Trypanosoma evansi contains two auxiliary enzymes of glycolytic metabolism: Phosphoenolpyruvate carboxykinase and pyruvate phosphate dikinase

Luz Amira Rivero, Juan Luis Concepción, Ender Quintero-Troconis, Wilfredo Quiñones, Paul A M Michels, Héctor Acosta*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Trypanosoma evansi is a monomorphic protist that can infect horses and other animal species of economic importance for man. Like the bloodstream form of the closely related species Trypanosoma brucei, T. evansi depends exclusively on glycolysis for its free-energy generation. In T. evansi as in other kinetoplastid organisms, the enzymes of the major part of the glycolytic pathway are present within organelles called glycosomes, which are authentic but specialized peroxisomes. Since T. evansi does not undergo stage-dependent differentiations, it occurs only as bloodstream forms, it has been assumed that the metabolic pattern of this parasite is identical to that of the bloodstream form of T. brucei. However, we report here the presence of two additional enzymes, phosphoenolpyruvate carboxykinase and PPi-dependent pyruvate phosphate dikinase in T. evansi glycosomes. Their colocalization with glycolytic enzymes within the glycosomes of this parasite has not been reported before. Both enzymes can make use of PEP for contributing to the production of ATP within the organelles. The activity of these enzymes in T. evansi glycosomes drastically changes the model assumed for the oxidation of glucose by this parasite.

Original languageEnglish
Pages (from-to)7-15
Number of pages9
JournalExperimental Parasitology
Volume165
Early online date9 Mar 2016
DOIs
Publication statusPublished - 1 Jun 2016

Keywords

  • glycosome
  • metabolism
  • Phosphoenolpyruvate carboxykinase
  • Phosphoglycerate kinase
  • Pyruvate phosphate dikinase
  • Trypanosoma evansi

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