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Artículo

The complex allosteric and redox regulation of the fumarate hydratase and malate dehydratase reactions of Arabidopsis thaliana Fumarase 1 and 2 gives clues for understanding the massive accumulation of fumarate

Zubimendi, Juan PabloIcon ; Martinatto, Andrea KarinaIcon ; Valacco, Maria PiaIcon ; Moreno, Silvia MargaritaIcon ; Andreo, Carlos SantiagoIcon ; Drincovich, Maria FabianaIcon ; Tronconi, Marcos ArielIcon
Fecha de publicación: 06/2018
Editorial: Wiley Blackwell Publishing, Inc
Revista: Febs Journal
ISSN: 1742-464X
e-ISSN: 1742-4658
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Bioquímica y Biología Molecular

Resumen

Arabidopsis thaliana possesses two fumarase genes (FUM), AtFUM1 (At2g47510) encoding for the mitochondrial Krebs cycle-associated enzyme and AtFUM2 (At5g50950) for the cytosolic isoform required for fumarate massive accumulation. Here, the comprehensive biochemical studies of AtFUM1 and AtFUM2 shows that they are active enzymes with similar kinetic parameters but differential regulation. For both enzymes, fumarate hydratase (FH) activity is favored over the malate dehydratase (MD) activity; however, MD is the most regulated activity with several allosteric activators. Oxalacetate, glutamine, and/or asparagine are modulators causing the MD reaction to become preferred over the FH reaction. Activity profiles as a function of pH suggest a suboptimal FUM activity in Arabidopsis cells; moreover, the direction of the FUM reaction is sensitive to pH changes. Under mild oxidation conditions, AtFUMs form high mass molecular aggregates, which present both FUM activities decreased to a different extent. The biochemical properties of oxidized AtFUMs (oxAtFUMs) were completely reversed by NADPH-supplied Arabidopsis leaf extracts, suggesting that the AtFUMs redox regulation can be accomplished in vivo. Mass spectrometry analyses indicate the presence of an active site-associated intermolecular disulfide bridge in oxAtFUMs. Finally, a phylogenetic approach points out that other plant species may also possess cytosolic FUM2 enzymes mainly encoded by paralogous genes, indicating that the evolutionary history of this trait has been drawn through a process of parallel evolution. Overall, according to our results, a multilevel regulatory pattern of FUM activities emerges, supporting the role of this enzyme as a carbon flow monitoring point through the organic acid metabolism in plants.
Palabras clave: ALLOSTERIC AND REDOX REGULATION , ARABIDOPSIS , ENZYME KINETICS , FUMARASE , PARALOGOUS GENES
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)
Identificadores
URI: http://hdl.handle.net/11336/87839
URL: https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.14483
DOI: http://dx.doi.org/10.1111/febs.14483
Colecciones
Articulos(CCT - ROSARIO)
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - ROSARIO
Articulos(CEFOBI)
Articulos de CENTRO DE EST.FOTOSINTETICOS Y BIOQUIMICOS (I)
Articulos(IQUIBICEN)
Articulos de INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CS. EXACTAS Y NATURALES
Citación
Zubimendi, Juan Pablo; Martinatto, Andrea Karina; Valacco, Maria Pia; Moreno, Silvia Margarita; Andreo, Carlos Santiago; et al.; The complex allosteric and redox regulation of the fumarate hydratase and malate dehydratase reactions of Arabidopsis thaliana Fumarase 1 and 2 gives clues for understanding the massive accumulation of fumarate; Wiley Blackwell Publishing, Inc; Febs Journal; 285; 12; 6-2018; 2205-2224
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