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Carbonic Anhydrases as Biocatalysts: From Theory to Medical and Industrial Applications [Kietas viršelis]

Edited by (Full Professor, University of Florence, Neuroscience, Psychology, Medicine and Child Health, Florence, Italy), Edited by (Institute of Biostructures and Bioimaging (IBB) of the Italian National Research Council, Napoli, Italy)
  • Formatas: Hardback, 398 pages, aukštis x plotis: 235x191 mm, weight: 900 g, 50 illustrations; Illustrations, unspecified
  • Išleidimo metai: 08-Jan-2015
  • Leidėjas: Elsevier Science Ltd
  • ISBN-10: 0444632581
  • ISBN-13: 9780444632586
Kitos knygos pagal šią temą:
Carbonic Anhydrases as Biocatalysts: From Theory to Medical and Industrial ApplicationsDidesnis paveikslėlis
  • Formatas: Hardback, 398 pages, aukštis x plotis: 235x191 mm, weight: 900 g, 50 illustrations; Illustrations, unspecified
  • Išleidimo metai: 08-Jan-2015
  • Leidėjas: Elsevier Science Ltd
  • ISBN-10: 0444632581
  • ISBN-13: 9780444632586
Kitos knygos pagal šią temą:
Pastovi nuoroda: https://www.kriso.lt/db/9780444632586.html

Carbonic anhydrases (CAs, EC 4.2.1.1) are ubiquitous metalloenzymes, present throughout most living organisms and encoded by five evolutionarily unrelated gene families.The Carbonic Anhydrases as Biocatalysts: From Theory to Medical and Industrial Applications presents information on the growing interest in the study of this enzyme family and their applications to both medicine and biotechnology.

  • Offers comprehensive coverage of the carbonic anhydrases enzyme family and their properties as biocatalysts
  • Includes current applications of carbonic anhydrases in biotechnology on the basis of their catalytic efficiency, including new technologies for CO2 capture processes
  • Identifies new targets for drug design studies
  • Provides a selectivity profile for the different carbonic anhydrases and their related biomedical applications

