A Combined Crystallographic and Theoretical Study Explains the Capability of Carboxylic Acids to Adopt Multiple Binding Modes in the Active Site of Carbonic Anhydrases. Issue 1 (30th November 2015)

• Record Type: Journal Article
• Authors: Langella, Emma; D'Ambrosio, Katia; D'Ascenzio, Melissa; Carradori, Simone; Monti, Simona M.; Supuran, Claudiu T.; De Simone, Giuseppina
• Is Part Of: Chemistry. Volume 22:Issue 1(2016)
• Page Start: 97
• Page End: 100
• Publication Date: 2015-11-30
• Subjects: carbonic anhydrases -- drug design -- inhibitors -- theoretical calculations -- X‐ray structures; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201503748
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract: Carboxylates are the least investigated class of inhibitors of carbonic anhydrases (CAs). Here we explain the versatility of binding of these molecules to CAs by examining a new adduct of hCA II with N‐carboxymethyl‐saccharin. Abstract : Mapping enzymes : Carboxylates are the least investigated class of inhibitors of carbonic anhydrases (CAs). Here we explain the versatility of binding of these molecules to CAs by examining a new adduct of CA II with N ‐carboxymethyl‐saccharin (see figure).