{"product_id":"introduction-to-enzyme-and-coenzyme-chemistry-isbn-9781119995951","title":"Introduction to Enzyme and Coenzyme Chemistry","description":"\u003cp\u003eEnzymes 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.\u003c\/p\u003e \u003cp\u003eThe popular textbook \u003ci\u003eIntroduction to Enzyme and Coenzyme Chemistry\u003c\/i\u003e 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.\u003c\/p\u003e \u003cp\u003eThis 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.\u003c\/p\u003e \u003cp\u003ePreface ix\u003c\/p\u003e \u003cp\u003eRepresentation of Protein Three-dimensional Structures x\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 From Jack Beans to Designer Genes 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e1.1 Introduction 1\u003c\/p\u003e \u003cp\u003e1.2 The discovery of enzymes 1\u003c\/p\u003e \u003cp\u003e1.3 The discovery of coenzymes 3\u003c\/p\u003e \u003cp\u003e1.4 The commercial importance of enzymes in biosynthesis and biotechnology 3\u003c\/p\u003e \u003cp\u003e1.5 The importance of enzymes as targets for drug discovery 6\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 All Enzymes Are Proteins 7\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction 7\u003c\/p\u003e \u003cp\u003e2.2 The structures of the L-α-amino acids 7\u003c\/p\u003e \u003cp\u003e2.3 The primary structure of polypeptides 9\u003c\/p\u003e \u003cp\u003e2.4 Alignment of amino acid sequences 11\u003c\/p\u003e \u003cp\u003e2.5 Secondary structures found in proteins 12\u003c\/p\u003e \u003cp\u003e2.6 The folded tertiary structure of proteins 15\u003c\/p\u003e \u003cp\u003e2.7 Enzyme structure and function 17\u003c\/p\u003e \u003cp\u003e2.8 Metallo-enzymes 20\u003c\/p\u003e \u003cp\u003e2.9 Membrane-associated enzymes 21\u003c\/p\u003e \u003cp\u003e2.10 Glycoproteins 23\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Enzymes Are Wonderful Catalysts 26\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 26\u003c\/p\u003e \u003cp\u003e3.2 A thermodynamic model of catalysis 28\u003c\/p\u003e \u003cp\u003e3.3 Proximity effects 30\u003c\/p\u003e \u003cp\u003e3.4 The importance of transition state stabilisation 32\u003c\/p\u003e \u003cp\u003e3.5 Acid\/base catalysis in enzymatic reactions 36\u003c\/p\u003e \u003cp\u003e3.6 Nucleophilic catalysis in enzymatic reactions 40\u003c\/p\u003e \u003cp\u003e3.7 The use of strain energy in enzyme catalysis 44\u003c\/p\u003e \u003cp\u003e3.8 Desolvation of substrate and active site nucleophiles 45\u003c\/p\u003e \u003cp\u003e3.9 Catalytic perfection 46\u003c\/p\u003e \u003cp\u003e3.10 The involvement of protein dynamics in enzyme catalysis 47\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Methods for Studying Enzymatic Reactions 50\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction 50\u003c\/p\u003e \u003cp\u003e4.2 Enzyme purification 50\u003c\/p\u003e \u003cp\u003e4.3 Enzyme kinetics 52\u003c\/p\u003e \u003cp\u003e4.4 The stereochemical course of an enzymatic reaction 59\u003c\/p\u003e \u003cp\u003e4.5 The existence of intermediates in enzymatic reactions 64\u003c\/p\u003e \u003cp\u003e4.6 Analysis of transition states in enzymatic reactions 68\u003c\/p\u003e \u003cp\u003e4.7 Determination of active site catalytic groups 71\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Hydrolytic and Group Transfer Enzymes 77\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction 77\u003c\/p\u003e \u003cp\u003e5.2 The peptidases 79\u003c\/p\u003e \u003cp\u003eCASE STUDY: HIV-1 protease 90\u003c\/p\u003e \u003cp\u003e5.3 Esterases and lipases 92\u003c\/p\u003e \u003cp\u003e5.4 Acyl transfer reactions in biosynthesis (coenzyme A) 93\u003c\/p\u003e \u003cp\u003e5.5 Enzymatic phosphoryl transfer reactions 95\u003c\/p\u003e \u003cp\u003e5.6 Adenosine 5 ′ -triphosphate (ATP) 101\u003c\/p\u003e \u003cp\u003e5.7 Enzymatic glycosyl transfer reactions 102\u003c\/p\u003e \u003cp\u003e5.8 Methyl group transfer: use of S-adenosyl methionine and tetrahydrofolate coenzymes for one-carbon transfers 107\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Enzymatic Redox Chemistry 115\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction 115\u003c\/p\u003e \u003cp\u003e6.2 Nicotinamide adenine dinucleotide-dependent dehydrogenases 117\u003c\/p\u003e \u003cp\u003e6.3 Flavin-dependent dehydrogenases and oxidases 122\u003c\/p\u003e \u003cp\u003e6.4 Flavin-dependent mono-oxygenases 128\u003c\/p\u003e \u003cp\u003e6.5 CASE STUDY: Glutathione and trypanothione reductases 129\u003c\/p\u003e \u003cp\u003e6.6 Deazaflavins and pterins 133\u003c\/p\u003e \u003cp\u003e6.7 Iron-sulphur clusters 135\u003c\/p\u003e \u003cp\u003e6.8 Metal-dependent mono-oxygenases 136\u003c\/p\u003e \u003cp\u003e6.9 -Ketoglutarate-dependent dioxygenases 140\u003c\/p\u003e \u003cp\u003e6.10 Non-heme iron-dependent dioxygenases 141\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Enzymatic Carbon–Carbon Bond Formation 148\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction 148\u003c\/p\u003e \u003cp\u003eCarbon–carbon bond formation via carbanion equivalents 149\u003c\/p\u003e \u003cp\u003e7.2 Aldolases 149\u003c\/p\u003e \u003cp\u003eCASE STUDY: Fructose 1,6-bisphosphate aldolase 150\u003c\/p\u003e \u003cp\u003e7.3 Claisen enzymes 153\u003c\/p\u003e \u003cp\u003e7.4 Assembly of fatty acids and polyketides 156\u003c\/p\u003e \u003cp\u003e7.5 Carboxylases: Use of biotin 158\u003c\/p\u003e \u003cp\u003e7.6 Ribulose bisphosphate carboxylase\/oxygenase (Rubisco) 161\u003c\/p\u003e \u003cp\u003e7.7 Vitamin K-dependent carboxylase 163\u003c\/p\u003e \u003cp\u003e7.8 Thiamine pyrophosphate-dependent enzymes 165\u003c\/p\u003e \u003cp\u003eCarbon–carbon bond formation via carbocation intermediates 168\u003c\/p\u003e \u003cp\u003e7.9 Terpene cyclases 168\u003c\/p\u003e \u003cp\u003eCarbon–carbon formation through radical intermediates 173\u003c\/p\u003e \u003cp\u003e7.10 Phenolic radical couplings 173\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Enzymatic Addition\/Elimination Reactions 181\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction 181\u003c\/p\u003e \u003cp\u003e8.2 Hydratases and dehydratases 182\u003c\/p\u003e \u003cp\u003e8.3 Ammonia lyases 187\u003c\/p\u003e \u003cp\u003e8.4 Elimination of phosphate and pyrophosphate 190\u003c\/p\u003e \u003cp\u003e8.5 CASE STUDY: 5-Enolpyruvyl shikimate 3-phosphate (EPSP) synthase 191\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Enzymatic Transformations of Amino Acids 197\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction 197\u003c\/p\u003e \u003cp\u003e9.2 Pyridoxal 5 ′ -phosphate-dependent reactions at the α-position 197\u003c\/p\u003e \u003cp\u003e9.3 CASE STUDY: Aspartate aminotransferase 201\u003c\/p\u003e \u003cp\u003e9.4 Reactions at the β- and γ-positions of amino acids 204\u003c\/p\u003e \u003cp\u003e9.5 Serine hydroxymethyltransferase 206\u003c\/p\u003e \u003cp\u003e9.6 N-Pyruvoyl-dependent amino acid decarboxylases 208\u003c\/p\u003e \u003cp\u003e9.7 Imines and enamines in alkaloid biosynthesis 208\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Isomerases 213\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction 