Book Description:
The activity of a bacterial enzyme ¡°able to degrade penicillin¡± had first been described in 1940, even before the exact structure of penicillin was elucidated and, by 1970, several enzymes had been purified to homogeneity, the amino acid sequence of a staphylococcal penicillinase was also known and that of its Bacillus licheniformis counterpart was well under way. By contrast, their catalytic mechanism remained quite mysterious. A Zn++ metallo-beta-lactamase (¦Â-lactamase II, BcII or ¦ÂII) had also been described as soon as 1967 and later purified. It was thus surprising that the first mechanistic information demonstrating the presence of a penicillin-binding serine residue was obtained with a penicillin-sensitive DD-peptidase rather than a ¦Â-lactamase. This seemed to open the floodgates and several class A ¦Â-lactamases were then rapidly shown to be active-site serine enzymes. This book presents current research in the study of beta-lactamases. (Imprint: Nova)

Table of Contents:
Preface ix

Foreword xv

Chapter 1 Before Our Time: Early ß-Lactamase Papers and the People Who Wrote Them;pp. 1-18
(James R. Knox,The University of Connecticut, Storrs,USA)

Part 1: Structural Data

Chapter 2. Structure of Class a Beta-Lactamases;pp. 21-39
(Wladimir Sougakoff, Universite Pierre et Marie Curie,Sorbonne Universities,Paris,France)

Chapter 3. X-ray Structures and Mechanisms of Metallo--lactamases;pp. 41-77
(Carine Bebrone, Gianpiero Garau, Isabel Garcia-Saez, Laurent Chantalat, Andrea Carfi and Otto Dideberg,Universite de Liege,Belgique)

Chapter 4. Structures of Class C ß -lactamases and Perspectives in Drug Design;pp. 79-101
(Johan Wouters and Cédric Bauvois, University of Namur, Belgium and others)

Chapter 5. Structures of Class D ß - lactamase;pp. 103-135
(Frédéric Kerff, Eric Sauvage, Lionel Vercheval and Paulette Charlier,University of Leige,Belgium)

Part 2: Kinetics, Mechanisms, Inhibitors and Inactivation

Chapter 6. Kinetics of ß -lactamases in Theory and in Practice;pp. 139-160
(Jean-Marie Frère,University of Lieg,Belgium)

Chapter 7. The Mechanisms of Catalysis by -Lactamases;pp. 161-198
(Anthony L. Fink and Michael I. Page,University of California,Santa Cruz,USA and others)

Chapter 8. Insights into the Mechanisms of ß-lactamases from Nuclear Magnetic Resonance Studies;pp. 199-216
(Christian Damblon and Gordon Roberts,University of Leicester,UK)

Chapter 9. ß-Lactams as Inhibitors of ß-Lactamases;pp. 217-258
(John D. Buynak, Southern Methodist University, Dallas,TX,USA)

Chapter 10. ß-Lactamase Inhibitors: Non--Lactams;pp. 259-292
(Rex F. Pratt,Wesleyan University, Middletown,CT.USA)

Chapter 11. ß-Lactamase Inhibitory Proteins;pp. 293-314
(Michael Gretes, Susan Jensen and Natalie Strynadka,University of British Columbia,Vancouver,Canada and others)

Chapter 12. Quantum Chemistry Applied to the Study of the ß-lactamases;pp. 315-340
(Dominique Dehareng and Georges Dive,Centre for Protein Engineering, Institut de Chimie,Liege,Belgium)

Part 3: Clinical Aspects

Chapter 13. Emergence of Completely New Sequences;pp. 343-367
(Roger Labia and Patrice Nordmann,Universite Europeenne de Bretagne,Quimper,France and others)

Chapter 14. Emergence of New Phenotypes Mediated by Amino Acid Substitutions in -Lactamases;pp. 369-382
(George Jacoby and Karen Bush,Lahey Clinic,Burlington, MA,USA and others)

Chapter 15. The Clinical Problem of Beta-lactam Resistance in Multidrug Resistant (MDR) Klebsiella Pneumoniae, Acinetobacter Baumannii, and Pseudomonas Aeruginosa;pp. 383-399
(Robert A. Bonomo,Louis Stokes Cleveland Dept. of Veterans Affairs Medical Center,Case Western Reserve University School of Medicine,Cleveland,Ohio,USA)

Chapter 16. Interplay between β-lactamase Activity, Outer Membrane Permeability and Active Efflux System;pp. 401-418
(Jean-Denis Docquier, Gian Maria Rossolini, Hiroshi Nikaido and Jean-Marie Frère,Universita degli Studi di Siena,Italy and others)

Part 4: Β-Lactamases as Model Enzymes and Tools

Chapter 17. The Induction of ß-lactamases in Eubacteria;pp. 421-435
(Bernard Joris and Jean Dusart,Universite de Liege,Belgium)

Chapter 18. Random Mutagenesis as a Probe of ß -lactamase Structure, Function and Evolution;pp. 437-457
(Jacques Fastrez and Timothy Palzkill,Universite catholique de Louvain,Belgium and others)

Chapter 19. Folding and Stability of Class A β-Lactamases;pp. 459-477
(André Matagne and Roger H. Pai,Universiti de Liege,Belgium and others)

Chapter 20. How to Make Good Use of a “Bad” Enzyme: Utilization of Efficient ß-lactamases for the Benefits of Biochemical Research;pp. 479-503
(Marylène Vandevenne, Moreno Galleni and Patrice Filée,University of Liege,Belgium)

Part 5: Other Βeta-Lactamases

Chapter 21. Are there Unknown Classes of -lactamases? Sensitivity of β-lactams to Nucleophilic Agents and other Enzymes;pp. 507-514
(Stephane Baurin, Xavier Henry, Nathalie Hoyez and Jean-Marie Frère,Universite de Liege,Belgium)

Index;pp. 515-537