Characterization of Fructose-1,6-Bisphosphate Aldolase 1 of Echinococcus multilocularis

Glycolysis is one of the important ways by which Echinococcus multilocularis acquires energy. Fructose-1, 6-bisphosphate aldolase (FBA) plays an important role in this process, but it is not fully characterized in E. multilocularis yet. The results of genome-wide analysis showed that the Echinococcus species contained four fba genes (FBA1-4), all of which had the domain of FBA I and multiple conserved active sites. EmFBA1 was mainly located in the germinal layer and the posterior of the protoscolex. The enzyme activity of EmFBA1 was 67.42 U/mg with K-m and V-max of 1.75 mM and 0.5 mmol/min, respectively. EmFBA1 was only susceptible to Fe3+ but not to the other four ions (Na+, Ca2+, K+, Mg2+), and its enzyme activity was remarkably lost in the presence of 0.5 mM Fe3+. The current study reveals the biochemical characters of EmFBA1 and is informative for further investigation of its role in the glycolysis in E. multilocularis.

Automated summary

Glycolysis is an important energy-acquiring pathway in Echinococcus multilocularis. Fructose-1, 6-bisphosphate aldolase (FBA) plays a crucial role in this process. Genome-wide analysis revealed the presence of four fba genes (FBA1-4) in Echinococcus species, with EmFBA1 being mainly expressed in the germinal layer and posterior of the protoscolex. EmFBA1 enzyme activity is susceptible to Fe3+ and significantly affected in its presence.