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.

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 1-12nM, whereas l-His, l/d-DOPA, d-Tyr, and several biogenic amines/catecholamines were slightly less effective activators (K(A) in the range of 37nM-0.97μM). The least effective SspCA activator was d-Phe (K(A) of 5.13μM). The thermal stability, robustness and very high catalytic activity of SspCA make this enzyme an ideal candidate for biomimetic CO(2) capture processes.