{"product_id":"introduction-to-enzyme-and-coenzyme-chemistry-9781119995951","title":"Introduction to Enzyme and Coenzyme Chemistry","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\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.\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTrade Review\u003c\/b\u003e\u003cbr\u003e\u003cp\u003e“Summing Up: Recommended.  Lower-and upper-division undergraduates.”  (\u003ci\u003eChoice\u003c\/i\u003e, 1 April 2013)\u003c\/p\u003e\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003e\u003ci\u003ePreface ix\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003ci\u003eRepresentation of Protein Three-Dimensional Structures x\u003c\/i\u003e\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\u003c\/p\u003e \u003cp\u003ecoenzymes 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 α-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 B12-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\u003e\u003cb\u003eAppendix 1: Cahn-Ingold-Prelog Rule for Stereochemical Nomenclature 258\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eAppendix 2: Amino Acid Abbreviations 260\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eAppendix 3: A Simple Demonstration of Enzyme Catalysis 261\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eAppendix 4: Answers to Problems 263\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eIndex 271\u003c\/b\u003e\u003c\/p\u003e","brand":"Wiley-Blackwell","offers":[{"title":"Default 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