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Carbonic anhydrases as biocatalysts : from theory to medical and industrial applications /

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 in...

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Supuran, Claudiu T., 1962- (Editor ), Simone, Giuseppina De (Editor )
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Amsterdam : Elsevier, [2015]
Temas:
Acceso en línea:Texto completo

MARC

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245 0 0 |a Carbonic anhydrases as biocatalysts :  |b from theory to medical and industrial applications /  |c edited by Claudiu T. Supuran, Giuseppina De Simone. 
264 1 |a Amsterdam :  |b Elsevier,  |c [2015] 
264 4 |c �2015 
300 |a 1 online resource :  |b illustrations (some color) 
336 |a text  |b txt  |2 rdacontent 
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504 |a Includes bibliographical references and index. 
588 0 |a Online resource; title from PDF title page (EBSCO, viewed January 21, 2015). 
520 |a 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. 
505 0 |a 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. 
505 8 |a 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. 
505 8 |a 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? 
505 8 |a 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. 
505 8 |a 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. 
505 8 |a 6.7.9 -- Environmental factors contributing to RP-17 associated with CA IV mutations. 
650 0 |a Carbonic anhydrase. 
650 0 |a Carbonic anhydrase  |x Therapeutic use. 
650 0 |a Enzymes. 
650 0 |a Enzymes  |x Therapeutic use. 
650 0 |a Biotechnology. 
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650 2 |a Enzymes  |0 (DNLM)D004798 
650 2 |a Biotechnology  |0 (DNLM)D001709 
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650 6 |a Enzymes  |0 (CaQQLa)201-0002557  |x Emploi en th�erapeutique.  |0 (CaQQLa)201-0373975 
650 6 |a Biotechnologie.  |0 (CaQQLa)201-0004007 
650 7 |a enzyme.  |2 aat  |0 (CStmoGRI)aat300212647 
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650 7 |a Carbonic anhydrase  |2 fast  |0 (OCoLC)fst00846939 
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700 1 |a Supuran, Claudiu T.,  |d 1962-  |e editor. 
700 1 |a Simone, Giuseppina De,  |e editor. 
776 0 8 |i Print version:  |a Supuran, Claudiu T.  |t Carbonic Anhydrases as Biocatalysts : From Theory to Medical and Industrial Applications.  |d Burlington : Elsevier Science, �2015  |z 9780444632586 
856 4 0 |u https://sciencedirect.uam.elogim.com/science/book/9780444632586  |z Texto completo