Literature

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.

DOI： 10.1016/j.bmcl.2006.07.021

Carbonic anhydrase activators: The first X-ray crystallographic study of an adduct of isoform I

Bioorganic & Medicinal Chemistry Letters 2006.0

Carbonic anhydrase activators: X-ray crystal structure of the adduct of human isozyme II with l-histidine as a platform for the design of stronger activators

Bioorganic & Medicinal Chemistry Letters 2005.0

Carbonic anhydrase activators: l-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV

Bioorganic & Medicinal Chemistry Letters 2007.0

Carbonic anhydrase activators: Kinetic and X-ray crystallographic study for the interaction of d- and l-tryptophan with the mammalian isoforms I–XIV

Bioorganic & Medicinal Chemistry 2008.0

Carbonic anhydrase activators: Activation of human isozymes I, II and IX with phenylsulfonylhydrazido l-histidine derivatives

Bioorganic & Medicinal Chemistry Letters 2009.0

Carbonic anhydrase activators: Activation of the human cytosolic isozyme III and membrane-associated isoform IV with amino acids and amines