| Literature DB >> 33000794 |
Katia D'Ambrosio1, Simone Carradori2, Stefania Cesa3, Andrea Angeli4, Simona M Monti1, Claudiu T Supuran4, Giuseppina De Simone1.
Abstract
To date, catechols have been only poorly investigated as carbonic anhydrase (CA) inhibitors. Here we report the first structural information on the CA inhibition mechanism of these molecules, showing that they adopt a peculiar binding mode to the enzyme active site which involves the zinc-bound water molecule and the "deep water".Entities:
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Year: 2020 PMID： 33000794 DOI： 10.1039/d0cc05172a
Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.222