Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1367381 | Bioorganic & Medicinal Chemistry Letters | 2006 | 5 Pages |
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.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Claudia Temperini, Andrea Scozzafava, Claudiu T. Supuran,