Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei

Autores
Leroux, Alejandro Ezequiel; Maugeri, Dante A.; Opperdoes, Fred R.; Cazzulo, Juan Jose; Nowicki, Cristina
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Comparative studies showed that, like Trypanosoma cruzi, Trypanosoma brucei exhibits functional cytosolic and mitochondrial malic enzymes (MEs), which are specifically linked to NADP. Kinetic studies provided evidence that T. cruzi and T.brucei MEs display similarly high affinities towards NADP1 and are also almost equally efficient in catalyzing the production of NADPH. Nevertheless, in contrast to the cytosolic ME from T. cruzi, which is highly activated by L-aspartate (over 10-fold), the T. brucei homologue is slightly more active (50%) in the presence of this amino acid. In T. brucei, both isozymes appear to be clearly more abundant in the insect stage, although they can be immunodetected in the bloodstream forms. By contrast, in T. cruzi the expression of the mitochondrial ME seems to be clearly upregulated in amastigotes, whereas the cytosolic isoform appears to be more abundant in the insect stages of the parasite. It might be hypothesized that in those environments where glucose is very low or absent, these pathogens depend on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power.
Fil: Leroux, Alejandro Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Maugeri, Dante A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Opperdoes, Fred R.. Université Catholique de Louvain; Bélgica
Fil: Cazzulo, Juan Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Nowicki, Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Materia
Trypanosoma cruzi
Trypanosoma brucei
Enzimas málicas
Propiedades bioquímicas
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/278225
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/278225
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma bruceiLeroux, Alejandro EzequielMaugeri, Dante A.Opperdoes, Fred R.Cazzulo, Juan JoseNowicki, CristinaTrypanosoma cruziTrypanosoma bruceiEnzimas málicasPropiedades bioquímicashttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Comparative studies showed that, like Trypanosoma cruzi, Trypanosoma brucei exhibits functional cytosolic and mitochondrial malic enzymes (MEs), which are specifically linked to NADP. Kinetic studies provided evidence that T. cruzi and T.brucei MEs display similarly high affinities towards NADP1 and are also almost equally efficient in catalyzing the production of NADPH. Nevertheless, in contrast to the cytosolic ME from T. cruzi, which is highly activated by L-aspartate (over 10-fold), the T. brucei homologue is slightly more active (50%) in the presence of this amino acid. In T. brucei, both isozymes appear to be clearly more abundant in the insect stage, although they can be immunodetected in the bloodstream forms. By contrast, in T. cruzi the expression of the mitochondrial ME seems to be clearly upregulated in amastigotes, whereas the cytosolic isoform appears to be more abundant in the insect stages of the parasite. It might be hypothesized that in those environments where glucose is very low or absent, these pathogens depend on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power.Fil: Leroux, Alejandro Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Maugeri, Dante A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); ArgentinaFil: Opperdoes, Fred R.. Université Catholique de Louvain; BélgicaFil: Cazzulo, Juan Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); ArgentinaFil: Nowicki, Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaWiley Blackwell Publishing, Inc2011-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/278225Leroux, Alejandro Ezequiel; Maugeri, Dante A.; Opperdoes, Fred R.; Cazzulo, Juan Jose; Nowicki, Cristina; Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei; Wiley Blackwell Publishing, Inc; FEMS Microbiology Letters; 314; 1; 6-2011; 25-330378-1097CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/femsle/article-abstract/314/1/25/552119?redirectedFrom=fulltextinfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1574-6968.2010.02142.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T13:17:10Zoai:ri.conicet.gov.ar:11336/278225instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-12-23 13:17:10.73CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei
title Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei
spellingShingle Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei
Leroux, Alejandro Ezequiel
Trypanosoma cruzi
Trypanosoma brucei
Enzimas málicas
Propiedades bioquímicas
title_short Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei
title_full Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei
title_fullStr Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei
title_full_unstemmed Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei
title_sort Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei
dc.creator.none.fl_str_mv Leroux, Alejandro Ezequiel
Maugeri, Dante A.
Opperdoes, Fred R.
