Enzymes

Enzymes

Biochemistry, Biotechnology, Clinical Chemistry

2nd Edition - April 4, 2007

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  • Authors: T Palmer, P L Bonner
  • eBook ISBN: 9780857099921

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Description

In recent years, there have been considerable developments in techniques for the investigation and utilisation of enzymes. With the assistance of a co-author, this popular student textbook has been updated to include techniques such as membrane chromatography, aqueous phase partitioning, engineering recombinant proteins for purification and due to the rapid advances in bioinformatics/proteomics, a discussion of the analysis of complex protein mixtures by 2D-electrophoresis and RPHPLC prior to sequencing by mass spectroscopy. Written with the student firmly in mind, no previous knowledge of biochemistry, and little of chemistry, is assumed. It is intended to provide an introduction to enzymology, and a balanced account of all the various theoretical and applied aspects of the subject which are likely to be included in a course.

Key Features

  • Provides an introduction to enzymology and a balanced account of the theoretical and applied aspects of the subject
  • Discusses techniques such as membrane chromatography, aqueous phase partitioning and engineering recombinant proteins for purification
  • Includes a discussion of the analysis of complex protein mixtures by 2D-electrophoresis and RPHPLC prior to sequencing by mass spectroscopy

Readership

Undergraduate students

Table of Contents

  • Part 1: Structure and Function of Enzymes

    1: An Introduction to Enzymes

    • 1.1 WHAT ARE ENZYMES?
    • 1.2 A BRIEF HISTORY OF ENZYMES
    • 1.3 THE NAMING AND CLASSIFICATION OF ENZYMES
    • SUMMARY OF CHAPTER 1
    • PROBLEMS

    2: The Structure of Proteins

    • 2.1 INTRODUCTION
    • 2.2 AMINO ACIDS, THE BUILDING BLOCKS OF PROTEINS
    • 2.3 THE BASIS OF PROTEIN STRUCTURE
    • 2.4 THE DETERMINATION OF PRIMARY STRUCTURE
    • 2.5 THE DETERMINATION OF PROTEIN STRUCTURE BY X-RAY CRYSTALLOGRAPHY
    • 2.6 THE INVESTIGATION OF PROTEIN STRUCTURE IN SOLUTION
    • SUMMARY OF CHAPTER 2
    • PROBLEMS

    3: The Biosynthesis and Properties of Proteins

    • 3.1 THE BIOSYNTHESIS OF PROTEINS
    • 3.2 THE PROPERTIES OF PROTEINS
    • SUMMARY OF CHAPTER 3
    • PROBLEMS

    4: Specificity of Enzyme Action

    • 4.1 TYPES OF SPECIFICITY
    • 4.2 THE ACTIVE SITE
    • 4.3 THE FISCHER ‘LOCK-AND-KEY’ HYPOTHESIS
    • 4.4 THE KOSHLAND ‘INDUCED-FIT’ HYPOTHESIS
    • 4.5 HYPOTHESES INVOLVING STRAIN OR TRANSITION-STATE STABILIZATION
    • 4.6 FURTHER COMMENTS ON SPECIFICITY
    • SUMMARY OF CHAPTER 4

    5: Monomeric and Oligomeric Enzymes

    • 5.1 MONOMERIC ENZYMES
    • 5.2 OLIGOMERIC ENZYMES
    • SUMMARY OF CHAPTER 5

    Part 2: Kinetic and Chemical Mechanisms of Enzyme-Catalysed Reactions

    6: An Introduction to Bioenergetics, Catalysis and Kinetics

    • 6.1 SOME CONCEPTS OF BIOENERGETICS
    • 6.2 FACTORS AFFECTING THE RATES OF CHEMICAL REACTIONS
    • 6.3 KINETICS OF UNCATALYSED CHEMICAL REACTIONS
    • 6.4 KINETICS OF ENZYME-CATALYSED REACTIONS: AN HISTORICAL INTRODUCTION
    • 6.5 METHODS USED FOR INVESTIGATING THE KINETICS OF ENZYME-CATALYSED REACTIONS
    • 6.6 THE NATURE OF ENZYME CATALYSIS
    • SUMMARY OF CHAPTER 6
    • PROBLEMS

    7: Kinetics of Single-Substrate Enzyme-Catalysed Reactions

    • 7.1 THE RELATIONSHIP BETWEEN INITIAL VELOCITY AND SUBSTRATE CONCENTRATION
    • 7.2 RAPID-REACTION kINETICS
    • 7.3 THE kING AND ALTMAN PROCEDURE
    • SUMMARY OF CHAPTER 7
    • PROBLEMS

    8: Enzyme Inhibition

    • 8.1 INTRODUCTION
    • 8.2 REVERSIBLE INHIBITION
    • 8.3 IRREVERSIBLE INHIBITION
    • SUMMARY OF CHAPTER 8
    • PROBLEMS

    9: Kinetics of Multi-Substrate Enzyme-Catalysed Reactions

    • 9.1 EXAMPLES OF POSSIBLE MECHANISMS
    • 9.2 STEADY-STATE KINETICS
    • 9.3 INVESTIGATION OF REACTION MECHANISMS USING STEADY-STATE METHODS
    • 9.4 INVESTIGATION OF REACTION MECHANISMS USING NON-STEADY-STATE METHODS
    • SUMMARY OF CHAPTER 9
    • PROBLEMS

    10: The Investigation of Active Site Structure

    • 10.1 THE IDENTIFICATION OF BINDING SITES AND CATALYTIC SITES
    • 10.2 THE INVESTIGATION OF THE THREE-DIMENSIONAL STRUCTURES OF ACTIVE SITES
    • SUMMARY OF CHAPTER 10
    • PROBLEM

