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The liver fluke zoonoses,  Fasciola  spp. are parasitic helminths infecting humans and animals globally. Recent sequencing of the genome of  Fasciola gigantica  has provided a basis to understand the biochemistry of this parasite. Here, we identified the cytosolic malate dehydrogenase in  F. gigantica  (FgMDH) and characterized the enzyme biochemically and structurally.  F. gigantica  encodes a single cytosolic MDH, a key enzyme of the citric acid cycle. It catalyzes the reversible oxidation of malate to oxaloacetate using NAD + . The  Fgmdh  gene was amplified and cloned for expression of the recombinant protein. The purified protein showed a molecular weight of ~ 36 kDa that existed in a dimeric form in solution. The recombinant enzyme was catalytically active as it catalyzed both forward and reverse reactions efficiently. The kinetic parameters were determined for both directions. The structure of FgMDH and human MDH were modeled and validated. The superimposition of both the model structures showed overall structural similarity in the active site loop region, however, the conformation of the residues was different. Molecular docking elucidated the binding sites and affinities of the substrates and cofactors to the enzyme. Simulation of molecular dynamics and principal component analysis indicated the stability of the systems and collective motions, respectively. Understanding the structural and functional properties of MDH is important to better understand the roles of this enzyme in the biochemistry of the parasite.

Identification and characterization of cytosolic malate dehydrogenase from the liver fluke Fasciola gigantica