Carbonic Anhydrases as Biocatalysts
From Theory to Medical and Industrial Applications
- 1st Edition - January 8, 2015
- Latest edition
- Editors: Claudiu T. Supuran, Giuseppina De Simone
- Language: English
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 Carbo… Read more
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
It can be useful for many type of readers: biochemists, chemists and specialists in drug design, but also medical doctors and students of life sciences.
- List of Contributors
- Preface
- Part 1: Introduction
- Chapter 1: Carbonic Anhydrases: An Overview
- Abstract
- 1.1. Carbonic anhydrase families
- 1.2. Catalytic features
- 1.3. CA inhibition and activation
- 1.4. Biomedical applications of the CAs
- 1.5. Biotechnological applications of the CAs
- Chapter 1: Carbonic Anhydrases: An Overview
- Part 2: Carbonic Anhydrases as Drug Targets
- Chapter 2: Human Carbonic Anhydrases: Catalytic Properties, Structural Features, and Tissue Distribution
- Abstract
- 2.1. Introduction
- 2.2. hCAs’ structural features
- 2.3. hCAs’ catalytic features
- 2.4. hCAs’ tissue distribution and their role as drug targets
- Chapter 3: Carbonic Anhydrase I
- Abstract
- 3.1. Introduction
- 3.2. Structure of CA I
- 3.3. Tissue localization and physiological functions
- 3.4. CA I as pharmacological target
- 3.5. CA I inhibitors
- 3.6. CA I activators
- 3.7. Conclusions and perspectives
- Acknowledgment
- Chapter 4: Carbonic Anhydrase II as Target for Drug Design
- Abstract
- 4.1. Introduction
- 4.2. Biochemical properties, genetic relationship with the other cytosolic isoforms, and 3D structure of hCA II
- 4.3. hCA II inhibitors
- 4.4. Antiglaucoma agents
- 4.5. Diuretics with CA inhibitory properties
- 4.6. Agents for the management of altitude sickness
- 4.7. Various pharmacological actions connected with CA II inhibition: serendipity or off-targeting with impressive efficacy?
- 4.8. CA II inhibitors in the management of tumors?
- 4.9. New strategies to design CA II–selective inhibitors
- 4.10. CA II activation
- 4.11. Conclusions
- Chapter 5: Carbonic Anhydrase III
- Abstract
- 5.1. Introduction
- 5.2. Discovery of CA III
- 5.3. Physiological role of CA III
- 5.4. Molecular characterization of CA III
- 5.5. Catalytic properties and proton transfer of CA III
- 5.6. CA III as a biomarker: role in disease states
- 5.7. CA III as a drug target
- Acknowledgment
- Chapter 6: Carbonic Anhydrase IV
- Abstract
- 6.1. Introduction
- 6.2. Genomic organization and chromosomal localization of human CA IV
- 6.3. Cloning and molecular characterization of human CA IV
- 6.4. Structure/function: the role of disulfide bonds
- 6.5. Characterization of catalytic properties of human CA IV and its inhibition by sulfonamide inhibitors
- 6.6. Expression of CA IV in different tissues
- 6.7. Physiological functions of CA IV
- Acknowledgments
- Chapter 7: The Structure, Physiological Role, and Potential Medicinal Applications of Carbonic Anhydrase V
- Abstract
- 7.1. Introduction
- 7.2. Physiological role and potential medicinal applications of hCA VA and hCA VB
- 7.3. Selective ligands for carbonic anhydrase V
- 7.4. Sequence and three-dimensional structures of CA V isozymes
- 7.5. Final remarks
- Chapter 8: Secreted Carbonic Anhydrase Isoenzyme VI
- Abstract
- 8.1. Introduction
- 8.2. CA VI structure
- 8.3. Catalytic properties of CA VI
- 8.4. CA VI in salivary glands, saliva, and oral cavity
- 8.5. CA VI in mammary glands and milk
- 8.6. CA VI in esophagus and lower alimentary tract
- 8.7. CA VI in respiratory tract
- 8.8. CA VI in other organ systems
- 8.9. Potential medical applications
- 8.10. Conclusions and future prospects
- Chapter 9: Carbonic Anhydrase VII
- Abstract
- 9.1. Introduction
- 9.2. Kinetic and structural features of hCA VII
- 9.3. hCA VII and oxidative stress
- 9.4. The role of the CA VII in epileptogenesis and neuropathic pain
- 9.5. Inhibitors of hCA VII
- 9.6. Conclusions
- Chapter 10: Tumor-Associated Carbonic Anhydrases IX and XII
- Abstract
- 10.1. Introduction
- 10.2. History
- 10.3. Structure of CA IX and CA XII
- 10.4. Tissue distribution and subcellular localization
