Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase

Memórias do Instituto Oswaldo Cruz

Evelyn Rodríguez¹  Noelia Lander¹  Jose Luis Ramirez¹ 

[1] ,Instituto de Estudios Avanzados Centro de Biotecnología Caracas,Venezuela

关键词: Trypanosoma cruzi;    Kinetoplastida;    phosphofructokinase;    glycolytic enzyme;    molecular biochemical characterisation;   

DOI  :  10.1590/S0074-02762009000500014

来源: SciELO

【 摘 要 】

The characterisation of the gene encoding Trypanosoma cruzi CL Brener phosphofructokinase (PFK) and the biochemical properties of the expressed enzyme are reported here. In contradiction with previous reports, the PFK genes of CL Brener and YBM strain T. cruzi were found to be similar to their Leishmania mexicana and Trypanosoma brucei homologs in terms of both kinetic properties and size, with open reading frames encoding polypeptides with a deduced molecular mass of 53,483. The predicted amino acid sequence contains the C-terminal glycosome-targeting tripeptide SKL; this localisation was confirmed by immunofluorescence assays. In sequence comparisons with the genes of other eukaryotes, it was found that, despite being an adenosine triphosphate-dependent enzyme, T. cruzi PFK shows significant sequence similarity with inorganic pyrophosphate-dependent PFKs.

【 授权许可】

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