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 Fe(3+) but not to the other four ions (Na(+), Ca(2+), K(+), Mg(2+)), and its enzyme activity was remarkably lost in the presence of 0.5 mM Fe(3+). The current study reveals the biochemical characters of EmFBA1 and is informative for further investigation of its role in the glycolysis in E. multilocularis.