    11: The chemical nature of enzyme catalysis

    • 11.1 AN INTRODUCTION TO REACTION MECHANISMS IN ORGANIC CHEMISTRY
    • 11.2 MECHANISMS OF CATALYSIS
    • 11.3 MECHANISMS OF REACTIONS CATALYSED BY ENZYMES WITHOUT COFACTORS
    • 11.4 METAL-ACTIVATED ENZYMES AND METALLOENZYMES
    • 11.5 THE INVOLVEMENT OF COENZYMES IN ENZYME-CATALYSED REACTIONS
    • SUMMARY OF CHAPTER 11

    12: The Binding of Ligands to Proteins

    • 12.1 INTRODUCTION
    • 12.2 THE BINDING OF A LIGAND TO A PROTEIN HAVING A SINGLE LIGAND-BINDING SITE
    • 12.3 COOPERATIVITY
    • 12.4 POSITIVE HOMOTROPIC COOPERATIVITY AND THE HILL EQUATION
    • 12.5 THE ADAIR EQUATION FOR THE BINDING OF A LIGAND TO A PROTEIN HAVING TWO BINDING SITES FOR THAT LIGAND
    • 12.6 THE ADAIR EQUATION FOR THE BINDING OF A LIGAND TO A PROTEIN HAVING THREE BINDING SITES FOR THAT LIGAND
    • 12.7 THE ADAIR EQUATION FOR THE BINDING OF A LIGAND TO A PROTEIN HAVING FOUR BINDING SITES FOR THAT LIGAND
    • 12.8 INVESTIGATION OF COOPERATIVE EFFECTS
    • 12.9 THE BINDING OF OXYGEN TO HAEMOGLOBIN
    • SUMMARY OF CHAPTER 12
    • PROBLEMS

    13: Sigmoidal Kinetics and Allosteric Enzymes

    • 13.1 INTRODUCTION
    • 13.2 THE MONOD-WYMAN-CHANGEUX (MWC) MODEL
    • 13.3 THE KOSHLAND-NÉMETHY-FILMER (KNF) MODEL
    • 13.4 DIFFERENTIATION BETWEEN MODELS FOR COOPERATIVE BINDING IN PROTEINS
    • 13.5 SIGMOIDAL KINETICS IN THE ABSENCE OF COOPERATIVE BINDING
    • SUMMARY OF CHAPTER 13
    • PROBLEMS

    14: The Significance of Sigmoidal Behaviour

    • 14.1 THE PHYSIOLOGICAL IMPORTANCE OF COOPERATIVE OXYGEN-BINDING BY HΔEMOGLOBIN
    • 14.2 ALLOSTERIC ENZYMES AND METABOLIC REGULATION
    • SUMMARY OF CHAPTER 14

    Part 3: Application of Enzymology

    15: Investigation of Enzymes in Biological Preparations

    • 15.1 CHOICE OF PREPARATION FOR THE INVESTIGATION OF ENZYME CHARACTERISTICS
    • 15.2 ENZYME ASSAY
    • 15.3 INVESTIGATION OF SUB-CELLULAR COMPARTMENTATION OF ENZYMES
    • SUMMARY OF CHAPTER 15
    • PROBLEM

    16: Extraction and Purification of Enzymes

    • 16.1 EXTRACTION OF ENZYMES
    • 16.2 PURIFICATION OF ENZYMES
    • 16.3 DETERMINATION OF MOLECULAR WEIGHTS OF ENZYMES
    • SUMMARY OF CHAPTER 16
    • PROBLEM

    17: Enzymes as Analytical Reagents

    • 17.1 THE VALUE OF ENZYMES AS ANALYTICAL REAGENTS
    • 17.2 PRINCIPLES OF ENZYMATIC ANALYSIS
    • 17.3 HANDLING ENZYMES AND COENZYMES
    • SUMMARY OF CHAPTER 17
    • PROBLEMS

    18: Instrumental Techniques Available for Use in Enzymatic Analysis

    • 18.1 PRINCIPLES OF THE AVAILABLE DETECTION TECHNIQUES
    • 18.2 AUTOMATION IN ENZYMATIC ANALYSIS
    • 18.3 HIGH-THROUGHPUT ASSAYS (HTA)
    • SUMMARY OF CHAPTER 18

    19: Applications of Enzymatic Analysis in Medicine, Forensic Science and Industry

    • 19.1 APPLICATIONS IN MEDICINE
    • 19.2 APPLICATIONS IN FORENSIC SCIENCE
    • 19.3 APPLICATIONS IN INDUSTRY
    • SUMMARY OF CHAPTER 19

    20: Biotechnological Applications of Enzymes

    • 20.1 LARGE-SCALE PRODUCTION AND PURIFICATION OF ENZYMES
    • 20.2 IMMOBILIZED ENZYMES
    • 20.3 ENZYME UTILIZATION IN INDUSTRY
    • SUMMARY OF CHAPTER 20
    • PROBLEMS

    21: Genomics, Proteomics and Bioinformatics

    • 21.1 ENZYMES AND RECOMBINANT DNA TECHNOLOGY
    • 21.2 PROTEOMICS
    • 21.3 ENZYMES AND BIOINFORMATICS
    • SUMMARY OF CHAPTER 21
    • PROBLEMS

    Answers to Problems
    Abbreviations

Product details

  • No. of pages: 432
  • Language: English
  • Copyright: © Woodhead Publishing 2007
  • Published: April 4, 2007
  • Imprint: Woodhead Publishing
  • eBook ISBN: 9780857099921

About the Authors

T Palmer

P L Bonner

Affiliations and Expertise

Nottingham Trent University, UK

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