Effect of amino acids and amines on the activity of the recombinant ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii |
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| Authors: | Viviana De Luca Andrea Petreni Vincenzo Carginale Andrea Scaloni Claudiu T. Supuran Clemente Capasso |
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| Affiliation: | aDepartment of Neurofarba, Sezione di Scienze Farmaceutiche, Università degli Studi di Firenze, Polo Scientifico, Florence, Italy;bProteomics & Mass Spectrometry Laboratory, Institute for the Animal Production System in the Mediterranean Environment, CNR, Naples, Italy;cDepartment of Biology, Agriculture and Food Sciences, CNR, Institute of Biosciences and Bioresources, Napoli, Italy |
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| Abstract: | We here report a study on the activation of the ι-class bacterial CA from Burkholderia territorii (BteCAι). This protein was recently characterised as a zinc-dependent enzyme that shows a significant catalytic activity (kcat 3.0 × 105 s−1) for the physiological reaction of CO2 hydration to bicarbonate and protons. Some amino acids and amines, among which some proteinogenic derivatives as well as histamine, dopamine and serotonin, showed efficient activating properties towards BteCAι, with activation constants in the range 3.9–13.3 µM. L-Phe, L-Asn, L-Glu, and some pyridyl-alkylamines, showed a weaker activating effect towards BteCAι, with KA values ranging between 18.4 µM and 45.6 µM. Nowadays, no information is available on active site architecture, metal ion coordination and catalytic mechanism of members of the ι-group of CAs, and this study represents another contribution towards a better understanding of this still uncharacterised class of enzymes. |
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| Keywords: | Carbonic anhydrase, ι -class, activator, kinetics, amino acid, amine |
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