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Carbonic anhydrase activators: activation of the beta-carbonic anhydrase Nce103 from the yeast Saccharomyces cerevisiae with amines and amino acids.

Bioorganic & medicinal chemistry letters (2009-02-24)
Semra Isik, Feray Kockar, Meltem Aydin, Oktay Arslan, Ozen Ozensoy Guler, Alessio Innocenti, Andrea Scozzafava, Claudiu T Supuran
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.

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