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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 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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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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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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Introduction to the carbonic anhydrases
2000Since the discovery, almost 70 years ago, of the enzyme carbonic anhydrase (CA), which plays an important role in the red blood cell by catalyzing the hydration of carbon dioxide (CO2 + H2O ↔ HCO– 3+ H+), a fascinating and complex story has unfolded of three enzyme families performing numerous functions in many different organisms.
W R, Chegwidden, N D, Carter
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Perspectives on carbonic anhydrase
Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, 2010In the years since Larimer and Schmidt-Nielsen published their examination of red blood cell (RBC) carbonic anhydrase (CA) activities as a function of body mass in mammals, our knowledge of CA has expanded dramatically. We are now aware of the diversity of CA isoforms and their implication in a wide array of physiological processes.
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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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Carbonic Anhydrase II Deficiency
Clinical Orthopaedics and Related Research, 1993Carbonic anhydrase (CA) isoenzyme II deficiency--formerly called the syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification--is an autosomal recessive "inborn error of metabolism" that has disclosed important insight concerning osteoclast function.
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Carboxysomal Carbonic Anhydrases
2013Cyanobacteria and some chemoautotrophic bacteria enhance their carbon fixation efficiency by actively concentrating bicarbonate within their cytosol. However, converting bicarbonate into carbon dioxide - the form required by RubisCO - would result in its rapid escape through cellular membranes.
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