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
Sprache
Verlagsort
Verlagsgruppe
Elsevier Science & Techn.
Dateigröße
ISBN-13
978-0-323-97200-0 (9780323972000)
Schweitzer Klassifikation
List of contributorsAbout the editorsPrefacePart I Introduction1 Ureases: an overviewConrado Pedebos and Rodrigo Ligabue-Braun1.1 Introduction1.2 Structure and activation1.3 Relevance in health and technology1.4 ConclusionsReferencesPart II Historical aspects2 Historical hallmarks in urease studyPaula Bacaicoa Caruso and Rodrigo Ligabue-Braun2.1 Introduction2.2 From urea to urease: 1700-19002.3 Enzymes are proteins and they can have nickel: 1900-752.4 Structure-function(s) of urease: 1981currently2.5 Urease origins: notes on urease prehistoryReferences3 Genetics of plant urease, the enzyme that keeps surprising usJoe C. Polacco3.1 An innocent young man3.2 A quixotic quest: biological and biographical background3.3 The urease play, with a cast of "firsts"3.4 Nickel enters the fray3.5 Soybean urease isozymes enter the fray3.6 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 fray3.9 A urease-mediated insight into plant associations with bacteria3.10 Other nickel roles in the plant world?3.11 Are urea and NO children of the same parents?3.12 DedicationReferencesPart III Classes and special cases4 Microbial ureasesCelia Regina Carlini, Deiber Olivera-Severo and Rodrigo Ligabue-Braun4.1 Historical aspects and relevance of microbial ureases4.2 Structural organization of microbial ureases and evolution4.3 Genomic organization and expression regulation of bacterial ureases4.4 Urease-negative bacteria4.5 Beneficial roles of bacterial ureases4.6 Microbial ureases as virulence factors4.7 Nonenzymatic properties of three-chained ureases4.8 Concluding remarksReferences5 Plant ureases: biochemistry, structure, physiological functions, role of urease inhibitors, and urease applications in industrySandeep Kumar and Arvind M. Kayastha5.1 Introduction5.2 Historical milestones of urease5.3 Biochemistry of urea catalysis5.4 A Ubiquitous enzyme5.5 Structure of plant urease5.6 Urease inhibitors of agricultural interest5.7 Physiological role of urease in plants5.8 Nonenzymatic properties of plant ureases5.9 Applications of ureases5.10 ConclusionReferences6 Jack bean ureaseAnuradha Balasubramanian and Karthe Ponnuraj6.1 Introduction6.2 Role of plant urease6.3 Urease architecture6.4 Challenges in crystallizing jack bean urease6.5 Crystallization of JBU6.6 X-ray analysis of native and fluoride-inhibited JBU6.7 Structure determination of native and fluoride-inhibited JBU6.8 Structure of JBU monomer6.9 Oligomeric assembly6.10 Active site architecture of JBU6.11 Active site mobile flap6.12 Insecticidal activityAcknowledgmentReferences7 Fungal ureasesAlfred Botha and Barbra Toplis7.1 Introduction7.2 Producers of fungal ureases7.3 Environmental role of fungal ureases7.4 Fungal ureases as virulence factors7.5 The role of ureases in fungal cell metabolism7.6 ConclusionReferencesPart IV Activation, catalysis, inhibition8 Urease: structure, function, catalysis, and inhibitionLuca Mazzei, Francesco Musiani, Barbara Zambelli, Stefano Benini, Michele Cianci and Stefano Ciurli8.1 Introduction8.2 The three-dimensional architecture of ureases8.3 The active site of urease8.4 The urease operon8.5 The accessory proteins of urease8.6 The urease maturation process8.7 The catalytic mechanism8.8 The inhibition of ureaseReferences9 Inhibition of ureases: studies and applicationsRobert P. Hausinger9.1 Introduction: the importance of urease inhibitors and inactivators9.2 Proper design of urease inhibitor/inactivator studies9.3 Inhibitors that bind directly to the urease metallocenter9.4 Inactivators that react with the flexible protein flap covering the urease active site9.5 Other compounds that reduce urease activity9.6 ConclusionAcknowledgmentsReferences10 Nonenzymatic properties of ureasesMatheus V.C. Grahl, Augusto F. Uberti and Celia Regina Carlini10.1 Introduction10.2 Entomotoxic property of plant ureases10.
