Carbonic Anhydrase in Bacteria

Veitch, F. P.; Blankenship, L. C.

doi:10.1038/197076a0

Cited by 58 publications

(28 citation statements)

References 6 publications

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“…The first report of bacterial carbonic anhydrase was presented in 1963 by Veitch and Blankenship [8], who measured significant activities in strains of several species of the genus Neisseria and in a strain of Streptococcus salivariu. The enzyme from Neisseria sicca, strain 6021, has been purified [9], and some of its properties have been characterized [lo].…”

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The Complete Sequence, Expression in Escherichia Coli, Purification and Some Properties of Carbonic Anhydrase from Neisseria Gonorrhoeae

Chirică¹,

Elleby²,

Jonsson³

et al. 1997

European Journal of Biochemistry

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The complete nucleotide sequence of the carbonic anhydrase gene from Neisseria gonorrhoeae has been determined. The gene encodes a 252-residue polypeptide with a molecular mass of 28085 Da. The gene has been cloned and overexpressed in Escherichia coli, and the enzyme has been purified. A 26-residue signal peptide is cleaved off by the E. coli processing machinery. Thus, the isolated enzyme contains 226 amino acid residues with a molecular mass of 25 314 Da. Most of the enzyme seems to be produced as a soluble protein located in the periplasm of E. coli. The enzyme is homologous to carbonic anhydrases from the animal kingdom; it is an a-carbonic anhydrase. A comparison with the amino acid sequences of human carbonic anhydrases I and I1 suggests that the secondary structures are essentially intact in the bacterial enzyme but that several loops are much shorter than in the human forms. Most of the active-site residues are identical to those found in the high-activity human isozyme 11. The bacterial enzyme has a high CO, hydration activity with a k,,, of 1.1 . lo6 s-' and K,, of 20 mM at pH 9 and 25°C.The enzyme also catalyzes the hydrolysis of 4-nitrophenyl acetate. The pH/rate profile can be described as a titration curve with pK, of 6.7 and a maximal value of the catalytic second-order rate constant, k,,,,,

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The Complete Sequence, Expression in Escherichia Coli, Purification and Some Properties of Carbonic Anhydrase from Neisseria Gonorrhoeae

Chirică¹,

Elleby²,

Jonsson³

et al. 1997

European Journal of Biochemistry

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“…Carbonic anhydrases are also abundant in plants and unicellular green algae, where they are essential for photosynthetic CO 2 fixation (3). Although they are ubiquitous in highly evolved organisms from the Eukarya, the extent to which carbonic anhydrases occur in the Archaea and Bacteria domains is unknown; the enzyme has been purified from only five prokaryotic species (4-8) since 1963, when it was first identified in Neisseria sicca (9).…”

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Carbonic anhydrase is an ancient enzyme widespread in prokaryotes

Smith

Jakubzick

Whittam

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

359

289

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Carbonic anhydrases catalyze the reversible hydration of CO2 and are ubiquitous in highly evolved eukaryotes. The recent identification of a third class of carbonic anhydrase (␥ class) in a methanoarchaeon and our present finding that the ␤ class also extends into thermophilic species from the Archaea domain led us to initiate a systematic search for these enzymes in metabolically and phylogenetically diverse prokaryotes. Here we show that carbonic anhydrase is widespread in the Archaea and Bacteria domains, and is an ancient enzyme. The occurrence in chemolithoautotrophic species occupying deep branches of the universal phylogenetic tree suggests a role for this enzyme in the proposed autotrophic origin of life. The presence of the ␤ and ␥ classes in metabolically diverse species spanning the Archaea and Bacteria domains demonstrates that carbonic anhydrases have a far more extensive and fundamental role in prokaryotic biology than previously recognized. Carbonic anhydrase is a zinc-containing enzyme catalyzing the reversible hydration of CO 2 [CO 2 ϩ H 2 O º HCO 3 Ϫ ϩ H ϩ ]. Since the discovery of the enzyme in bovine erythrocytes in 1933 (1), isozymes have been found in virtually all mammalian tissues and cell types, where they function in CO 2 transport and other physiological processes (2). Carbonic anhydrases are also abundant in plants and unicellular green algae, where they are essential for photosynthetic CO 2 fixation (3). Although they are ubiquitous in highly evolved organisms from the Eukarya, the extent to which carbonic anhydrases occur in the Archaea and Bacteria domains is unknown; the enzyme has been purified from only five prokaryotic species (4-8) since 1963, when it was first identified in Neisseria sicca (9).All carbonic anhydrases are divided into three distinct classes (␣, ␤, and ␥) that evolved independently and have no sequence homology (10). Carbonic anhydrases from mammals (including the 10 active human isoforms) (10, 11), together with the two periplasmic enzymes from the unicellular green alga Chlamydomonas reinhardtii (12, 13), belong to the ␣ class. The ␤ class is comprised of enzymes from the chloroplasts of both monocotyledonous and dicotyledonous plants (10). Within the Bacteria domain, the enzymes purified from Neisseria gonorrhoeae and Escherichia coli also belong to the ␣ and ␤ classes (14, 15), respectively. Recently, a gene encoding a putative ␤ type carbonic anhydrase in the methanoarchaeon Methanobacterium thermoautotrophicum was expressed in E. coli and found to encode a thermostable carbonic anhydrase (16). A carbonic anhydrase purified from the archaeon Methanosarcina thermophila is decidedly distinct from the ␣ and ␤ classes, and is the prototype of a different class, the ␥ class (17).Our detection of documented ␤ and ␥ carbonic anhydrases in the methanoarchaea prompted us to investigate the distribution of carbonic anhydrases in the Archaea and Bacteria domains. The results indicate not only that carbonic anhydrases are widely distributed in prokaryotes, but that th...

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“…Since Kw is dissociation constant of water, equation (27) can be modified, (28) where (CH+)o is the hydrogen ion concentration of the reaction system. The relationship between the kinetics of oxygen absorption and that of carbon dioxide absorption in pH-stat agitation system can be expressed in the following equation by substituting equation (23) into equation (28).…”

Section: Agitation Strengthmentioning

confidence: 99%