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. 2018 Dec;33(1):680-685.
doi: 10.1080/14756366.2018.1447570.

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

Andrea Angeli  1 , Fatmah A S Alasmary  2 , Sonia Del Prete  1   3 , Sameh M Osman  2 , Zeid AlOthman  2 , William A Donald  4 , Clemente Capasso  3 , Claudiu T Supuran  1   4
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The first activation study of a δ-carbonic anhydrase: TweCAδ from the diatom Thalassiosira weissflogii is effectively activated by amines and amino acids

Andrea Angeli et al. J Enzyme Inhib Med Chem. 2018 Dec.

Abstract

The activation of the δ-class carbonic anhydrase (CAs, EC 4.2.1.1) from the diatom Thalassiosira weissflogii (TweCAδ) was investigated using a panel of natural and non-natural amino acids and amines. The most effective activator of TweCAδ was d-Tyr (KA of 51 nM), whereas several other amino acids and amines, such as L-His, L-Trp, d-Trp, dopamine and serotonin were submicromolar activators (KAs from 0.51 to 0.93 µM). The most ineffective activator of TweCAδ was 4-amino-l-Phe (18.9 µM), 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 (KAs from 1.34 to 8.16 µM). For any δ-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.

Keywords: Carbonic anhydrase; Thalassiosira weissflogii; activators; diatoms; metalloenzymes.

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Figures

Figure 1.
Figure 1.
Amino acids 1–11 and amines 12–19 investigated as TweCAδ activators.
See this image and copyright information in PMC

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