Cazzulo, Juan Jose
Nowicki, Cristina
author Leroux, Alejandro Ezequiel
author_facet Leroux, Alejandro Ezequiel
Maugeri, Dante A.
Opperdoes, Fred R.
Cazzulo, Juan Jose
Nowicki, Cristina
author_role author
author2 Maugeri, Dante A.
Opperdoes, Fred R.
Cazzulo, Juan Jose
Nowicki, Cristina
author2_role author
author
author
author
dc.subject.none.fl_str_mv Trypanosoma cruzi
Trypanosoma brucei
Enzimas málicas
Propiedades bioquímicas
topic Trypanosoma cruzi
Trypanosoma brucei
Enzimas málicas
Propiedades bioquímicas
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Comparative studies showed that, like Trypanosoma cruzi, Trypanosoma brucei exhibits functional cytosolic and mitochondrial malic enzymes (MEs), which are specifically linked to NADP. Kinetic studies provided evidence that T. cruzi and T.brucei MEs display similarly high affinities towards NADP1 and are also almost equally efficient in catalyzing the production of NADPH. Nevertheless, in contrast to the cytosolic ME from T. cruzi, which is highly activated by L-aspartate (over 10-fold), the T. brucei homologue is slightly more active (50%) in the presence of this amino acid. In T. brucei, both isozymes appear to be clearly more abundant in the insect stage, although they can be immunodetected in the bloodstream forms. By contrast, in T. cruzi the expression of the mitochondrial ME seems to be clearly upregulated in amastigotes, whereas the cytosolic isoform appears to be more abundant in the insect stages of the parasite. It might be hypothesized that in those environments where glucose is very low or absent, these pathogens depend on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power.
Fil: Leroux, Alejandro Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Maugeri, Dante A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Opperdoes, Fred R.. Université Catholique de Louvain; Bélgica
Fil: Cazzulo, Juan Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Nowicki, Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
description Comparative studies showed that, like Trypanosoma cruzi, Trypanosoma brucei exhibits functional cytosolic and mitochondrial malic enzymes (MEs), which are specifically linked to NADP. Kinetic studies provided evidence that T. cruzi and T.brucei MEs display similarly high affinities towards NADP1 and are also almost equally efficient in catalyzing the production of NADPH. Nevertheless, in contrast to the cytosolic ME from T. cruzi, which is highly activated by L-aspartate (over 10-fold), the T. brucei homologue is slightly more active (50%) in the presence of this amino acid. In T. brucei, both isozymes appear to be clearly more abundant in the insect stage, although they can be immunodetected in the bloodstream forms. By contrast, in T. cruzi the expression of the mitochondrial ME seems to be clearly upregulated in amastigotes, whereas the cytosolic isoform appears to be more abundant in the insect stages of the parasite. It might be hypothesized that in those environments where glucose is very low or absent, these pathogens depend on NADP-linked dehydrogenases such as the MEs for NADPH production, as in those conditions the pentose phosphate pathway cannot serve as a source of essential reducing power.
publishDate 2011
dc.date.none.fl_str_mv 2011-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/278225
Leroux, Alejandro Ezequiel; Maugeri, Dante A.; Opperdoes, Fred R.; Cazzulo, Juan Jose; Nowicki, Cristina; Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei; Wiley Blackwell Publishing, Inc; FEMS Microbiology Letters; 314; 1; 6-2011; 25-33
0378-1097
CONICET Digital
CONICET
url http://hdl.handle.net/11336/278225
identifier_str_mv Leroux, Alejandro Ezequiel; Maugeri, Dante A.; Opperdoes, Fred R.; Cazzulo, Juan Jose; Nowicki, Cristina; Comparative studies on the biochemical properties of the malic enzymes fromTrypanosoma cruzi andTrypanosoma brucei; Wiley Blackwell Publishing, Inc; FEMS Microbiology Letters; 314; 1; 6-2011; 25-33
0378-1097
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/femsle/article-abstract/314/1/25/552119?redirectedFrom=fulltext
info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1574-6968.2010.02142.x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.952241

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