Cloning of a pyruvate phosphate dikinase from Trypanosoma cruzi

Rosa A. Maldonado, Alan H. Fairlamb (Lead / Corresponding author)

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    14 Citations (Scopus)


    We have cloned and characterised a gene that encodes a putative pyruvate phosphate dikinase (PPDK) from Trypanosoma cruzi, an enzyme that catalyses the reversible conversion of phosphoenolpyruvate to pyruvate. PPDK is absent in mammalian cells, but has been found in a wide variety of other organisms, including plants and bacteria. In T. cruzi, two genes (PPDK1 and PPDK2) are present in a tandem array localised on a 1 Mbp chromosome. Northern and Western blot analyses indicates that PPDK is expressed as a 100-kDa protein in epimastigote, amastigote and trypomastigote forms. PPDK1 and PPDK2 encode an identical protein of 100.8 kDa with a C-terminal extension ending with the sequence AKL, a signal for glycosomal import. Both T. cruzi and T. brucei enzymes possess a 23-residue insertion, that is absent in other PPDKs. A three-dimensional alignment with the crystal structure of the enzyme from Clostridium symbiosum predicts that this insertion is located on the surface of the nucleotide-binding domain. Phylogenetic studies indicate that bacterial and protist PPDKs cluster as a separate group from those of plants. The evolutionary implications and possible role of this enzyme in T. cruzi is discussed.

    Original languageEnglish
    Pages (from-to)183-191
    Number of pages9
    JournalMolecular and Biochemical Parasitology
    Issue number2
    Publication statusPublished - Feb 2001


    • Gluconeogenesis
    • Metabolism
    • Pyruvate orthophosphate dikinase
    • Trypanosoma

    ASJC Scopus subject areas

    • Parasitology
    • Molecular Biology


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