Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate

Autores
Tronconi, Marcos Ariel; Wheeler, Mariel Gerrard; Martinatto, Andrea; Zubimendi, Juan Pablo; Andreo, Carlos Santiago; Drincovich, Maria Fabiana
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Plant mitochondria can use L-malate and fumarate, which accumulate in large levels, as respiratory substrates. In part, this property is due to the presence of NAD-dependent malic enzymes (NAD-ME) with particular biochemical characteristics. Arabidopsis NAD-ME1 exhibits a non-hyperbolic behavior for the substrate L-malate and its activity is strongly stimulated by fumarate. Here, the possible structural connection between these properties was explored through mutagenesis, kinetics and fluorescence studies. The results indicate that NAD-ME1 presents a regulatory site for L-malate that can also bind fumarate. L-malate binding to this site elicits a sigmoidal and low substrate-affinity response. Instead, fumarate binding turns NAD-ME1 into a hyperbolic and high substrate affinity enzyme. This effect was also observed when the allosteric site was either removed or altered. Hence, fumarate is not really an activator but suppresses the inhibitory effect of L-malate. In addition, residues Arg50, Arg80 and Arg84 showed different participationroless in organic acid binding. These residues form a triad, which is the basis of the homo and heterotrophic effects that characterize NAD-ME1. The binding of L-malate and fumarate at the same allosteric site is here reported for the first time for a malic enzyme and clearly indicates an important role for of NAD-ME1 in the processes that control the flow of C4 organic acids in Arabidopsis mitochondrial metabolism
Fil: Tronconi, Marcos Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Wheeler, Mariel Gerrard. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Martinatto, Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Zubimendi, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Drincovich, Maria Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Materia
Malic Enzyme
Regulation
Allosteric
Arabidopsis
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/7844
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/7844
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarateTronconi, Marcos ArielWheeler, Mariel GerrardMartinatto, AndreaZubimendi, Juan PabloAndreo, Carlos SantiagoDrincovich, Maria FabianaMalic EnzymeRegulationAllostericArabidopsishttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Plant mitochondria can use L-malate and fumarate, which accumulate in large levels, as respiratory substrates. In part, this property is due to the presence of NAD-dependent malic enzymes (NAD-ME) with particular biochemical characteristics. Arabidopsis NAD-ME1 exhibits a non-hyperbolic behavior for the substrate L-malate and its activity is strongly stimulated by fumarate. Here, the possible structural connection between these properties was explored through mutagenesis, kinetics and fluorescence studies. The results indicate that NAD-ME1 presents a regulatory site for L-malate that can also bind fumarate. L-malate binding to this site elicits a sigmoidal and low substrate-affinity response. Instead, fumarate binding turns NAD-ME1 into a hyperbolic and high substrate affinity enzyme. This effect was also observed when the allosteric site was either removed or altered. Hence, fumarate is not really an activator but suppresses the inhibitory effect of L-malate. In addition, residues Arg50, Arg80 and Arg84 showed different participationroless in organic acid binding. These residues form a triad, which is the basis of the homo and heterotrophic effects that characterize NAD-ME1. The binding of L-malate and fumarate at the same allosteric site is here reported for the first time for a malic enzyme and clearly indicates an important role for of NAD-ME1 in the processes that control the flow of C4 organic acids in Arabidopsis mitochondrial metabolismFil: Tronconi, Marcos Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaFil: Wheeler, Mariel Gerrard. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaFil: Martinatto, Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaFil: Zubimendi, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaFil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaFil: Drincovich, Maria Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaElsevier2015-02info: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/11336/7844Tronconi, Marcos Ariel; Wheeler, Mariel Gerrard; Martinatto, Andrea; Zubimendi, Juan Pablo; Andreo, Carlos Santiago; et al.; Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate; Elsevier; Phytochemistry; 111; 2-2015; 37-470031-9422enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0031942214004920info:eu-repo/semantics/altIdentifier/doi/10.1016/j.phytochem.2014.11.009info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:24:32Zoai:ri.conicet.gov.ar:11336/7844instacron: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:34982025-09-29 10:24:32.752CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate
title Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate
spellingShingle Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate
Tronconi, Marcos Ariel
