Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I.
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.
Temperini
Claudia
C
Università degli Studi di Firenze, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, I-50019 Sesto Fiorentino, Firenze, Italy.
Scozzafava
Andrea
A
Supuran
Claudiu T
CT
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
D000596:Amino Acids; D006639:Histidine; D024401:Carbonic Anhydrase I