Citrate synthase from the liver fluke Fasciola hepatica

Veronika L. Zinsser, Catherine M. Moore, Elizabeth M. Hoey, Alan Trudgett, David J. Timson

    Research output: Contribution to journalArticlepeer-review


    Citrate synthase catalyses the first step of the Krebs' tricarboxylic acid cycle. A sequence encoding citrate synthase from the common liver fluke, Fasciola hepatica, has been cloned. The encoded protein sequence is predicted to fold into a largely α-helical protein with high structural similarity to mammalian citrate synthases. Although a hexahistidine-tagged version of the protein could be expressed in Escherichia coli, it was not possible to purify it by nickel-affinity chromatography. Similar results were obtained with a version of the protein which lacks the putative mitochondrial targeting sequence (residues 1 to 29). However, extracts from bacterial cells expressing this version had additional citrate synthase activity after correcting for the endogenous, bacterial activity. The apparent K m for oxaloacetate was found to be 0.22 mM, which is higher than that observed in mammalian citrate synthases. Overall, the sequence and structure of F. hepatica citrate synthase are similar to ones from other eukaryotes, but there are enzymological differences which merit further investigation.

    Original languageEnglish
    Pages (from-to)2413-2417
    Number of pages5
    JournalParasitology Research
    Issue number6
    Publication statusPublished - 1 Jun 2013


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