The first activation study of a δ-carbonic anhydrase: TweCAδ from the diatom Thalassiosira weissflogii is effectively activated by amines and amino acids

The activation of the delta-class carbonic anhydrase (CAs, EC 4.2.1.1) from the diatom Thalassiosira weissflogii (TweCA delta) was investigated using a panel of natural and non-natural amino acids and amines. The most effective activator of TweCA delta was D-Tyr (K-A of 51 nM), whereas several other amino acids and amines, such as L-His, L-Trp, D-Trp, dopamine and serotonin were submicromolar activators (K(A)s from 0.51 to 0.93 mu M). The most ineffective activator of TweCA delta was 4-amino-L-Phe (18.9 mu M), whereas D-His, L-/D-Phe, L-/D-DOPA, L-Tyr, histamine, some pyridyl-alkylamines, L-adrenaline and aminoethyl-piperazine/morpholine were moderately potent activators (K(A)s from 1.34 to 8.16 mu M). For any delta-CA, there are no data on the crystal structure, homology modelling and the amino acid residues that are responsible for proton transfer to the active site are currently unknown making it challenging to provide a detailed rational for these findings. However, these data provide further evidence that this class of underexplored CA deserves more attention.