title: Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors.
abstract: Hydroxamates (R-CONHOH) have been scarcely investigated as carbonic anhydrase (CA, EC 4.2.1.1) inhibitors (CAIs). An inhibition/structural study of PhCONHOH is reported against all human isoforms. Comparing aliphatic (R = Me and CF(3)) and aromatic (R = Ph) hydroxamates as CAIs, we prove that CONHOH is a versatile zinc binding group. Depending on the nature of the R moiety, it can adopt different coordination modes to the catalytic ion within the CA active site.
authors: Istituto di Biostrutture e Bioimmagini - CNR, Napoli, Italy.
authors: Anna
authors: A
authors: Di Fiore
authors: Alfonso
authors: A
authors: Maresca
authors: Claudiu T
authors: CT
authors: Supuran
authors: Giuseppina
authors: G
authors: De Simone
mesh_terms: D002257:Carbonic Anhydrase Inhibitors / Q000737:chemistry*; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000378:metabolism; D020134:Catalytic Domain; D002614:Chelating Agents / Q000737:chemistry*; D056831:Coordination Complexes; D018360:Crystallography, X-Ray; D006801:Humans; D006877:Hydroxamic Acids / Q000737:chemistry*; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D013329:Structure-Activity Relationship; D013449:Sulfonamides / Q000737:chemistry; D015032:Zinc / Q000737:chemistry*
chemical_list: D002257:Carbonic Anhydrase Inhibitors; D002614:Chelating Agents; D056831:Coordination Complexes; D006877:Hydroxamic Acids; D007527:Isoenzymes; D013449:Sulfonamides; D002256:Carbonic Anhydrases; D015032:Zinc