Carbonic anhydrase from Neisseria sicca, strain 6021 I. Bacterial growth and purification of the enzyme

Adler, Lennart; Brundell, J.; Falkbring, S.O.; Nyman, Per Olof

doi:10.1016/0005-2744(72)90068-x

Cited by 56 publications

(31 citation statements)

References 22 publications

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“…α-, β-and γ-CAs, with the β-class enzymes being the most diffuse 8 . Within the Bacteria domain, the enzymes purified from Neisseria gonorrhoeae, Neisseria sicca and Helicobacter pylori belong to the α class [9][10][11][12] . The N. gonorrhoeae CA had a molecular mass of 28 kDa, being quite homologous to mammalian CAs and showed a high CO 2 hydratase activity, similarly to the human isoforms hCA II and an esterase activity for the hydrolysis of p-NpA 10 .…”

Section: Introductionmentioning

confidence: 99%

Biochemical properties of a novel and highly thermostable bacterial α-carbonic anhydrase fromSulfurihydrogenibium yellowstonense YO3AOP1

Capasso

Luca

Carginale

et al. 2012

Journal of Enzyme Inhibition and Medicinal Chemistry

116

109

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Section: Introductionmentioning

confidence: 99%

Biochemical properties of a novel and highly thermostable bacterial α-carbonic anhydrase fromSulfurihydrogenibium yellowstonense YO3AOP1

Capasso

Luca

Carginale

et al. 2012

Journal of Enzyme Inhibition and Medicinal Chemistry

116

109

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“…This was confirmed by experiments in which chloramphenicol (at 100 pug/ml, which stopped further protein synthesis) was added just before cyanate was completely degraded (however, degradation of cyanate continued and was completed in the same time period 1 2 3 4 5 6 7 8 9 because of the presence of endogenous cyanase at the time of addition of chloramphenicol). Results virtually identical to those shown in Fig.…”

Section: Methodsmentioning

confidence: 76%

“…On the other hand, the localization of induced E. coli carbonic anhydrase in the cytosol may stand in contrast to that of the few other carbonic anhydrases which have been characterized in prokaryotes, in which carbonic anhydrases are apparently not localized in the cytosol (1,2,10,15,18,26). In this context, we call attention to the structural properties of the N-terminal sequence of E. coli carbonic anhydrase, which poses possibly interesting questions concerning the function and evolution of this operon.…”

Section: Discussionmentioning

confidence: 96%

Expression of proteins encoded by the Escherichia coli cyn operon: carbon dioxide-enhanced degradation of carbonic anhydrase

et al. 1994

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Cyanase catalyzes the reaction of cyanate with bicarbonate to give 2CO2. The cynS gene encoding cyanase, together with the cynT gene for carbonic anhydrase, is part of the cyn operon, the expression ofwhich is induced in Escherichia coli by cyanate. The physiological role of carbonic anhydrase is to prevent depletion of cellular bicarbonate during cyanate decomposition due to loss of CO2 (M. B. Guilloton, A. F. Lamblin, E. I. Kozliak, M. Gerami-Nejad, C. Tu, D. Silverman, P. M. Anderson, and J. A. Fuchs. J. Bacteriol. 175:1443-1451, 1993. A AcynT mutant strain was extremely sensitive to inhibition of growth by cyanate and did not catalyze decomposition of cyanate (even though an active cyanase was expressed) when grown at a low pCO2 (in air) but had a Cyn' phenotype at a high pCO2. Here the expression of these two enzymes in this unusual system for cyanate degradation was characterized in more detail. Both enzymes were found to be located in the cytosol and to be present at approximately equal levels in the presence of cyanate. A AcynT mutant strain could be complemented with high levels of expressed human carbonic anhydrase II; however, the mutant defect was not completely abolished, perhaps because the E. coli carbonic anhydrase is significantly less susceptible to inhibition by cyanate than mammalian carbonic anhydrases. The induced E. coli carbonic anhydrase appears to be particularly adapted to its function in cyanate degradation. Active cyanase remained in cells grown in the presence of either low or high pCO2 after the inducer cyanate was depleted; in contrast, carbonic anhydrase protein was degraded very rapidly (minutes) at a high pCO2 but much more slowly (hours) at a low pCO2. A physiological significance of these observations is suggested by the observation that expression of carbonic anhydrase at a high pCO2 decreased the growth rate.Cyanase (EC 4.3.99.1) catalyzes the reaction of cyanate with bicarbonate to give 2CO2 (14) as follows: NCO-+ 3H+ + HCO-3>2CO2 + NH4+. This enzyme is induced in Escherichia coli, along with the enzyme carbonic anhydrase, by addition of cyanate to growth media (3, 12). The genes for these enzymes are part of the cyn operon, which includes three genes in the order cynT, cynS, and cynX, encoding carbonic anhydrase, cyanase, and a hydrophobic protein with an unknown function, respectively (12,(33)(34)(35). A recent study using chromosomal mutants constructed so that either the induced cyanase or carbonic anhydrase, respectively, was inactive provided evidence that the role of carbonic anhydrase is to prevent depletion of cellular bicarbonate during cyanate decomposition due to loss of CO2, which diffuses out of the cells faster than noncatalyzed hydration back to bicarbonate. Thus, even though cyanase activity was induced in a AcynT mutant (nonfunctional carbonic anhydrase), the mutant strain was extremely sensitive to inhibition of growth by cyanate, did not catalyze decomposition of cyanate, and could not grow on cyanate as a sole source of nitrogen when grown under aerati...

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“…The purified and native pfCA enzyme has a KI value of AZA higher than those of the human CA II and many bacterial CAs. Notably, the yeast CA, the plant CA and the mammalian CA III are peculiarly insensitive to AZA inhibition [60][61][62][63][64][65][66][67] .…”

Section: Gene and Protein Of Malaria Parasite 毩 -Carbonic Anhydrasementioning

confidence: 99%

Malaria parasite carbonic anhydrase: inhibition of aromatic/heterocyclic sulfonamides and its therapeutic potential

Krungkrai¹,

Krungkrai²

2011

Asian Pacific Journal of Tropical Biomedicine

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Carbonic anhydrase from Neisseria sicca, strain 6021 I. Bacterial growth and purification of the enzyme

Cited by 56 publications

References 22 publications

Biochemical properties of a novel and highly thermostable bacterial α-carbonic anhydrase fromSulfurihydrogenibium yellowstonense YO3AOP1

Biochemical properties of a novel and highly thermostable bacterial α-carbonic anhydrase fromSulfurihydrogenibium yellowstonense YO3AOP1

Expression of proteins encoded by the Escherichia coli cyn operon: carbon dioxide-enhanced degradation of carbonic anhydrase

Malaria parasite carbonic anhydrase: inhibition of aromatic/heterocyclic sulfonamides and its therapeutic potential

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