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Carbonic anhydrase --- Carbonate Dehydratase --- Carbonic Anhydrase Inhibitors
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Carbonic anhydrase. --- Carbonic Anhydrases --- chemistry. --- pharmacokinetics. --- Carbonate dehydratase --- Lyases --- Zinc enzymes
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Animal biochemistry --- Carbonic anhydrase --- Congresses --- Carbonic Anhydrases --- Congresses. --- congresses. --- Carbonate dehydratase --- Lyases --- Zinc enzymes --- Carbonic anhydrase - Congresses
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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 biocatalystsIncludes current applications of carbonic anhydrases in biotechnology on the basis of their
Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- Carbonic anhydrase. --- Carbonic anhydrase --- Enzymes. --- Enzymes --- Biotechnology. --- Therapeutic use. --- Chemical engineering --- Genetic engineering --- Biocatalysts --- Ferments --- Soluble ferments --- Catalysts --- Proteins --- Enzymology --- Carbonate dehydratase --- Lyases --- Zinc enzymes
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The study of carbonic anhydrase has spanned multiple generations of scientists. Carbonic anhydrase was first discovered in 1932 by Meldrum and Roughton. Inhibition by sulfanilamide was shown in 1940 by Mann and Keilin. Even Hans Krebs contributed to early studies with a paper in 1948 showing the relationship of 25 different sulfonamides to CA inhibition. It was he who pointed out the importance of both the charged and uncharged character of these compounds for physiological experiments. The field of study that focuses on carbonic anhydrase (CA) has exploded in recent years with the identification of new families and isoforms. The CAs are metalloenzymes which are comprised of 5 structurally different families: the alpha, beta, gamma, and delta, and epsilon classes. The alpha class is found primarily in animals with several isoforms associated with human disease. The beta CAs are expressed primarily in plants and are the most divergent. The gamma CAs are the most ancient. These are structurally related to the beta CAs, but have a mechanism more similar to the alpha CAs. The delta CAs are found in marine algae and diflagellates. The epsilon class is found in prokaryotes in which it is part of the carboxysome shell perhaps supplying RuBisCO with CO2 for carbon fixation. With the excitement surrounding the discovery of disease-related CAs, scientists have redoubled their efforts to better understand structure-function relationships, to design high affinity, isotype-specific inhibitors, and to delineate signaling systems that play regulatory roles over expression and activity. We have designed the book to cover basic information of mechanism, structure, and function of the CA families. The authors included in this book bring to light the newest data with regard to the role of CA in physiology and pathology, across phylums, and in unique environmental niches.
Carbonic anhydrase. --- Lyases. --- Desmolases --- Carbonate dehydratase --- Medicine. --- Medical genetics. --- Proteins. --- Biomedicine. --- Gene Function. --- Protein Science. --- Biomedicine general. --- Enzymes --- Lyases --- Zinc enzymes --- Biochemistry. --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Medical sciences --- Pathology --- Physicians --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Clinical genetics --- Diseases --- Heredity of disease --- Human genetics --- Genetic disorders --- Composition --- Genetic aspects --- Health Workforce --- Proteins . --- Biomedicine, general. --- Proteids --- Biomolecules --- Polypeptides --- Proteomics --- Medicine --- Medical Genetics. --- Protein Biochemistry. --- Biomedical Research. --- Research. --- Biological research --- Biomedical research
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This book offers deep insights into the thermodynamics and molecular structures of the twelve catalytically active isoforms of human carbonic anhydrase (CA) with a particular focus on inhibitor binding for drug design. X-ray crystallographic structures in combination with enzyme kinetic testing provide information on the interaction of CAs and their inhibitors, knowledge which is crucial for rational drug design. CAs are zinc carrying enzymes that catalyse the reversible interconversion of carbon dioxide and bicarbonate and are involved in numerous cellular processes. They are therefore a common target for drugs. The suppression of CA activities through inhibitory compounds has found application for example in diuretics and in glaucoma therapy. In this book methods used to determine binding thermodynamics of inhibitory compounds (Isothermal titration calorimetry, Fluorescent thermal shift assay/differential scanning fluorimetry and others) will be compared in detail. Also types and chemical synthesis of CA inhibitors, the use of antibodies against CAs as well as inhibitor application in animals are discussed. .
Carbonic anhydrase. --- Carbonate dehydratase --- Lyases --- Zinc enzymes --- Medicine. --- Biochemistry. --- RNA-ligand interactions. --- Pharmaceutical technology. --- Molecular Medicine. --- Medical Biochemistry. --- Protein-Ligand Interactions. --- Medicinal Chemistry. --- Pharmaceutical Sciences/Technology. --- Pharmaceutical laboratory techniques --- Pharmaceutical laboratory technology --- Technology, Pharmaceutical --- Technology --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Health Workforce --- Composition --- Molecular biology. --- Medical biochemistry. --- Proteins . --- Medicinal chemistry. --- Chemistry, Medical and pharmaceutical --- Chemistry, Pharmaceutical --- Drug chemistry --- Drugs --- Medical chemistry --- Medicinal chemistry --- Pharmacochemistry --- Proteids --- Biomolecules --- Polypeptides --- Proteomics --- Medical biochemistry --- Pathobiochemistry --- Pathological biochemistry --- Biochemistry --- Pathology --- Molecular biochemistry --- Molecular biophysics --- Biophysics --- Systems biology
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