Enzyme kinetics 52
 
4.4 The stereochemical course of an enzymatic reaction 59
 
4.5 The existence of intermediates in enzymatic reactions 64
 
4.6 Analysis of transition states in enzymatic reactions 68
 
4.7 Determination of active site catalytic groups 71
 
5 Hydrolytic and Group Transfer Enzymes 77
 
5.1 Introduction 77
 
5.2 The peptidases 79
 
CASE STUDY: HIV-1 protease 90
 
5.3 Esterases and lipases 92
 
5.4 Acyl transfer reactions in biosynthesis (coenzyme A) 93
 
5.5 Enzymatic phosphoryl transfer reactions 95
 
5.6 Adenosine 5'-triphosphate (ATP) 101
 
5.7 Enzymatic glycosyl transfer reactions 102
 
5.8 Methyl group transfer: use of S-adenosyl methionine and tetrahydrofolate
 
coenzymes for one-carbon transfers 107
 
6 Enzymatic Redox Chemistry 115
 
6.1 Introduction 115
 
6.2 Nicotinamide adenine dinucleotide-dependent dehydrogenases 117
 
6.3 Flavin-dependent dehydrogenases and oxidases 122
 
6.4 Flavin-dependent mono-oxygenases 128
 
6.5 CASE STUDY: Glutathione and trypanothione reductases 129
 
6.6 Deazaflavins and pterins 133
 
6.7 Iron-sulphur clusters 135
 
6.8 Metal-dependent mono-oxygenases 136
 
6.9 alpha-Ketoglutarate-dependent dioxygenases 140
 
6.10 Non-heme iron-dependent dioxygenases 141
 
7 Enzymatic Carbon-Carbon Bond Formation 148
 
7.1 Introduction 148
 
Carbon-carbon bond formation via carbanion equivalents 149
 
7.2 Aldolases 149
 
CASE STUDY: Fructose 1,6-bisphosphate aldolase 150
 
7.3 Claisen enzymes 153
 
7.4 Assembly of fatty acids and polyketides 156
 
7.5 Carboxylases: Use of biotin 158
 
7.6 Ribulose bisphosphate carboxylase/oxygenase (Rubisco) 161
 
7.7 Vitamin K-dependent carboxylase 163
 
7.8 Thiamine pyrophosphate-dependent enzymes 165
 
Carbon-carbon bond formation via carbocation intermediates 168
 
7.9 Terpene cyclases 168
 
Carbon-carbon formation t

Report

"Summing Up: Recommended. Lower-and upper-division undergraduates." ( Choice , 1 April 2013)

Product details

• Authors: T. D. H. Bugg, Timothy Bugg, Bugg T. D. H.
• Publisher: Wiley, John and Sons Ltd
• Languages: English
• Product format: Hardback
• Released: 20.07.2012
• EAN: 9781119995951
• ISBN: 978-1-119-99595-1
• No. of pages: 296
• Dimensions: 173 mm x 251 mm x 17 mm
• Subjects: Natural sciences, medicine, IT, technology > Technology > Chemical engineering; Chemie, Biochemie, Enzyme, Katalyse, chemistry, Catalysis, Bioorganic Chemistry, Enzyme u. Rezeptoren, Enzymes & Receptors, Bioorganische Chemie