Malic Enzyme
Regulation
Allosteric
Arabidopsis
title_short Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate
title_full Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate
title_fullStr Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate
title_full_unstemmed Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate
title_sort Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate
dc.creator.none.fl_str_mv Tronconi, Marcos Ariel
Wheeler, Mariel Gerrard
Martinatto, Andrea
Zubimendi, Juan Pablo
Andreo, Carlos Santiago
Drincovich, Maria Fabiana
author Tronconi, Marcos Ariel
author_facet Tronconi, Marcos Ariel
Wheeler, Mariel Gerrard
Martinatto, Andrea
Zubimendi, Juan Pablo
Andreo, Carlos Santiago
Drincovich, Maria Fabiana
author_role author
author2 Wheeler, Mariel Gerrard
Martinatto, Andrea
Zubimendi, Juan Pablo
Andreo, Carlos Santiago
Drincovich, Maria Fabiana
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Malic Enzyme
Regulation
Allosteric
Arabidopsis
topic Malic Enzyme
Regulation
Allosteric
Arabidopsis
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Plant mitochondria can use L-malate and fumarate, which accumulate in large levels, as respiratory substrates. In part, this property is due to the presence of NAD-dependent malic enzymes (NAD-ME) with particular biochemical characteristics. Arabidopsis NAD-ME1 exhibits a non-hyperbolic behavior for the substrate L-malate and its activity is strongly stimulated by fumarate. Here, the possible structural connection between these properties was explored through mutagenesis, kinetics and fluorescence studies. The results indicate that NAD-ME1 presents a regulatory site for L-malate that can also bind fumarate. L-malate binding to this site elicits a sigmoidal and low substrate-affinity response. Instead, fumarate binding turns NAD-ME1 into a hyperbolic and high substrate affinity enzyme. This effect was also observed when the allosteric site was either removed or altered. Hence, fumarate is not really an activator but suppresses the inhibitory effect of L-malate. In addition, residues Arg50, Arg80 and Arg84 showed different participationroless in organic acid binding. These residues form a triad, which is the basis of the homo and heterotrophic effects that characterize NAD-ME1. The binding of L-malate and fumarate at the same allosteric site is here reported for the first time for a malic enzyme and clearly indicates an important role for of NAD-ME1 in the processes that control the flow of C4 organic acids in Arabidopsis mitochondrial metabolism
Fil: Tronconi, Marcos Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Wheeler, Mariel Gerrard. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Martinatto, Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Zubimendi, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Drincovich, Maria Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
description Plant mitochondria can use L-malate and fumarate, which accumulate in large levels, as respiratory substrates. In part, this property is due to the presence of NAD-dependent malic enzymes (NAD-ME) with particular biochemical characteristics. Arabidopsis NAD-ME1 exhibits a non-hyperbolic behavior for the substrate L-malate and its activity is strongly stimulated by fumarate. Here, the possible structural connection between these properties was explored through mutagenesis, kinetics and fluorescence studies. The results indicate that NAD-ME1 presents a regulatory site for L-malate that can also bind fumarate. L-malate binding to this site elicits a sigmoidal and low substrate-affinity response. Instead, fumarate binding turns NAD-ME1 into a hyperbolic and high substrate affinity enzyme. This effect was also observed when the allosteric site was either removed or altered. Hence, fumarate is not really an activator but suppresses the inhibitory effect of L-malate. In addition, residues Arg50, Arg80 and Arg84 showed different participationroless in organic acid binding. These residues form a triad, which is the basis of the homo and heterotrophic effects that characterize NAD-ME1. The binding of L-malate and fumarate at the same allosteric site is here reported for the first time for a malic enzyme and clearly indicates an important role for of NAD-ME1 in the processes that control the flow of C4 organic acids in Arabidopsis mitochondrial metabolism
publishDate 2015
dc.date.none.fl_str_mv 2015-02
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/11336/7844
Tronconi, Marcos Ariel; Wheeler, Mariel Gerrard; Martinatto, Andrea; Zubimendi, Juan Pablo; Andreo, Carlos Santiago; et al.; Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate; Elsevier; Phytochemistry; 111; 2-2015; 37-47
0031-9422
url http://hdl.handle.net/11336/7844
identifier_str_mv Tronconi, Marcos Ariel; Wheeler, Mariel Gerrard; Martinatto, Andrea; Zubimendi, Juan Pablo; Andreo, Carlos Santiago; et al.; Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate; Elsevier; Phytochemistry; 111; 2-2015; 37-47
0031-9422
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0031942214004920
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.phytochem.2014.11.009
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 13.070432

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