Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia

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The aim of this work was to elucidate the molecular and biochemical mechanisms that control L-ascorbic acid (AsA) content variation in Myrciaria dubia. The AsA was quantified by high-performance liquid chromatography, gene expression by real-time quantitative PCR, and enzyme activities by spectropho...

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Detalles Bibliográficos
Autores: Castro Gómez, Juan Carlos, Cobos Ruiz, Marianela, Maddox, J. Dylan, Imán Correa, Sixto Alfredo, Egoavil Reátegui, Alina del Carmen, Torres, Juan, Gutierrez, F.
Formato: artículo
Fecha de Publicación:2015
Institución:Instituto Nacional de Innovación Agraria
Repositorio:INIA-Institucional
Lenguaje:inglés
OAI Identifier:oai:null:20.500.12955/1218
Enlace del recurso:https://repositorio.inia.gob.pe/handle/20.500.12955/1218
https://doi.org/10.1007/s10535-015-0540-z
Nivel de acceso:acceso abierto
Materia:GDP-D-mannose-3′,5′-epimerase
GDP-D-mannose pyrophosphorylase
GDP-L-galactose phosphorylase
L-galactono-1-4-lactone dehydrogenase
L-galactose dehydrogenase
L-galactose-1-phosphate phosphatase
Biotecnología agrícola, Biotecnología alimentaria
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dc.title.es_PE.fl_str_mv Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia
title Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia
spellingShingle Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia
Castro Gómez, Juan Carlos
GDP-D-mannose-3′,5′-epimerase
GDP-D-mannose pyrophosphorylase
GDP-L-galactose phosphorylase
L-galactono-1-4-lactone dehydrogenase
L-galactose dehydrogenase
L-galactose-1-phosphate phosphatase
Biotecnología agrícola, Biotecnología alimentaria
title_short Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia
title_full Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia
title_fullStr Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia
title_full_unstemmed Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia
title_sort Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia
author Castro Gómez, Juan Carlos
author_facet Castro Gómez, Juan Carlos
Cobos Ruiz, Marianela
Maddox, J. Dylan
Imán Correa, Sixto Alfredo
Egoavil Reátegui, Alina del Carmen
Torres, Juan
Gutierrez, F.
author_role author
author2 Cobos Ruiz, Marianela
Maddox, J. Dylan
Imán Correa, Sixto Alfredo
Egoavil Reátegui, Alina del Carmen
Torres, Juan
Gutierrez, F.
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Castro Gómez, Juan Carlos
Cobos Ruiz, Marianela
Maddox, J. Dylan
Imán Correa, Sixto Alfredo
Egoavil Reátegui, Alina del Carmen
Torres, Juan
Gutierrez, F.
dc.subject.es_PE.fl_str_mv GDP-D-mannose-3′,5′-epimerase
GDP-D-mannose pyrophosphorylase
GDP-L-galactose phosphorylase
L-galactono-1-4-lactone dehydrogenase
L-galactose dehydrogenase
L-galactose-1-phosphate phosphatase
topic GDP-D-mannose-3′,5′-epimerase
GDP-D-mannose pyrophosphorylase
GDP-L-galactose phosphorylase
L-galactono-1-4-lactone dehydrogenase
L-galactose dehydrogenase
L-galactose-1-phosphate phosphatase
Biotecnología agrícola, Biotecnología alimentaria
dc.subject.ocde.es_PE.fl_str_mv Biotecnología agrícola, Biotecnología alimentaria
description The aim of this work was to elucidate the molecular and biochemical mechanisms that control L-ascorbic acid (AsA) content variation in Myrciaria dubia. The AsA was quantified by high-performance liquid chromatography, gene expression by real-time quantitative PCR, and enzyme activities by spectrophotometric methods from leaves and immature fruits of two genotypes (Md-60,06 and Md-02,04) with pronounced (about 2 times) differences in the AsA content. In either genotype, the fruit peel had ∼ 1.5 times more AsA than the fruit pulp and ∼ 15.0 times more than the leaf. All tissues examined demonstrated the capability for AsA biosynthesis through the D-mannose/L-galactose pathway because mRNAs of the six key genes [GDP-D-mannose pyrophosphorylase (GMP), GDP-D-mannose-3′,5′-epimerase (GME), GDP-L-galactose phosphorylase (GGP), L-galactose-1-phosphate phosphatase (GPP), L-galactose dehydrogenase (GDH), and L-galactono-1-4-lactone dehydrogenase (GLDH)] and catalytic activities of the corresponding enzymes (GMP, GDH, and GLDH) were detected. The differential expressions of genes and enzyme activities mostly correlated with the respective AsA content. Thus, the expression of several genes of the D-mannose/L-galactose pathway determined the AsA content variation in tissues of M. dubia.
