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

By Claudiu T Supuran, Giuseppina De Simone

ISBN-10: 0444632581

ISBN-13: 9780444632586

Carbonic anhydrases (CAs, EC 4.2.1.1) are ubiquitous metalloenzymes, current all through so much dwelling organisms and encoded by means of 5 evolutionarily unrelated gene households. The Carbonic Anhydrases as Biocatalysts:From idea to clinical and commercial Applications provides info at the starting to be curiosity within the learn of this enzyme relatives and their functions to either medication and biotechnology.

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

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Download e-book for kindle: Carbonic Anhydrases as Biocatalysts: From Theory to Medical by Claudiu T Supuran, Giuseppina De Simone

Carbonic anhydrases (CAs, EC four. 2. 1. 1) are ubiquitous metalloenzymes, current all through such a lot residing organisms and encoded through 5 evolutionarily unrelated gene households. The Carbonic Anhydrases as Biocatalysts:From conception to scientific and commercial purposes provides info at the growing to be curiosity within the learn of this enzyme family members and their purposes to either drugs and biotechnology.

Additional resources for Carbonic Anhydrases as Biocatalysts: From Theory to Medical and Industrial Applications

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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.

Temperini C, Innocenti A, Guerri A, Scozzafava A, Rusconi S, Supuran CT. Phosph(on)ate as a zincbinding group in metalloenzyme inhibitors: x-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I. Bioorg Med Chem Lett 2007;17:2210–5. 21. Alterio V, Monti SM, Truppo E, Pedone C, Supuran CT, De Simone G. The first example of a significant active site conformational rearrangement in a carbonic anhydrase-inhibitor adduct: the carbonic anhydrase I-topiramate complex.

On the contrary, the hydrophilic half of the active site facilitates the binding of the polar components generated from the CO2 hydration reaction (bicarbonate and protons) and their release from the cavity toward the environment. At least for the protons, it is, in fact, well demonstrated that a relay of water molecules and several histidines (proton shuttling residues other than His64) are involved in such processes (57,58).

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


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