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HUMAN CARBONIC ANHYDRASES AND CARBONIC ANHYDRASE DEFICIENCIES
Annual Review of Biochemistry, 1995Carbonic anhydrases (CAs I-VII) are products of a gene family that encodes seven isozymes and several homologous, CA- related proteins. All seven isozymes have been cloned, sequenced, and mapped, and the intron-exon organization of five genes established. They differ in subcellular localizations, being cytoplasmic (CA I, II, III, and VII), GPI-anchored
W S, Sly, P Y, Hu
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ChemInform, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
SCOZZAFAVA, ANDREA +2 more
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AbstractFor Abstract see ChemInform Abstract in Full Text.
SCOZZAFAVA, ANDREA +2 more
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International Journal of Biochemistry, 1987
Some of the current studies of carbonic anhydrases are directed to the genetic mechanisms underlying their synthesis. Determination of the structure of their genes will probably most readily resolve the question of whether the membrane bound forms of the enzyme represent products of additional loci other than those of the three well-known soluble forms.
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Some of the current studies of carbonic anhydrases are directed to the genetic mechanisms underlying their synthesis. Determination of the structure of their genes will probably most readily resolve the question of whether the membrane bound forms of the enzyme represent products of additional loci other than those of the three well-known soluble forms.
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2000
Microalgae grown in ordinary air (0.04% CO2) show a much higher affinity for inorganic carbon (Ci) in photosynthesis than those grown with 2% to 5% CO2, although at saturating CO2 concentrations the maximum rate of photosynthesis is almost the same.
H, Fukuzawa, M, Tsuzuki, S, Miyachi
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Microalgae grown in ordinary air (0.04% CO2) show a much higher affinity for inorganic carbon (Ci) in photosynthesis than those grown with 2% to 5% CO2, although at saturating CO2 concentrations the maximum rate of photosynthesis is almost the same.
H, Fukuzawa, M, Tsuzuki, S, Miyachi
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1987
The ṗroperties of Carbonic Anhydrase, the enzyme which catalyzes the CO2 hydration and HCO3 - dehydration, are reviewed. The mechanism is discussed in details in terms of Zn-OH attacking CO2 to give rise to HCO3 which is then released after H20 uptake. H+ is then released. The inhibition mechanism is also discussed.
BERTINI, IVANO +2 more
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The ṗroperties of Carbonic Anhydrase, the enzyme which catalyzes the CO2 hydration and HCO3 - dehydration, are reviewed. The mechanism is discussed in details in terms of Zn-OH attacking CO2 to give rise to HCO3 which is then released after H20 uptake. H+ is then released. The inhibition mechanism is also discussed.
BERTINI, IVANO +2 more
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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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