Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase

Detalhes bibliográficos
Autor(a) principal: Rodríguez,Evelyn
Data de Publicação: 2009
Outros Autores: Lander,Noelia, Ramirez,Jose Luis
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Memórias do Instituto Oswaldo Cruz
Texto Completo: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762009000500014
Resumo: 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 Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinaseTrypanosoma cruziKinetoplastidaphosphofructokinaseglycolytic enzymemolecular biochemical characterisationThe 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.Instituto Oswaldo Cruz, Ministério da Saúde2009-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762009000500014Memórias do Instituto Oswaldo Cruz v.104 n.5 2009reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02762009000500014info:eu-repo/semantics/openAccessRodríguez,EvelynLander,NoeliaRamirez,Jose Luiseng2020-04-25T17:50:31Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:16:21.065Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue
dc.title.none.fl_str_mv Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase
title Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase
spellingShingle Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase
Rodríguez,Evelyn
Trypanosoma cruzi
Kinetoplastida
phosphofructokinase
glycolytic enzyme
molecular biochemical characterisation
title_short 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_sort Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase
author Rodríguez,Evelyn
author_facet Rodríguez,Evelyn
Lander,Noelia
Ramirez,Jose Luis
author_role author
author2 Lander,Noelia
Ramirez,Jose Luis
author2_role author
author
dc.contributor.author.fl_str_mv Rodríguez,Evelyn
Lander,Noelia
Ramirez,Jose Luis
dc.subject.por.fl_str_mv Trypanosoma cruzi
Kinetoplastida
phosphofructokinase
glycolytic enzyme
molecular biochemical characterisation
topic Trypanosoma cruzi
Kinetoplastida
phosphofructokinase
glycolytic enzyme
molecular biochemical characterisation
dc.description.none.fl_txt_mv 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.
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.
publishDate 2009
dc.date.none.fl_str_mv 2009-08-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762009000500014
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762009000500014
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0074-02762009000500014
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
dc.source.none.fl_str_mv Memórias do Instituto Oswaldo Cruz v.104 n.5 2009
reponame:Memórias do Instituto Oswaldo Cruz
instname:Fundação Oswaldo Cruz
instacron:FIOCRUZ
reponame_str Memórias do Instituto Oswaldo Cruz
collection Memórias do Instituto Oswaldo Cruz
instname_str Fundação Oswaldo Cruz
instacron_str FIOCRUZ
institution FIOCRUZ
repository.name.fl_str_mv Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz
repository.mail.fl_str_mv
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