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Beta-Lactamases
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Editors: Jean-Marie Frre (Universite de Liege, Centre for Protein Engineering, Belgium)
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 (-lactamase II, BcII or II) 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 -lactamase. This seemed to open the floodgates and several class A -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 -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 -lactamases and Perspectives in Drug Design;pp. 79-101
(Johan Wouters and Cdric Bauvois, University of Namur, Belgium and others)

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

Part 2: Kinetics, Mechanisms, Inhibitors and Inactivation

Chapter 6. Kinetics of -lactamases in Theory and in Practice;pp. 139-160
(Jean-Marie Frre,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 -lactamases from Nuclear Magnetic Resonance Studies;pp. 199-216
(Christian Damblon and Gordon Roberts,University of Leicester,UK)

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

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

Chapter 11. -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 -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 Frre,Universita degli Studi di Siena,Italy and others)

Part 4: Β-Lactamases as Model Enzymes and Tools

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

Chapter 18. Random Mutagenesis as a Probe of -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
(Andr 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 -lactamases for the Benefits of Biochemical Research;pp. 479-503
(Marylne Vandevenne, Moreno Galleni and Patrice File,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 Frre,Universite de Liege,Belgium)

Index;pp. 515-537

   Series:
      Molecular Anatomy and Physiology of Proteins - Vladimir N. Uversky (Indiana University of Medicine, USA), Series Editor
   Binding: Hardcover
   Pub. Date: 2012- December
   Pages: 546, 7 x 10 (NBC - C) 537pp.
   ISBN: 978-1-61324-638-2
   Status: AV
  
Status Code Description
AN Announcing
FM Formatting
PP Page Proofs
FP Final Production
EP Editorial Production
PR At Prepress
AP At Press
AV Available
  
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