Carbonic anhydrases (CAs, EC 4.2.1.1) are ubiquitous metalloenzymes, present throughout most living organisms and encoded by five evolutionarily unrelated gene families: the α-, β-, γ-, δ-, and ζ-CAs The α- β- and δ-CAs contain a Zn(II) ion at the active site, the γ-CAs are probably Fe(II) enzymes (but they are active also with Zn(II) or Co(II) ions), while the metal ion is usually replaced by cadmium in the ζ-CAs. Herein we report a state of the art structural crystallographyc investigation.

Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms? / V. Alterio;A. D. Fiore;K. D'Ambrosio;C. T. Supuran;G. D. Simone. - In: CHEMICAL REVIEWS. - ISSN 0009-2665. - STAMPA. - 112:(2012), pp. 4421-4468. [10.1021/cr200176r]

Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms?

SUPURAN, CLAUDIU TRANDAFIR;
2012

Abstract

Carbonic anhydrases (CAs, EC 4.2.1.1) are ubiquitous metalloenzymes, present throughout most living organisms and encoded by five evolutionarily unrelated gene families: the α-, β-, γ-, δ-, and ζ-CAs The α- β- and δ-CAs contain a Zn(II) ion at the active site, the γ-CAs are probably Fe(II) enzymes (but they are active also with Zn(II) or Co(II) ions), while the metal ion is usually replaced by cadmium in the ζ-CAs. Herein we report a state of the art structural crystallographyc investigation.
2012
112
4421
4468
V. Alterio;A. D. Fiore;K. D'Ambrosio;C. T. Supuran;G. D. Simone
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/776392
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