Literature

Abstract

The protein encoded by the Nce103 gene of Saccharomyces cerevisiae, a beta-carbonic anhydrase (CA, EC 4.2.1.1) designated as scCA, was investigated for its activation with amines and amino acids. scCA was poorly activated by amino acids such as l-/d-His, Phe, DOPA, Trp (K(A)s of 82-90 microM) and more effectively activated by amines such as histamine, dopamine, serotonin, pyridyl-alkylamines, aminoethyl-piperazine/morpholine (K(A)s of 10.2-21.3 microM). The best activator was l-adrenaline, with an activation constant of 0.95 microM. This study may help to better understand the catalytic/activation mechanisms of the beta-CAs and eventually to design modulators of CA activity for similar enzymes present in pathogenic fungi, such as Candida albicans and Cryptococcus neoformans.

DOI： 10.1016/j.bmcl.2009.01.105

Carbonic anhydrase activators: Activation of the β-carbonic anhydrase Nce103 from the yeast Saccharomyces cerevisiae with amines and amino acids

Bioorganic & Medicinal Chemistry Letters 2009.0

Carbonic anhydrase activators: Activation of the β-carbonic anhydrase from the pathogenic yeast Candida glabrata with amines and amino acids

Bioorganic & Medicinal Chemistry Letters 2010.0

Carbonic anhydrase activators: Activation of the β-carbonic anhydrases from the pathogenic fungi Candida albicans and Cryptococcus neoformans with amines and amino acids

Bioorganic & Medicinal Chemistry 2010.0

Carbonic anhydrase activators: Activation of the β-carbonic anhydrase from Malassezia globosa with amines and amino acids

Bioorganic & Medicinal Chemistry Letters 2016.0

Carbonic anhydrase inhibitors. Inhibition of the β-class enzyme from the yeast Saccharomyces cerevisiae with anions

Bioorganic & Medicinal Chemistry Letters 2008.0

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