Journal
METABOLITES
Volume 9, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/metabo9020026
Keywords
Entamoeba histolytica; carbonic anhydrase; metalloenzymes; protozoan; amine; amino acid; activator
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Funding
- Academy of Finland
- Sigrid Juselius Foundation
- Jane and Aatos Erkko Foundation
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The beta-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 K(A)s ranging between 1.07 and 10.1 mu M. The best activator was D-Tyr (K-A of 1.07 mu M). L-Phe, L-DOPA, L-adrenaline, L-Asn, L-Asp, L-Glu and L-Gln showed medium potency activation, with K(A)s of 16.5-25.6 mu M. Some heterocyclic- alkyl amines, such as 2-pyridyl-methyl/ethyl-amine and 4-(2-aminoethyl)-morpholine, were devoid of EhiCA activating properties with K(A)s > 100 mu M. 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.
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