Literature

Abstract

The activation of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1) with L-adrenaline and histamine has been investigated by kinetic and X-ray crystallographic studies. L-Adrenaline behaves as a potent activator of isozyme CA I (activation constant of 90 nM), being a much weaker activator of isozyme CA II (activation constant of 96 microM). Isoforms CA IV, VA, VII, and XIV were activated by L-adrenaline with K(A)s in the range of 36-63 microM. The X-ray crystal structure of the CA II-L-adrenaline adduct revealed that the activator plugs the entrance of the active site cavity, obstructing it almost completely.

DOI： 10.1016/j.bmcl.2006.11.027

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: 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: 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 isoforms VII (cytosolic) and XIV (transmembrane) with amino acids and amines

Bioorganic & Medicinal Chemistry Letters 2007.0

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

Bioorganic & Medicinal Chemistry Letters 2008.0

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