Carbonic anhydrases as biocatalysts : from theory to medical and industrial applications / edited by Claudiu T. Supuran, Giuseppina De Simone.

Includes bibliographical references and index.

Cover; Title Page; Copyright Page; Table of contents; List of Contributors; Preface; Part 1 -- Introduction; Chapter 1 -- Carbonic Anhydrases: An Overview; 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; References; Part 2 -- Carbonic Anhydrasesas Drug Targets; Chapter 2 -- Human Carbonic Anhydrases: Catalytic Properties, Structural Features, and Tissue Distribution; 2.1 -- Introduction; 2.2 -- hCAs' structural features; 2.3 -- hCAs' catalytic features.

2.4 -- hCAs' tissue distribution and their role as drug targetsReferences; Chapter 3 -- Carbonic Anhydrase I; 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; References; Chapter 4 -- Carbonic Anhydrase II as Target for Drug Design; 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 agents4.4.1 -- First-generation inhibitors; 4.4.2 -- Second-generation inhibitors: topically acting sulfonamides; 4.4.3 -- Third-generation inhibitors; 4.4.4 -- Dithiocarbamates and xanthates as topically acting antiglaucoma CAIs targeting hCA II; 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 inhibitors4.10 -- CA II activation; 4.11 -- Conclusions; References; Chapter 5 -- Carbonic Anhydrase III; 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; References; Chapter 6 -- Carbonic Anhydrase IV; 6.1 -- Introduction; 6.2 -- Genomic organization and chromosomal localization of human CA IV.

6.3 -- Cloning and molecular characterization of human CA IV6.4 -- 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; 6.7.1 -- Kidney function; 6.7.2 -- Neuronal function; 6.7.3 -- Eye function; 6.7.4 -- Skeletal and cardiac muscle function; 6.7.5 -- CA IV functions in metabolons; 6.7.6 -- The role of CA IV in the taste of carbonation; 6.7.7 -- Disease-causing mutations in CA IV; 6.7.8 -- Kidney disease.

6.7.9 -- Environmental factors contributing to RP-17 associated with CA IV mutations.

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.

Description based on online resource; title from PDF title page (EBSCO, viewed January 21, 2015).

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