1. Effect of amino acids and amines on the activity of the recombinant ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii
- Author
-
Clemente Capasso, Viviana De Luca, Andrea Petreni, Claudiu T. Supuran, Vincenzo Carginale, and Andrea Scaloni
- Subjects
Burkholderia ,Kinetics ,RM1-950 ,medicine.disease_cause ,01 natural sciences ,activator ,law.invention ,Structure-Activity Relationship ,law ,Carbonic anhydrase ,Drug Discovery ,medicine ,Burkholderia territorii ,Amines ,Amino Acids ,Carbonic Anhydrases ,Pharmacology ,chemistry.chemical_classification ,Dose-Response Relationship, Drug ,Molecular Structure ,biology ,010405 organic chemistry ,Activator (genetics) ,General Medicine ,Recombinant Proteins ,ι-class ,0104 chemical sciences ,Amino acid ,010404 medicinal & biomolecular chemistry ,Enzyme ,amine ,chemistry ,Biochemistry ,kinetics ,Recombinant DNA ,biology.protein ,Amine gas treating ,Therapeutics. Pharmacology ,amino acid ,Research Article ,Research Paper - 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.
- Published
- 2021
- Full Text
- View/download PDF