Description
Ureases: Foundations, Classes, and Applications provides a thorough, practical analysis of ureases—enzymes of growing relevance across a range of biotechnological applications and drug discovery. Unique in many aspects, ureases are one of the few enzymes to have nickel in their active sites. Ureases covers all aspects of this enzymatic class. Starting with foundational overview, the book discusses historical urease research and the current state, from basic biochemistry to the use of ureases as hallmarks in enzymology, crystallography, and bioinorganic chemistry. The different classes of ureases, structurally diverse but chemically equivalent, are individually discussed. The multi-protein, multi-step activation of ureases (with chemical modification of residues, transport, and transfer of nickel ions) are examined in-depth, along with the catalytic mechanisms of ureolysis and its inhibitors. The final two sections of the book address multiple applications of ureases in health and biotechnology, respectively, going from gastric ulcer treatment to architectural uses in buildings and engineering. Future applications and next steps in research are also considered.- Considers fundamental aspects of urease biochemistry, ureolysis and urease inhibitors- Discusses urease research across a range of applications, from drug discovery to biosensors, water purification, architecture and the food industry- Features chapter contributions from international leaders in the field
Table of Contents
List of contributors About the editors Preface Part I Introduction 1 Ureases: an overview Conrado Pedebos and Rodrigo Ligabue-Braun 1.1 Introduction 1.2 Structure and activation 1.3 Relevance in health and technology 1.4 Conclusions References Part II Historical aspects 2 Historical hallmarks in urease study Paula Bacaicoa Caruso and Rodrigo Ligabue-Braun 2.1 Introduction 2.2 From urea to urease: 1700-1900 2.3 Enzymes are proteins and they can have nickel: 1900-75 2.4 Structure-function(s) of urease: 1981currently 2.5 Urease origins: notes on urease prehistory References 3 Genetics of plant urease, the enzyme that keeps surprising us Joe C. Polacco 3.1 An innocent young man 3.2 A quixotic quest: biological and biographical background 3.3 The urease play, with a cast of "firsts" 3.4 Nickel enters the fray 3.5 Soybean urease isozymes enter the fray 3.6 Nickel insertion proteins enter the fray (in vitro activation of soybean urease) 3.7 Does urea enter the fray? Of course, but from which tissues? 3.8 Dueling metabolic precursors of urea enter the fray 3.9 A urease-mediated insight into plant associations with bacteria 3.10 Other nickel roles in the plant world? 3.11 Are urea and NO children of the same parents? 3.12 Dedication References Part III Classes and special cases 4 Microbial ureases Celia Regina Carlini, Deiber Olivera-Severo and Rodrigo Ligabue-Braun 4.1 Historical aspects and relevance of microbial ureases 4.2 Structural organization of microbial ureases and evolution 4.3 Genomic organization and expression regulation of bacterial ureases 4.4 Urease-negative bacteria 4.5 Beneficial roles of bacterial ureases 4.6 Microbial ureases as virulence factors 4.7 Nonenzymatic properties of three-chained ureases 4.8 Concluding remarks References 5 Plant ureases: biochemistry, structure, physiological functions, role of urease inhibitors, and urease applications in industry Sandeep Kumar and Arvind M. Kayastha 5.1 Introduction 5.2 Historical milestones of urease 5.3 Biochemistry of urea catalysis 5.4 A Ubiquitous enzyme 5.5 Structure of plant urease 5.6 Urease inhibitors of agricultural interest 5.7 Physiological role of urease in plants 5.8 Nonenzymatic properties of plant ureases 5.9 Applications of ureases 5.10 Conclusion References 6 Jack bean urease Anuradha Balasubramanian and Karthe Ponnuraj 6.1 Introduction 6.2 Role of plant urease 6.3 Urease architecture 6.4 Challenges in crystallizing jack bean urease 6.5 Crystallization of JBU 6.6 X-ray analysis of native and fluoride-inhibited JBU 6.7 Structure determination of native and fluoride-inhibited JBU 6.8 Structure of JBU monomer 6.9 Oligomeric assembly 6.10 Active site architecture of JBU 6.11 Active site mobile flap 6.12 Insecticidal activity Acknowledgment References 7 Fungal ureases Alfred Botha and Barbra Toplis 7.1 Introduction 7.2 Producers of fungal ureases 7.3 Environmental role of fungal ureases 7.4 Fungal ureases as virulence factors 7.5 The role of ureases in fungal cell metabolism 7.6 Conclusion References Part IV Activation, catalysis, inhibition 8 Urease: structure, function, catalysis, and inhibition Luca Mazzei, Francesco Musiani, Barbara Zambelli, Stefano Benini, Michele Cianci and Stefano Ciurli 8.1 Introduction 8.2 The three-dimensional architecture of ureases 8.3 The active site of urease 8.4 The urease operon 8.5 The accessory proteins of urease 8.6 The urease maturation process 8.7 The catalytic mechanism 8.8 The inhibition of urease References 9 Inhibition of ureases: studies and applications Robert P. Hausinger 9.1 Introduction: the importance of urease inhibitors and inactivators 9.2 Proper design of urease inhibitor/inactivator studies 9.3 Inhibitors that bind directly to the urease metallocenter 9.4 Inactivators that react with the flexible protein flap covering the urease active site 9.5 Other compounds that reduce urease activity 9.6 Conclusion Acknowledgments References 10 Nonenzymatic properties of ureases Matheus V.
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