期刊
METABOLITES
卷 9, 期 2, 页码 -出版社
MDPI
DOI: 10.3390/metabo9020026
关键词
Entamoeba histolytica; carbonic anhydrase; metalloenzymes; protozoan; amine; amino acid; activator
资金
- Academy of Finland
- Sigrid Juselius Foundation
- Jane and Aatos Erkko Foundation
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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