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Structural and Functional Aspects of Enzyme Catalysis

32. Colloquium, 23. - 25. April 1981

  • Conference proceedings
  • © 1981

Overview

Editors:
  1. Hermann Eggerer

    1. Physiologisch-Chemisches Institut, Technische Universität, München 40, Germany

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    You can also search for this editor in PubMed   Google Scholar

  2. Robert Huber

    1. Max-Planck-Institut für Biochemie, Martinsried, Germany

    View editor publications

    You can also search for this editor in PubMed   Google Scholar

Part of the book series: Colloquium der Gesellschaft für Biologische Chemie in Mosbach Baden (MOSBACH, volume 32)

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Table of contents (19 papers)

  1. Front Matter

    Pages I-IX
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  2. Mechanism of Enzyme Action

    1. Front Matter

      Pages 1-1
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    2. Stereochemistry in Relation to Enzyme Mechanism

      • J. W. Cornforth
      Pages 3-16

    3. How Do Enzymes Work?

      • W. N. Lipscomb
      Pages 17-23

    4. Design of Synthetic Molecular Receptors and Catalysts

      • J. P. Behr, J. M. Lehn
      Pages 24-32

    5. Cyclodextrins as Catalysts

      • W. Saenger
      Pages 33-42

  3. Dynamics of Molecular Recognition

    1. Front Matter

      Pages 43-43
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    2. Dynamics of Molecular Recognition in Enzyme-Catalyzed Reactions

      • E. Neumann
      Pages 45-58

    3. NMR in the Study of Enzyme Catalysis

      • H. Rüterjans
      Pages 59-62

    4. The Study of Enzyme Reactions at Subzero Temperatures

      • P. Douzou
      Pages 63-72

  4. Function of Metals in Enzymes: Thermophilic Enzymes

    1. Front Matter

      Pages 73-73
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    2. Active Site Metals as Probes of Local Conformation and Function of Enzymes

      • B. Vallee
      Pages 75-95

    3. Selenoenzymes

      • T. C. Stadtman
      Pages 96-103

    4. The Structure of the Selenoenzyme GSH Peroxidase

      • R. Ladenstein, O. Epp, A. Wendel
      Pages 104-113

    5. Structure and Function of Thermophilic Enzymes

      • H. Zuber
      Pages 114-127

  5. Biological and Chemical Modifications of Enzymes

    1. Front Matter

      Pages 129-129
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    2. Specific Enzyme Inactivators in Vitro and in Vivo

      • R. R. Rando
      Pages 131-135

    3. Correlation of Amino Acid Sequence with Inhibitor Activity and Specificity of Protein Inhibitors of Serine Proteinases

      • M. Laskowski Jr., M. W. Empie, I. Kato, W. J. Kohr, W. Ardelt, W. C. Bogard Jr. et al.
      Pages 136-152

    4. Human Latent PMN Leukocyte Collagenase and Regulation of Activity via Disulfide-Thiol Interchange as Catalyzed by the Glutathione Cycle

      • H. Tschesche, H. W. Macartney
      Pages 153-162

    5. The Neural and Hormonal Control of Glycogen Metabolism in Mammalian Skeletal Muscle

      • P. Cohen
      Pages 163-174
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Keywords

About this book

Enzymes perform the executive role in growth, energy conversion, and repair of a living organism. Their activity is adjusted to their en­ vironment within the cell, being turned off, switched on, or finely tuned by specific metabolites according to demands at the physiologi­ cal level. Each enzyme discovered in the long history of enzymology has revealed its own individuality. Even closely related members of a family differ in specificity, stability or regulatory properties. Despite these, at first sight overwhelming aspects of individuality, common factors of enzymic reactions have been recognized. Enzymes are stereospecific catalysts even when a nonspecific process would yield the same product. Knowledge of the detailed stereochemistry of an enzymic reaction helps to deduce reaction mechanisms and to ob­ tain insight into the specific binding of substrates at the active site. This binding close to catalytically competent groups is related to the enormous speed of enzyme-catalyzed reactions. The physical ba­ sis of rate-enhancement is understood in principle and further exploit­ ed in the design of small organic receptor molecules as model enzymes. These aspects of enzyme catalysis are discussed in Session 1. Session 2 emphasizes the dynamic aspects of enzyme substrate inter­ action. Substrate must diffuse from solution space to the enzyme's surface. This process is influenced and can be greatly facilitated by certain electrostatic propterties of enzymes. The dynamic events during catalysis are studied by relaxation kinetics or NMR techniques.

Editors and Affiliations

  • Physiologisch-Chemisches Institut, Technische Universität, München 40, Germany

    Hermann Eggerer

  • Max-Planck-Institut für Biochemie, Martinsried, Germany

    Robert Huber

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