Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase

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 Leish...

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Main Authors: Evelyn Rodríguez, Noelia Lander, Jose Luis Ramirez
Format: Article
Language:English
Published: Fundação Oswaldo Cruz (FIOCRUZ) 2009-08-01
Series:Memorias do Instituto Oswaldo Cruz
Subjects:
Online Access:http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762009000500014
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author Evelyn Rodríguez
Noelia Lander
Jose Luis Ramirez
author_facet Evelyn Rodríguez
Noelia Lander
Jose Luis Ramirez
author_sort Evelyn Rodríguez
collection DOAJ
description 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.
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spelling doaj.art-e050789e2a444789b35cc1b866af37712023-09-02T21:33:21ZengFundação Oswaldo Cruz (FIOCRUZ)Memorias do Instituto Oswaldo Cruz0074-02761678-80602009-08-01104574574810.1590/S0074-02762009000500014Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinaseEvelyn RodríguezNoelia LanderJose Luis RamirezThe 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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762009000500014Trypanosoma cruziKinetoplastidaphosphofructokinaseglycolytic enzymemolecular biochemical characterisation
spellingShingle Evelyn Rodríguez
Noelia Lander
Jose Luis Ramirez
Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase
Memorias do Instituto Oswaldo Cruz
Trypanosoma cruzi
Kinetoplastida
phosphofructokinase
glycolytic enzyme
molecular biochemical characterisation
title Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase
title_full Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase
title_fullStr Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase
title_full_unstemmed Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase
title_short Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase
title_sort molecular and biochemical characterisation of trypanosoma cruzi phosphofructokinase
topic Trypanosoma cruzi
Kinetoplastida
phosphofructokinase
glycolytic enzyme
molecular biochemical characterisation
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762009000500014
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