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 1–12 nM, whereas l-His, l/d-DOPA, d-Tyr, and several biogenic amines/catecholamines were slightly less effective activators (KA in the range of 37 nM–0.97 μM). The least effective SspCA activator was d-Phe (KA of 5.13 μM). The thermal stability, robustness and very high catalytic activity of SspCA make this enzyme an ideal candidate for biomimetic CO2 capture processes.

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