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Introduction to enzyme and coenzyme chemistry / T.D.H. Bugg.

By: Bugg, TimMaterial type: TextTextPublication details: Chichester, West Sussex : Wiley, 2012. Edition: 3rd edDescription: 1 online resourceContent type: text Media type: computer Carrier type: online resourceISBN: 9781118348994; 1118348990; 9781118348963; 1118348966; 9781118348987; 1118348982; 9781118348970; 1118348974Subject(s): Enzymes | Coenzymes | MEDICAL -- Biochemistry | Coenzymes | EnzymesGenre/Form: Electronic books.Additional physical formats: Print version:: Introduction to enzyme and coenzyme chemistry.DDC classification: 612/.0151 LOC classification: QP601Online resources: Wiley Online Library
Contents:
2.6 The folded tertiary structure of proteins2.7 Enzyme structure and function; 2.8 Metallo-enzymes; 2.9 Membrane-associated enzymes; 2.10 Glycoproteins; 3 Enzymes Are Wonderful Catalysts; 3.1 Introduction; 3.2 A thermodynamic model of catalysis; 3.3 Proximity effects; 3.4 The importance of transition state stabilisation; 3.5 Acid/base catalysis in enzymatic reactions; 3.6 Nucleophilic catalysis in enzymatic reactions; 3.7 The use of strain energy in enzyme catalysis; 3.8 Desolvation of substrate and active site nucleophiles; 3.9 Catalytic perfection.
3.10 The involvement of protein dynamics in enzyme catalysis4 Methods for Studying Enzymatic Reactions; 4.1 Introduction; 4.2 Enzyme purification; 4.3 Enzyme kinetics; 4.4 The stereochemical course of an enzymatic reaction; 4.5 The existence of intermediates in enzymatic reactions; Direct observation; Trapping; Chemical inference; Isotope exchange; 4.6 Analysis of transition states in enzymatic reactions; 4.7 Determination of active site catalytic groups; 5 Hydrolytic and Group Transfer Enzymes; 5.1 Introduction; 5.2 The peptidases; The Serine Proteases; The Cysteine Proteases.
The Metallo-proteasesThe Aspartyl Proteases; CASE STUDY: HIV-1 protease; 5.3 Esterases and lipases; 5.4 Acyl transfer reactions in biosynthesis (coenzyme A); 5.5 Enzymatic phosphoryl transfer reactions; 5.6 Adenosine 5'-triphosphate (ATP); 5.7 Enzymatic glycosyl transfer reactions; 5.8 Methyl group transfer: use of S-adenosyl methionine and tetrahydrofolate coenzymes for one-carbon transfers; 6 Enzymatic Redox Chemistry; 6.1 Introduction; 6.2 Nicotinamide adenine dinucleotide-dependent dehydrogenases; 6.3 Flavin-dependent dehydrogenases and oxidases; 6.4 Flavin-dependent mono-oxygenases.
Summary: Looking at enzymes from an organic chemistry perspective, this updated reference includes information on recent advances in our understanding of enzyme action; topical examples to illustrate key points; two-color figures of the active sites of enzymes discussed in the text to illustrate the interplay between enzyme structure and function; and end-of-chapter problems to allow readers to check their understanding of the material. This concise but comprehensive guide is essential for undergraduate and postgraduate students of organic, bio-organic, and medicinal chemistry, chemical biology, bioche.
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Includes bibliographical references and index.

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2.6 The folded tertiary structure of proteins2.7 Enzyme structure and function; 2.8 Metallo-enzymes; 2.9 Membrane-associated enzymes; 2.10 Glycoproteins; 3 Enzymes Are Wonderful Catalysts; 3.1 Introduction; 3.2 A thermodynamic model of catalysis; 3.3 Proximity effects; 3.4 The importance of transition state stabilisation; 3.5 Acid/base catalysis in enzymatic reactions; 3.6 Nucleophilic catalysis in enzymatic reactions; 3.7 The use of strain energy in enzyme catalysis; 3.8 Desolvation of substrate and active site nucleophiles; 3.9 Catalytic perfection.

3.10 The involvement of protein dynamics in enzyme catalysis4 Methods for Studying Enzymatic Reactions; 4.1 Introduction; 4.2 Enzyme purification; 4.3 Enzyme kinetics; 4.4 The stereochemical course of an enzymatic reaction; 4.5 The existence of intermediates in enzymatic reactions; Direct observation; Trapping; Chemical inference; Isotope exchange; 4.6 Analysis of transition states in enzymatic reactions; 4.7 Determination of active site catalytic groups; 5 Hydrolytic and Group Transfer Enzymes; 5.1 Introduction; 5.2 The peptidases; The Serine Proteases; The Cysteine Proteases.

The Metallo-proteasesThe Aspartyl Proteases; CASE STUDY: HIV-1 protease; 5.3 Esterases and lipases; 5.4 Acyl transfer reactions in biosynthesis (coenzyme A); 5.5 Enzymatic phosphoryl transfer reactions; 5.6 Adenosine 5'-triphosphate (ATP); 5.7 Enzymatic glycosyl transfer reactions; 5.8 Methyl group transfer: use of S-adenosyl methionine and tetrahydrofolate coenzymes for one-carbon transfers; 6 Enzymatic Redox Chemistry; 6.1 Introduction; 6.2 Nicotinamide adenine dinucleotide-dependent dehydrogenases; 6.3 Flavin-dependent dehydrogenases and oxidases; 6.4 Flavin-dependent mono-oxygenases.

Looking at enzymes from an organic chemistry perspective, this updated reference includes information on recent advances in our understanding of enzyme action; topical examples to illustrate key points; two-color figures of the active sites of enzymes discussed in the text to illustrate the interplay between enzyme structure and function; and end-of-chapter problems to allow readers to check their understanding of the material. This concise but comprehensive guide is essential for undergraduate and postgraduate students of organic, bio-organic, and medicinal chemistry, chemical biology, bioche.

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