Daugiau informacijos

An exhaustive description of the carbonic anhydrase enzyme family focusing attention on their main medical and biotechnological applications
List of Contributors
xi
Preface xv
PART 1 INTRODUCTION
1(14)
1 Carbonic Anhydrases: An Overview
3(12)
Claudiu T. Supuran
Giuseppina De Simone
1.1 Carbonic anhydrase families
3(2)
1.2 Catalytic features
5(2)
1.3 CA inhibition and activation
7(3)
1.4 Biomedical applications of the CAs
10(1)
1.5 Biotechnological applications of the CAs
11(4)
References
11(4)
PART 2 CARBONIC ANHYDRASES AS DRUG TARGETS
15(274)
2 Human Carbonic Anhydrases: Catalytic Properties, Structural Features, and Tissue Distribution
17(14)
Katia D'Ambrosio
Giuseppina De Simone
Claudiu T. Supuran
2.1 Introduction
17(2)
2.2 hCAs' structural features
19(3)
2.3 hCAs' catalytic features
22(3)
2.4 hCAs' tissue distribution and their role as drug targets
25(6)
References
26(5)
3 Carbonic Anhydrase I
31(20)
Nicolino Pala
Roberta Cadoni
Mario Sechi
3.1 Introduction
31(1)
3.2 Structure of CA I
32(2)
3.3 Tissue localization and physiological functions
34(1)
3.4 CA I as pharmacological target
34(2)
3.5 CA I inhibitors
36(7)
3.6 CA I activators
43(2)
3.7 Conclusions and perspectives
45(6)
Acknowledgment
45(1)
References
46(5)
4 Carbonic Anhydrase II as Target for Drug Design
51(40)
Claudiu T. Supuran
Clemente Capasso
Giuseppina De Simone
4.1 Introduction
51(2)
4.2 Biochemical properties, genetic relationship with the other cytosolic isoforms, and 3D structure of hCA II
53(2)
4.3 hCA II inhibitors
55(3)
4.4 Antiglaucoma agents
58(8)
4.5 Diuretics with CA inhibitory properties
66(6)
4.6 Agents for the management of altitude sickness
72(1)
4.7 Various pharmacological actions connected with CA II inhibition: serendipity or off-targeting with impressive efficacy?
72(4)
4.8 CA II inhibitors in the management of tumors?
76(1)
4.9 New strategies to design CA II--selective inhibitors
77(4)
4.10 CA II activation
81(1)
4.11 Conclusions
82(9)
References
84(7)
5 Carbonic Anhydrase III
91(18)
Brian P. Mahon
Robert McKenna
5.1 Introduction
91(1)
5.2 Discovery of CA III
92(1)
5.3 Physiological role of CA III
92(2)
5.4 Molecular characterization of CA III
94(1)
5.5 Catalytic properties and proton transfer of CA III
95(4)
5.6 CA III as a biomarker: role in disease states
99(3)
5.7 CA III as a drug target
102(7)
Acknowledgment
105(1)
References
105(4)
6 Carbonic Anhydrase IV
109(16)
Abdul Waheed
William S. Sly
6.1 Introduction
109(2)
6.2 Genomic organization and chromosomal localization of human CA IV
111(1)
6.3 Cloning and molecular characterization of human CA IV
111(1)
6.4 Structure/function: the role of disulfide bonds
112(1)
6.5 Characterization of catalytic properties of human CA IV and its inhibition by sulfonamide inhibitors
113(1)
6.6 Expression of CA IV in different tissues
114(2)
6.7 Physiological functions of CA IV
116(9)
Acknowledgments
121(1)
References
121(4)
7 The Structure, Physiological Role, and Potential Medicinal Applications of Carbonic Anhydrase V
125(14)
Atilla Akdemir
Ozlen Guzel-Akdemir
7.1 Introduction
125(1)
7.2 Physiological role and potential medicinal applications of hCA VA and hCA VB
126(3)
7.3 Selective ligands for carbonic anhydrase V
129(2)
7.4 Sequence and three-dimensional structures of CA V isozymes
131(5)
7.5 Final remarks
136(3)
References
136(3)
8 Secreted Carbonic Anhydrase Isoenzyme VI
139(12)
Jukka Leinonen
Seppo Parkkila
8.1 Introduction
139(1)
8.2 CA VI structure
140(1)
8.3 Catalytic properties of CA VI
141(1)
8.4 CA VI In salivary glands, saliva, and oral cavity
141(1)
8.5 CA VI in mammary glands and milk
142(1)
8.6 CA VI in esophagus and lower alimentary tract
143(1)
8.7 CA VI in respiratory tract
144(1)
8.8 CA VI in other organ systems
144(1)
8.9 Potential medical applications
145(1)
8.10 Conclusions and future prospects
145(6)
References
145(6)
9 Carbonic Anhydrase VII
151(18)
Simona M. Monti
Claudiu T. Supuran
Giuseppina De Simone
Anna Di Fiore
9.1 Introduction
151(1)
9.2 Kinetic and structural features of hCA VII
152(3)
9.3 hCA VII and oxidative stress
155(1)
9.4 The role of the CA VII in epileptogenesis and neuropathic pain
156(1)
9.5 Inhibitors of hCA VII
157(7)
9.6 Conclusions
164(5)
References
164(5)
10 Tumor-Associated Carbonic Anhydrases IX and XII
169(38)
Elena Ondriskova
Michaela Debreova
Silvia Pastorekova
10.1 Introduction
169(1)
10.2 History
170(1)
10.3 Structure of CA IX and CA XII
171(2)
10.4 Tissue distribution and subcellular localization
173(3)
10.5 Regulation of CA IX expression
176(5)
10.6 Regulation of CA XII expression
181(3)
10.7 Role of CA IX and CA XII in tumor biology
184(4)
10.8 Clinical significance
188(3)
10.9 CA IX and CA XII targeted therapy
191(2)
10.10 Conclusion
193(14)
Acknowledgments
194(1)
References
194(13)
11 Carbonic Anhydrase XIII
207(14)
Ashok Aspatwar
Martti E.E. Tolvanen
Harlan Barker
Seppo Parkkila
11.1 Introduction
207(1)
11.2 Normal expression of CA XIII
208(4)
11.3 Expression in pathological conditions
212(1)
11.4 Kinetic properties
212(2)
11.5 Inhibition studies
214(1)
11.6 Activation studies
215(1)
11.7 Structure of CA XIII
215(1)
11.8 Conclusions
216(5)
References
217(4)
12 Carbonic Anhydrase XIV: Structure, Functions, and Potential Medical Applications
221(18)
Jean-Yves Winum
12.1 Introduction
221(1)
12.2 Expression and structure of CA XIV
222(2)