213\u003c\/p\u003e \u003cp\u003e10.2 Cofactor-independent racemases and epimerases 213\u003c\/p\u003e \u003cp\u003e10.3 Keto-enol tautomerases 216\u003c\/p\u003e \u003cp\u003e10.4 Allylic isomerases 217\u003c\/p\u003e \u003cp\u003e10.5 CASE STUDY: Chorismate mutase 219\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Radicals in Enzyme Catalysis 225\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction 225\u003c\/p\u003e \u003cp\u003e11.2 Vitamin B 12 -dependent rearrangements 225\u003c\/p\u003e \u003cp\u003e11.3 The involvement of protein radicals in enzyme catalysis 229\u003c\/p\u003e \u003cp\u003e11.4 S-adenosyl-methionine-dependent radical reactions 232\u003c\/p\u003e \u003cp\u003e11.5 Biotin synthase and sulphur insertion reactions 233\u003c\/p\u003e \u003cp\u003e11.6 Radical chemistry in DNA repair enzymes 234\u003c\/p\u003e \u003cp\u003e11.7 Oxidised amino acid cofactors and quinoproteins 238\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Non-Enzymatic Biological Catalysis 242\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e12.1 Introduction 242\u003c\/p\u003e \u003cp\u003e12.2 Catalytic RNA 242\u003c\/p\u003e \u003cp\u003e12.3 Catalytic antibodies 246\u003c\/p\u003e \u003cp\u003e12.4 Synthetic enzyme models 251\u003c\/p\u003e \u003cp\u003eAppendix 1: Cahn-Ingold-Prelog Rule for Stereochemical Nomenclature 258\u003c\/p\u003e \u003cp\u003eAppendix 2: Amino Acid Abbreviations 260\u003c\/p\u003e \u003cp\u003eAppendix 3: A Simple Demonstration of Enzyme Catalysis 261\u003c\/p\u003e \u003cp\u003eAppendix 4: Answers to Problems 263\u003c\/p\u003e \u003cp\u003eIndex 271\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e“Summing Up: Recommended.  Lower-and upper-division undergraduates.”  (\u003ci\u003eChoice\u003c\/i\u003e, 1 April 2013)\u003c\/p\u003e \u003cb\u003eProfessor Timothy Bugg\u003c\/b\u003e, Department of Chemistry, University of Warwick, UK\u003cbr\u003eProfessor Bugg is Professor of Biological Chemistry at the University of Warwick. Following his PhD studies with Dr C. Abell at the University of Cambridge he spent two years as a SERC\/NATO postdoctoral research fellow in the laboratory of Professor CT Walsh at Harvard Medical School. In 1991 he began his academic career as a lecturer in organic chemistry at the University of Southampton, before moving to Warwick in 1999. His research interests are in the study of enzyme mechanisms, principally enzymes involved in the bacterial degradation of aromatic compounds, and enzymes involved in bacterial peptidoglycan biosynthesis. He has published approximately 100 journal publications since 1988, is the author of \"An Introduction to Enzyme and Coenzyme Chemistry\" (2 editions), and a contributor to \"Comprehensive Natural Products Chemistry\", and \"Encyclopaedia of Chemical Biology\" (for which he is on the Advisory Board).  \u003cp\u003eEnzymes 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.\u003c\/p\u003e \u003cp\u003eThe popular textbook \u003ci\u003eIntroduction to Enzyme and Coenzyme Chemistry\u003c\/i\u003e 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.\u003c\/p\u003e \u003cp\u003eThis 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.\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":47989459681509,"sku":"NP9781119995951","price":146.0,"currency_code":"USD","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/1842\/7735\/files\/9781119995951.jpg?v=1761784185","url":"https:\/\/k12savings.com\/products\/introduction-to-enzyme-and-coenzyme-chemistry-isbn-9781119995951","provider":"K12savings","version":"1.0","type":"link"}