- 10.5. Regulation of CA IX expression
- 10.6. Regulation of CA XII expression
- 10.7. Role of CA IX and CA XII in tumor biology
- 10.8. Clinical significance
- 10.9. CA IX and CA XII targeted therapy
- 10.10. Conclusion
- Acknowledgments
- Chapter 11: Carbonic Anhydrase XIII
- Abstract
- 11.1. Introduction
- 11.2. Normal expression of CA XIII
- 11.3. Expression in pathological conditions
- 11.4. Kinetic properties
- 11.5. Inhibition studies
- 11.6. Activation studies
- 11.7. Structure of CA XIII
- 11.8. Conclusions
- Chapter 12: Carbonic Anhydrase XIV: Structure, Functions, and Potential Medical Applications
- Abstract
- 12.1. Introduction
- 12.2. Expression and structure of CA XIV
- 12.3. Catalytic activity of CA XIV and its modulation
- 12.4. Physiological/pathological roles of CA XIV and potential medical applications
- 12.5. Conclusion
- Chapter 13: Acatalytic Carbonic Anhydrases (CAs VIII, X, XI)
- Abstract
- 13.1. Introduction
- 13.2. Primary sequence analysis
- 13.3. Three-dimensional structure analysis
- 13.4. Physiological function and tissue distribution of CAs VIII, X, and XI
- 13.5. CARPs’ biochemical properties after restoring the catalytic site
- 13.6. Phylogenetic analysis
- 13.7. Conclusions
- Chapter 14: β-Carbonic Anhydrases: General Features and Medical Implications
- Abstract
- 14.1. Introduction
- 14.2. Distribution and physiological roles
- 14.3. Structure
- 14.4. Catalytic mechanism
- 14.5. Inhibitors of β-CAs
- Chapter 15: Bacterial Carbonic Anhydrases as Drug Targets
- Abstract
- 15.1. Introduction
- 15.2. α- and β-CAs in pathogenic bacteria
- 15.3. Newly identified pathogenic CAs: VchCA (α-class), CpeCA (β-class), and PgiCA (γ-class)
- 15.4. Conclusions
- Chapter 2: Human Carbonic Anhydrases: Catalytic Properties, Structural Features, and Tissue Distribution
- Part 3: Carbonic Anhydrases for Biotechnological Applications
- Chapter 16: Engineered Mammalian Carbonic Anhydrases for CO2 Capture
- Abstract
- 16.1. Atmospheric CO2 sequestration
- 16.2. CA immobilization
- 16.3. Biomedical CO2 capture
- 16.4. CO2 capture for biofuel and biomass production
- 16.5. Directed evolution of hCA II
- 16.6. Other α-CAs
- 16.7. Conclusions
- Acknowledgment
- Chapter 17: Carbonic Anhydrases From Extremophiles and Their Biotechnological Applications
- Abstract
- 17.1. Introduction
- 17.2. Thermoactive CAs
- 17.3. Carbon capture with thermostable CAs: a biomimetic approach in CO2 capture
- 17.4. Use of heat-labile CAs in biomedical field
- 17.5. Conclusions
- Chapter 18: Carbonic Anhydrases of Environmentally and Medically Relevant Anaerobic Prokaryotes
- Abstract
- 18.1. Introduction
- 18.2. The fermentation of complex biomass
- 18.3. Methanogenesis
- 18.4. Medically important anaerobes
- 18.5. Conclusions
- Chapter 19: δ-Carbonic Anhydrases: Structure, Distribution, and Potential Roles
- Abstract
- 19.1. Introduction
- 19.2. Structural insights
- 19.3. Physiological role in marine algae
- 19.4. Concluding remarks
- Chapter 20: CDCA1 From Thalassiosira weissflogii as Representative Member of ζ-Class CAs: General Features and Biotechnological Applications
- Abstract
- 20.1. Introduction
- 20.2. Biochemical features, catalytic activity, and inhibition
- 20.3. Structural features of CDCA1 and its repeats R1, R2, and R3
- 20.4. Biotechnological applications
- Chapter 21: Carbonic Anhydrases as Esterases and Their Biotechnological Applications
- Abstract
- 21.1. Introduction
- 21.2. CA and esterase activity
- 21.3. Biotechnological applications of esterase activity of CAs
- Chapter 16: Engineered Mammalian Carbonic Anhydrases for CO2 Capture
- Index
- Edition: 1
- Latest edition
- Published: January 8, 2015
- Language: English
CS
Claudiu T. Supuran
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.
Affiliations and expertise
Full Professor, University of Florence, Neuroscience, Psychology, Medicine and Child Health, Florence, ItalyGD
Giuseppina De Simone
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.
Affiliations and expertise
Institute of Biostructures and Bioimaging (IBB) of the Italian National Research Council, Napoli, ItalyRead Carbonic Anhydrases as Biocatalysts on ScienceDirect