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dc.contributor.author
Tronconi, Marcos Ariel
dc.contributor.author
Wheeler, Mariel Gerrard
dc.contributor.author
Martinatto, Andrea
dc.contributor.author
Zubimendi, Juan Pablo
dc.contributor.author
Andreo, Carlos Santiago
dc.contributor.author
Drincovich, Maria Fabiana
dc.date.available
2016-10-27T21:21:09Z
dc.date.issued
2015-02
dc.identifier.citation
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
dc.identifier.issn
0031-9422
dc.identifier.uri
http://hdl.handle.net/11336/7844
dc.description.abstract
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
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Malic Enzyme
dc.subject
Regulation
dc.subject
Allosteric
dc.subject
Arabidopsis
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-03-14T12:49:51Z
dc.journal.volume
111
dc.journal.pagination
37-47
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Tronconi, Marcos Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
dc.description.fil
Fil: Wheeler, Mariel Gerrard. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
dc.description.fil
Fil: Martinatto, Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
dc.description.fil
Fil: Zubimendi, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
dc.description.fil
Fil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
dc.description.fil
Fil: Drincovich, Maria Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
dc.journal.title
Phytochemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0031942214004920
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.phytochem.2014.11.009


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