12.3 Catalytic activity of CA XIV and its modulation
224(9)
12.4 Physiological/pathological roles of CA XIV and potential medical applications
233(1)
12.5 Conclusion
234(5)
References
235(4)
13 Acatalytic Carbonic Anhydrases (CAs VIII, X, XI)
239(8)
Claudiu T. Supuran
Clemente Capasso
13.1 Introduction
239(1)
13.2 Primary sequence analysis
240(1)
13.3 Three-dimensional structure analysis
240(2)
13.4 Physiological function and tissue distribution of CAs VIII, X, and XI
242(1)
13.5 CARPs' biochemical properties after restoring the catalytic site
242(1)
13.6 Phylogenetic analysis
243(1)
13.7 Conclusions
244(3)
References
244(3)
14 β-Carbonic Anhydrases: General Features and Medical Implications
247(28)
Margaret M. Suhanovsky
Kelly Sheppard
Roger S. Rowlett
14.1 Introduction
248(1)
14.2 Distribution and physiological roles
248(4)
14.3 Structure
252(11)
14.4 Catalytic mechanism
263(4)
14.5 Inhibitors of β-CAs
267(8)
References
268(7)
15 Bacterial Carbonic Anhydrases as Drug Targets
275(14)
Clemente Capasso
Claudiu T. Supuran
15.1 Introduction
275(1)
15.2 α- and β-CAs in pathogenic bacteria
276(7)
15.3 Newly identified pathogenic CAs: VchCA (α-class), CpeCA (β-class), and PgiCA (γ-class)
283(1)
15.4 Conclusions
284(5)
References
285(4)
PART 3 CARBONIC ANHYDRASES FOR BIOTECHNOLOGICAL APPLICATIONS
289(84)
16 Engineered Mammalian Carbonic Anhydrases for CO, Capture
291(20)
Christopher D. Boone
Robert McKenna
16.1 Atmospheric CO2 sequestration
291(3)
16.2 CA Immobilization
294(2)
16.3 Biomedical CO2 capture
296(2)
16.4 CO2 capture for biofuel and biomass production
298(2)
16.5 Directed evolution of hCA II
300(2)
16.6 Other α-CAs
302(1)
16.7 Conclusions
302(9)
Acknowledgment
304(1)
References
304(7)
17 Carbonic Anhydrases From Extremophiles and Their Biotechnological Applications
311(14)
Clemente Capasso
Claudiu T. Supuran
17.1 Introduction
311(2)
17.2 Thermoactive CAs
313(5)
17.3 Carbon capture with thermostable CAs: a biomimetic approach in CO2 capture
318(3)
17.4 Use of heat-labile CAs in biomedical field
321(1)
17.5 Conclusions
322(3)
References
322(3)
18 Carbonic Anhydrases of Environmentally and Medically Relevant Anaerobic Prokaryotes
325(12)
James G. Ferry
18.1 Introduction
325(1)
18.2 The fermentation of complex biomass
326(1)
18.3 Methanogenesis
327(6)
18.4 Medically important anaerobes
333(1)
18.5 Conclusions
334(3)
References
334(3)
19 δ-Carbonic Anhydrases: Structure, Distribution, and Potential Roles
337(14)
Mathieu Beauchemin
David Morse
19.1 Introduction
337(4)
19.2 Structural insights
341(2)
19.3 Physiological role in marine algae
343(4)
19.4 Concluding remarks
347(4)
References
348(3)
20 CDCA 1 From Thalassiosira weissflogii as Representative Member of ζ-Class CAs: General Features and Biotechnological Applications
351(10)
Simona M. Monti
Giuseppina De Simone
Claudiu T. Supuran
Vincenzo Alterio
20.1 Introduction
351(1)
20.2 Biochemical features, catalytic activity, and Inhibition
352(2)
20.3 Structural features of CDCA1 and its repeats R1, R2, and R3
354(3)
20.4 Biotechnological applications
357(4)
References
358(3)
21 Carbonic Anhydrases as Esterases and Their Biotechnological Applications
361(12)
Jean-Yves Winum
Pedro Colinas
21.1 Introduction
361(1)
21.2 CA and esterase activity
362(5)
21.3 Biotechnological applications of esterase activity of CAs
367(6)
References
370(3)
Index 373
Dr. Claudiu T. Supuran received his BSc in chemistry from the Polytechnic University of Bucharest, Romania (1987) and PhD in chemistry at the same university in 1991. In 1990, he became Assistant and then Associate Professor of Chemistry at the University of Bucharest. He was Visiting Scholar at the University of Florida, Gainesville, United States, at Griffith University, Brisbane, Australia, and Visiting Professor at University of La Plata, Argentina. In 1995 he moved to the University of Florence, Italy, where he is currently Full Professor in the Department of Neuroscience, Psychology, Medicine and Child Health. His main research interests include design of enzyme inhibitors and activators, heterocyclic chemistry, chemistry of sulfonamides, sulfamates, and sulfamides, biologically active organo-element derivatives, QSAR studies, X-ray crystallography of metallo-enzymes, metal complexes with biologically active ligands (metal-based drugs), carbonic anhydrases, cyclooxygenases, serine proteases, matrix metalloproteinases, bacterial proteases, and amino acid derivatives among others. He has published more than 1900 papers in these fields. Giuseppina De Simone was born in Naples, Italy, and graduated in chemistry at the University of Naples Federico II (1993). She worked from August 1994 to January 1995 at the Drug Design Group”-Sandoz Pharma AG” in Basel, and from September 1995 to February 1996 at the University of Pavia. From November 1996 to January 1997 she was visiting scientist at the Max Plank Institute- Hamburg Germany. In 1998 she received her PhD at the University of Naples. Since 2003, she is Senior Researcher at the Institute of Biostructures and Bioimaging (IBB) of the Italian National Research Council. Her main research interests include X-ray crystallography of macromolecules, structure based drug design, carbonic anhydrases, serine proteases, esterases/lipases, peptide nucleic acids. She has published more than 90 papers in these fields.