title: The first activation study of a bacterial carbonic anhydrase (CA). The thermostable α-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines.
abstract: The α-carbonic anhydrase (CA, EC 4.2.1.1) from the newly discovered thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 (SspCA) was investigated for its activation with a series of amino acids and amines. D-His, L-Phe, L-Tyr, L- and D-Trp were the most effective SspCA activators, with activation constants in the range of 1-12 nM, whereas L-His, L/D-DOPA, D-Tyr, and several biogenic amines/catecholamines were slightly less effective activators (K(A) in the range of 37 nM-0.97 μM). The least effective SspCA activator was d-Phe (K(A) of 5.13 μM). The thermal stability, robustness and very high catalytic activity of SspCA make this enzyme an ideal candidate for biomimetic CO(2) capture processes.
authors.affiliation: Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Sesto Fiorentino, Florence, Italy.
authors.forename: Daniela
authors.initials: D
authors.lastname: Vullo
authors.forename: Viviana
authors.initials: V
authors.lastname: De Luca
authors.forename: Andrea
authors.initials: A
authors.lastname: Scozzafava
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Carginale
authors.forename: Mosè
authors.initials: M
authors.lastname: Rossi
authors.forename: Claudiu T
authors.initials: CT
authors.lastname: Supuran
authors.forename: Clemente
authors.initials: C
authors.lastname: Capasso
mesh_terms: D000588:Amines / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism; D002245:Carbon Dioxide / Q000378:metabolism; D002256:Carbonic Anhydrases / Q000378:metabolism*; D004789:Enzyme Activation; D006091:Gram-Negative Chemolithotrophic Bacteria / Q000201:enzymology*; D007700:Kinetics
chemical_list: D000588:Amines; D000596:Amino Acids; D002245:Carbon Dioxide; D002256:Carbonic Anhydrases