Literature

Abstract

The activity of the coral Stylophora pystillata secretory carbonic anhydrase STPCA has been tested in presence of amino acids and amines. All the investigated compounds showed a positive, activating effect on k(cat) and have been separated in weak (K(A) in the range of 21-126 microM), medium (10.1-19 microM) and strong enzyme activators (K(A) of 0.18-3.21 microM). D-DOPA was found to be the best coral enzyme activator, with an activation constant K(A) of 0.18 microM. This enhancement of STPCA activity, as well as previous enzyme inhibition results, might now be tested on living organisms to better understand the role played by these enzymes in the coral calcification processes.

DOI： 10.1016/j.bmc.2010.01.059

Carbonic anhydrase activators. The first activation study of a coral secretory isoform with amino acids and amines

Bioorganic & Medicinal Chemistry 2010.0

Carbonic anhydrase inhibitors. Inhibition studies with anions and sulfonamides of a new cytosolic enzyme from the scleractinian coral Stylophora pistillata

Bioorganic & Medicinal Chemistry Letters 2011.0

Carbonic anhydrase inhibitors: Inhibition studies of a coral secretory isoform with inorganic anions

Bioorganic & Medicinal Chemistry Letters 2009.0

Carbonic anhydrase inhibitors. Inhibition studies of a coral secretory isoform by sulfonamides

Bioorganic & Medicinal Chemistry 2009.0

Carbonic anhydrase activators: Activation of isozyme XIII with amino acids and amines

Bioorganic & Medicinal Chemistry Letters 2006.0

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