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dc.contributor.author
Gerrard Wheeler, Mariel Claudia
dc.contributor.author
Arias, Cintia Lucia
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da Fonseca Rezende e Mello, Juliana
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Cirauqui Diaz, Nuria
dc.contributor.author
Rangel Rodrigues, Carlos
dc.contributor.author
Drincovich, María Fabiana
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Mendonça Teles de Souza, Alessandra
dc.contributor.author
Alvarez, Clarisa Ester
dc.date.available
2023-01-09T10:52:57Z
dc.date.issued
2021-09
dc.identifier.citation
Gerrard Wheeler, Mariel Claudia; Arias, Cintia Lucia; da Fonseca Rezende e Mello, Juliana; Cirauqui Diaz, Nuria; Rangel Rodrigues, Carlos; et al.; Structural insights into the allosteric site of Arabidopsis NADP-malic enzyme 2: role of the second sphere residues in the regulatory signal transmission; Springer; Plant Molecular Biology; 107; 1-2; 9-2021; 37-48
dc.identifier.issn
0167-4412
dc.identifier.uri
http://hdl.handle.net/11336/183843
dc.description.abstract
t Structure–function studies contribute to deciphering how small modifcations in the primary structure could introduce desirable characteristics into enzymes without afecting its overall functioning. Malic enzymes (ME) are ubiquitous and responsible for a wide variety of functions. The availability of a high number of ME crystal structures from diferent species facilitates comparisons between sequence and structure. Specifcally, the structural determinants necessary for fumarate allosteric regulation of ME has been of particular interest. NADP-ME2 from Arabidopsis thaliana exhibits a distinctive and complex regulation by fumarate, acting as an activator or an inhibitor according to substrate and efector concentrations. However, the 3D structure for this enzyme is not yet reported. In this work, we characterized the NADP-ME2 allosteric site by structural modeling, molecular docking, normal mode analysis and mutagenesis. The regulatory site model and its docking analysis suggested that other C4 acids including malate, NADP-ME2 substrate, could also ft into fumarate’s pocket. Besides, a non-conserved cluster of hydrophobic residues in the second sphere of the allosteric site was identifed. The substitution of one of those residues, L62, by a less fexible residue as tryptophan, resulted in a complete loss of fumarate activation and a reduction of substrate afnities for the active site. In addition, normal mode analysis indicated that conformational changes leading to the activation could originate in the region surrounding L62, extending through the allosteric site till the active site. Finally, the results in this work contribute to the understanding of structural determinants necessary for allosteric regulation providing new insights for enzyme optimization.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
FUMARATE REGULATION
dc.subject
MALIC ENZYME
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STRUCTURE–FUNCTION
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Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Structural insights into the allosteric site of Arabidopsis NADP-malic enzyme 2: role of the second sphere residues in the regulatory signal transmission
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2022-09-05T16:58:45Z
dc.journal.volume
107
dc.journal.number
1-2
dc.journal.pagination
37-48
dc.journal.pais
Alemania
dc.description.fil
Fil: Gerrard Wheeler, Mariel Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
dc.description.fil
Fil: Arias, Cintia Lucia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
dc.description.fil
Fil: da Fonseca Rezende e Mello, Juliana. Universidade Federal do Rio de Janeiro; Brasil
dc.description.fil
Fil: Cirauqui Diaz, Nuria. Universidade Federal do Rio de Janeiro; Brasil
dc.description.fil
Fil: Rangel Rodrigues, Carlos. Universidad Nacional de Rosario; Argentina
dc.description.fil
Fil: Drincovich, María Fabiana. Universidade Federal do Rio de Janeiro; Brasil
dc.description.fil
Fil: Mendonça Teles de Souza, Alessandra. Universidad Nacional de Rosario; Argentina
dc.description.fil
Fil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
dc.journal.title
Plant Molecular Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s11103-021-01176-2
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