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Future Medicinal Chemistry, 2018
Mammalian carbonic anhydrases (CAs; EC 4.2.1.1) of which 16 isoforms are known, are involved in important physiological functions. Their inhibition is exploited pharmacologically for the treatment of many diseases (glaucoma, edema, epilepsy, obesity, hypoxic tumors, neuropathic pain, etc.) but the activators were less investigated till recently.
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Mammalian carbonic anhydrases (CAs; EC 4.2.1.1) of which 16 isoforms are known, are involved in important physiological functions. Their inhibition is exploited pharmacologically for the treatment of many diseases (glaucoma, edema, epilepsy, obesity, hypoxic tumors, neuropathic pain, etc.) but the activators were less investigated till recently.
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2016
Carbonic anhydrases (CAs, EC 4.2.1.1) belonging to the α-, β-, and η-classes are present in many pathogenic protozoa, such as those belonging to the Trypanosoma, Leishmania, and Plasmodium genera. In the last years many such enzymes have been cloned, purified, and extensively characterized.
Supuran C. T., Capasso C.
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Carbonic anhydrases (CAs, EC 4.2.1.1) belonging to the α-, β-, and η-classes are present in many pathogenic protozoa, such as those belonging to the Trypanosoma, Leishmania, and Plasmodium genera. In the last years many such enzymes have been cloned, purified, and extensively characterized.
Supuran C. T., Capasso C.
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Carbonic Anhydrase in Bacteria
Nature, 1963THE richest source of carbonic anhydrase is mammalian erythrocytes. It is also found in the pancreas, gastric mucosa, and kidney in fairly high concentration. Carbonic anhydrase has also been found localized in the cytoplasm of plant leaf tissue1–4. A survey of the literature revealed no report of the occurrence of microbial carbonic anhydrases.
F P, VEITCH, L C, BLANKENSHIP
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Carbonic Anhydrases An Overview
Current Pharmaceutical Design, 2008Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread metalloenzymes all over the phylogenetic tree, with at least 4 distinct gene families encoding for them. At least 16 different alpha-CA isoforms were isolated in mammals, where these enzymes play crucial physiological roles.
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2016
Carbonic anhydrases (CAs, EC 4.2.1.1) are metalloenzymes which catalyze the hydration of carbon dioxide to bicarbonate and protons. Many pathogenic bacteria encode such enzymes belonging to the α-, β-, and/or γ-CA families. In the last decade enzymes from Neisseria spp., Helicobacter pylori, Escherichia coli, Mycobacterium tuberculosis, Brucella spp ...
Capasso C., Supuran C. T.
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Carbonic anhydrases (CAs, EC 4.2.1.1) are metalloenzymes which catalyze the hydration of carbon dioxide to bicarbonate and protons. Many pathogenic bacteria encode such enzymes belonging to the α-, β-, and/or γ-CA families. In the last decade enzymes from Neisseria spp., Helicobacter pylori, Escherichia coli, Mycobacterium tuberculosis, Brucella spp ...
Capasso C., Supuran C. T.
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Bioorganic & Medicinal Chemistry Letters, 2010
Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread enzymes in all organisms, catalyzing CO2 hydration to bicarbonate and protons. Their inhibition is exploited clinically for decades for various classes of diuretics and systemically acting antiglaucoma agents.
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Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread enzymes in all organisms, catalyzing CO2 hydration to bicarbonate and protons. Their inhibition is exploited clinically for decades for various classes of diuretics and systemically acting antiglaucoma agents.
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CARBONIC ANHYDRASE IN THE PREMATURE
Pediatrics, 1968Carbonic anhydrase activity was measured in the blood of premature and full-term infants to determine if the arterial-alveolar carbon dioxide gradient was related to low levels of carbonic anhydrase. The time at which levels in these infants approached the adult was studied as well.
E, Poblete, D W, Thibeault, P A, Auld
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Carbonic Anhydrase in the Cornea
Acta Physiologica Scandinavica, 1974AbstractCarbonic anhydrase activity in the corneas of adult man, human fetus, monkey, rabbit, rat, cow, pig and American bullfrog was examined by the histochemical method of Hansson. In all species the endothelial cells were intensely and distinctly stained for carbonic anhydrase activity.
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Novel Carbonic Anhydrase Inhibitors
Future Medicinal Chemistry, 2021Abstract
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Nature, 1947
IN contrast to the wealth of information concerning carbonic anhydrase in the animal kingdom, there have been few reports of the occurrence of this enzyme in the plant kingdom1. It seemed desirable, therefore, briefly to describe the following observations made in the course of work on the enzyme in animal tissues.
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IN contrast to the wealth of information concerning carbonic anhydrase in the animal kingdom, there have been few reports of the occurrence of this enzyme in the plant kingdom1. It seemed desirable, therefore, briefly to describe the following observations made in the course of work on the enzyme in animal tissues.
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