Activation Studies of the β-Carbonic Anhydrase from the Pathogenic Protozoan Entamoeba histolytica with Amino Acids and Amines
| Autor: | Susanna Haapanen, Seppo Parkkila, Marianne Kuuslahti, Silvia Bua, Claudiu T. Supuran |
|---|---|
| Přispěvatelé: | Lääketieteen ja terveysteknologian tiedekunta - Faculty of Medicine and Health Technology, Laboratoriopalvelut - Laboratory Services, Tampere University |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Endocrinology
Diabetes and Metabolism Metalloenzymes carbonic anhydrase lcsh:QR1-502 01 natural sciences Biochemistry lcsh:Microbiology Article activator Biokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biology chemistry.chemical_compound Entamoeba histolytica Carbonic anhydrase parasitic diseases Activator Molecular Biology Amine chemistry.chemical_classification metalloenzymes biology 010405 organic chemistry Activator (genetics) protozoan biology.organism_classification 0104 chemical sciences Amino acid 010404 medicinal & biomolecular chemistry Enzyme chemistry amine Protozoan biology.protein Amine gas treating Serotonin Histamine amino acid |
| Zdroj: | Metabolites Volume 9 Issue 2 Metabolites, Vol 9, Iss 2, p 26 (2019) |
| ISSN: | 2218-1989 |
| DOI: | 10.3390/metabo9020026 |
| Popis: | 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 KAs ranging between 1.07 and 10.1 M. The best activator was D-Tyr (KA of 1.07 µ M). L-Phe, L-DOPA, L-adrenaline, L-Asn, L-Asp, L-Glu and L-Gln showed medium potency activation, with KAs of 16.5&ndash 25.6 µ M. 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 µ 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. |
| Databáze: | OpenAIRE |
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