title: Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I.
abstract: The X-ray crystallographic structure for the adduct of an activator with human carbonic anhydrase isozyme I (hCA I) is reported. L-Histidine binds deep within the enzyme active site, participating in a network of hydrogen bonds involving its carboxylate moiety and the zinc-bound water molecule, as well as the imidazole of His200, being in van der Waals contacts with Thr199, His200, His64, and His67. This binding is very different from that to the other major cytosolic isozyme hCA II.
authors.affiliation: Università degli Studi di Firenze, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, I-50019 Sesto Fiorentino, Firenze, Italy.
authors.forename: Claudia
authors.initials: C
authors.lastname: Temperini
authors.forename: Andrea
authors.initials: A
authors.lastname: Scozzafava
authors.forename: Claudiu T
authors.initials: CT
authors.lastname: Supuran
mesh_terms: D000596:Amino Acids; D001665:Binding Sites; D024401:Carbonic Anhydrase I / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004789:Enzyme Activation; D006639:Histidine / Q000737:chemistry*; D006801:Humans; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D011485:Protein Binding; D013329:Structure-Activity Relationship
chemical_list: D000596:Amino Acids; D006639:Histidine; D024401:Carbonic Anhydrase I