publishDate 2015
dc.date.accessioned.none.fl_str_mv 2021-01-12T15:14:01Z
dc.date.available.none.fl_str_mv 2021-01-12T15:14:01Z
dc.date.issued.fl_str_mv 2015-12-01
dc.type.es_PE.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.citation.es_PE.fl_str_mv Castro, J.C., Cobos, M., Maddox, J.D. et al. Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia . Biol Plant 59, 783–787 (2015). doi: 10.1007/s10535-015-0540-z
dc.identifier.uri.none.fl_str_mv https://repositorio.inia.gob.pe/handle/20.500.12955/1218
dc.identifier.journal.es_PE.fl_str_mv BIOLOGIA PLANTARUM
dc.identifier.doi.none.fl_str_mv https://doi.org/10.1007/s10535-015-0540-z
identifier_str_mv Castro, J.C., Cobos, M., Maddox, J.D. et al. Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia . Biol Plant 59, 783–787 (2015). doi: 10.1007/s10535-015-0540-z
BIOLOGIA PLANTARUM
url https://repositorio.inia.gob.pe/handle/20.500.12955/1218
https://doi.org/10.1007/s10535-015-0540-z
dc.language.iso.es_PE.fl_str_mv eng
language eng
dc.relation.ispartof.es_PE.fl_str_mv BIOLOGIA PLANTARUM 59 (4): 783-787, 2015
dc.relation.publisherversion.es_PE.fl_str_mv https://doi.org/10.1007/s10535-015-0540-z
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eu_rights_str_mv openAccess
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dc.coverage.spatial.es_PE.fl_str_mv Perú
dc.publisher.es_PE.fl_str_mv Springer Nature
dc.publisher.country.es_PE.fl_str_mv Chequia
dc.source.es_PE.fl_str_mv Instituto Nacional de Innovación Agraria
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spelling Castro Gómez, Juan CarlosCobos Ruiz, MarianelaMaddox, J. DylanImán Correa, Sixto AlfredoEgoavil Reátegui, Alina del CarmenTorres, JuanGutierrez, F.Perú2021-01-12T15:14:01Z2021-01-12T15:14:01Z2015-12-01Castro, J.C., Cobos, M., Maddox, J.D. et al. Gene expression and enzyme activities of the D-mannose/L-galactose pathway influence L-ascorbic acid content in Myrciaria dubia . Biol Plant 59, 783–787 (2015). doi: 10.1007/s10535-015-0540-zhttps://repositorio.inia.gob.pe/handle/20.500.12955/1218BIOLOGIA PLANTARUMhttps://doi.org/10.1007/s10535-015-0540-zThe aim of this work was to elucidate the molecular and biochemical mechanisms that control L-ascorbic acid (AsA) content variation in Myrciaria dubia. The AsA was quantified by high-performance liquid chromatography, gene expression by real-time quantitative PCR, and enzyme activities by spectrophotometric methods from leaves and immature fruits of two genotypes (Md-60,06 and Md-02,04) with pronounced (about 2 times) differences in the AsA content. In either genotype, the fruit peel had ∼ 1.5 times more AsA than the fruit pulp and ∼ 15.0 times more than the leaf. All tissues examined demonstrated the capability for AsA biosynthesis through the D-mannose/L-galactose pathway because mRNAs of the six key genes [GDP-D-mannose pyrophosphorylase (GMP), GDP-D-mannose-3′,5′-epimerase (GME), GDP-L-galactose phosphorylase (GGP), L-galactose-1-phosphate phosphatase (GPP), L-galactose dehydrogenase (GDH), and L-galactono-1-4-lactone dehydrogenase (GLDH)] and catalytic activities of the corresponding enzymes (GMP, GDH, and GLDH) were detected. The differential expressions of genes and enzyme activities mostly correlated with the respective AsA content. 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