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Metabolites 2019, 9(2), 26; https://doi.org/10.3390/metabo9020026

Activation Studies of the β-Carbonic Anhydrase from the Pathogenic Protozoan Entamoeba histolytica with Amino Acids and Amines

1
Sezione di Scienze Farmaceutiche e Nutraceutiche, Dipartimento Neurofarba, Università degli Studi di Firenze, Via U. Schiff 6, 50019 Sesto Fiorentino, 50019 Florence, Italy
2
Faculty of Medicine and Health Technology, Tampere University, 33100 Tampere, Finland
3
Fimlab Ltd., Tampere University Hospital, 33100 Tampere, Finland
*
Author to whom correspondence should be addressed.
These authors equally contributed to the article.
Received: 24 December 2018 / Revised: 23 January 2019 / Accepted: 31 January 2019 / Published: 1 February 2019
(This article belongs to the Special Issue Carbonic Anhydrases and Metabolism)
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Abstract

The β-carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic protozoan Entamoeba histolytica, EhiCA, was investigated for its activation with a panel of natural and non-natural amino acids and amines. EhiCA was potently activated by D-His, D-Phe, D-DOPA, L- and D-Trp, L- and D-Tyr, 4-amino-L-Tyr, histamine and serotonin, with KAs ranging between 1.07 and 10.1 µM. The best activator was D-Tyr (KA of 1.07 µM). L-Phe, L-DOPA, L-adrenaline, L-Asn, L-Asp, L-Glu and L-Gln showed medium potency activation, with KAs of 16.5–25.6 µM. Some heterocyclic- alkyl amines, such as 2-pyridyl-methyl/ethyl-amine and 4-(2-aminoethyl)-morpholine, were devoid of EhiCA activating properties with KAs > 100 µM. As CA activators have poorly been investigated for their interaction with protozoan CAs, our study may be relevant for an improved understanding of the role of this enzyme in the life cycle of E. histolytica. View Full-Text
Keywords: Entamoeba histolytica; carbonic anhydrase; metalloenzymes; protozoan; amine; amino acid; activator Entamoeba histolytica; carbonic anhydrase; metalloenzymes; protozoan; amine; amino acid; activator
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Bua, S.; Haapanen, S.; Kuuslahti, M.; Parkkila, S.; Supuran, C.T. Activation Studies of the β-Carbonic Anhydrase from the Pathogenic Protozoan Entamoeba histolytica with Amino Acids and Amines. Metabolites 2019, 9, 26.

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