By Claudiu T Supuran, Giuseppina De Simone

Carbonic anhydrases (CAs, EC 4.2.1.1) are ubiquitous metalloenzymes, current all through such a lot dwelling organisms and encoded via 5 evolutionarily unrelated gene households. The Carbonic Anhydrases as Biocatalysts:From thought to scientific and business Applications offers details at the starting to be curiosity within the research of this enzyme kin and their functions to either drugs and biotechnology.

  • Offers complete insurance of the carbonic anhydrases enzyme kinfolk and their houses as biocatalysts
  • Includes present purposes of carbonic anhydrases in biotechnology at the foundation in their catalytic potency, together with new applied sciences for CO2 catch processes
  • Identifies new ambitions for drug layout studies
  • Provides a selectivity profile for different carbonic anhydrases and their similar biomedical applications

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Extra info for Carbonic Anhydrases as Biocatalysts: From Theory to Medical and Industrial Applications

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22. Takaoka Y, Kioi Y, Morito A, Otani J, Arita K, Ashihara E, et al. Quantitative comparison of protein dynamics in live cells and in vitro by in-cell 19F-NMR. Chem Commun 2013;49:2801–3. 23. Supuran CT, Scozzafava A, Casini A. Carbonic anhydrase inhibitors. Med Res Rev 2003;23:146–89. 24. Supuran CT, Scozzafava A. Carbonic anhydrase inhibitors and their therapeutic potential. Expert Opin Ther Targets 2000;10:575–600. 25. Ren X, Lindskog S. Buffer dependence of CO2 hydration catalyzed by human carbonic anhydrase I.

Carbonic anhydrase inhibitors: synthesis and inhibition of the human carbonic anhydrase isoforms I, II, VII, IX and XII with benzene sulfonamides incorporating 4,5,6,7-tetrabromophthalimide moiety. Bioorg Med Chem 2013;21:5973–82. 69. Scozzafava A, Supuran C. Carbonic anhydrase inhibitors: ureido and thioureido derivatives of aromatic sulfonamides possessing increased affinities for isozyme I. A novel route to 2,5-disubstituted1,3,4-thiadiazoles via thioureas, and their interaction with isozymes I, II and IV.

Fierke CA, Calderone TL, Krebs JF. Functional consequences of engineering the hydrophobic pocket of carbonic anhydrase II. Biochemistry 1991;30:11054–63. 69. Alexander RS, Nair SK, Christianson DW. Engineering the hydrophobic pocket of carbonic anhydrase II. Biochemistry 1991;30:11064–72. 70. Tu CK, Silverman DN, Forsman C, Jonsson BH, Lindskog S. Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant. Biochemistry 1989;28: 7913–8. 71.

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Carbonic Anhydrases as Biocatalysts: From Theory to Medical by Claudiu T Supuran, Giuseppina De Simone
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