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Zinc enzymes --- Addresses, essays, lectures --- Enzymes --- Physiology --- Physiological effect
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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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Phosphatases such as TNAP are fundamental in regulating cellular, and consequently numerous body functions. TNAP is a ubiquitous enzyme with a wide spectrum of substrates and specificity regulation at the cellular level and the lack of TNAP activity is a lethal condition. Recent findings of a highly specific regional, laminar and subcellular localization of TNAP in the cerebral cortex indicates that in addition to its metabolic and skeletal functions, TNAP also plays a role in regulating cerebral functions, most probably cognition. In fact, TNAP disturbance could result in complex diseases such as epilepsy, developmental retardation and Alzheimer disease. Available data suggest that, regarding brain functions, TNAP is a potentially important target of clinical research. The proposed book aims to provide an overview of our current understanding of the functions of TNAP in the brain.
Biomedicine. --- Human Physiology. --- Animal Physiology. --- Developmental Biology. --- Neurosciences. --- Medicine. --- Human physiology. --- Developmental biology. --- Médecine --- Physiologie humaine --- Neurosciences --- Biologie du développement --- Alkaline phosphatase. --- Phosphatases. --- Human Anatomy & Physiology --- Health & Biological Sciences --- Physiology --- Phosphoesterases --- Phosphohydrolases --- Animal physiology. --- Phosphatases --- Zinc enzymes --- Esterases --- Development (Biology) --- Biology --- Growth --- Ontogeny --- Animal physiology --- Animals --- Anatomy --- Human biology --- Medical sciences --- Human body --- Neural sciences --- Neurological sciences --- Neuroscience --- Nervous system
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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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DNA-Directed DNA Polymerase --- DNA-Directed RNA Polymerases --- Enzyme Inhibitors. --- Antibiotics --- -DNA polymerases --- -RNA polymerases --- -DNA-dependent RNA polymerases --- DNA-directed RNA polymerases --- Polymerases, RNA --- Ribonucleate nucleotidyltransferases --- RNA nucleotidyltransferases --- Transferases --- Deoxyribonucleate nucleotidyltransferases --- DNA-dependent DNA polymerases --- DNA-directed DNA polymerases --- DNA nucleotidyltransferases --- Nucleotidyltransferases, Deoxyribonucleate --- Polymerases, DNA --- Zinc enzymes --- Polymerase chain reaction --- Anti-infective agents --- Microbial metabolites --- Allelopathic agents --- Antibiosis --- Pharmaceutical microbiology --- Phytoncides --- Inhibitors, Enzyme --- Enzymes --- Sulfhydryl Reagents --- antagonists & inhibitors. --- Physiological effect --- -Congresses --- Inhibitors --- antagonists & inhibitors --- -antagonists & inhibitors. --- DNA polymerases --- RNA polymerases --- Congresses. --- Enzyme Inhibitors --- DNA-dependent RNA polymerases --- Physiological effect&delete& --- Congresses --- Inhibitors&delete& --- Enzyme Inhibitor --- Inhibitor, Enzyme --- DNA Polymerase Inhibitors --- Inhibitors, DNA Synthesis --- Inhibitors, Nucleic Acid Synthesis --- Inhibitors, RNA Synthesis --- DNA Polymerase Inhibitor --- DNA Synthesis Inhibitor --- DNA Synthesis Inhibitors --- Nucleic Acid Synthesis Inhibitor --- RNA Synthesis Inhibitor --- RNA Synthesis Inhibitors --- Inhibitor, DNA Polymerase --- Inhibitor, DNA Synthesis --- Inhibitor, RNA Synthesis --- Inhibitors, DNA Polymerase --- Polymerase Inhibitor, DNA --- Polymerase Inhibitors, DNA --- Synthesis Inhibitor, DNA --- Synthesis Inhibitor, RNA --- Synthesis Inhibitors, DNA --- Synthesis Inhibitors, RNA --- DNA --- RNA --- ENZYME INHIBITORS --- CHEMICAL SYNTHESIS
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