Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h

Autores
Hartman, Matias Daniel; Figueroa, Carlos Maria; Piattoni, Claudia Vanesa; Iglesias, Alberto Alvaro
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Glucitol (Gol) is a major photosynthetic product in plants from the Rosaceae family. Herein we report the molecular cloning, heterologous expression, and characterization of Gol dehydrogenase (GolDHase, EC 1.1.1.14) from peach (Prunus persica) fruits. The recombinant enzyme showed kinetic parameters similar to those reported for orthologous enzymes purified from apple and pear fruits. The activity of recombinant GolDHase was strongly inhibited by Cu2+ and Hg2+, suggesting that it might have cysteine residues critical for functionality. Oxidizing compounds (like diamide, hydrogen peroxide, and oxidized glutathione) inactivated the enzyme, whereas its activity was restored after incubation with reduced glutathione and thioredoxin from Escherichia coli. Recombinant thioredoxin h from peach fruits also recovered the activity of oxidized GolDHase. Our results suggest that peach fruit GolDHase could be redox regulated in vivo and this would be of relevance to determine carbon assimilation and partitioning in plants accumulating sugar alcohols.
Fil: Hartman, Matias Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Figueroa, Carlos Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Piattoni, Claudia Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Materia
Glucitol Dehydrogenase
Glucitol Metabolism
Peach
Prunus Persica
Redox Regulation
Thioredoxin
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/13301
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin hHartman, Matias DanielFigueroa, Carlos MariaPiattoni, Claudia VanesaIglesias, Alberto AlvaroGlucitol DehydrogenaseGlucitol MetabolismPeachPrunus PersicaRedox RegulationThioredoxinhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Glucitol (Gol) is a major photosynthetic product in plants from the Rosaceae family. Herein we report the molecular cloning, heterologous expression, and characterization of Gol dehydrogenase (GolDHase, EC 1.1.1.14) from peach (Prunus persica) fruits. The recombinant enzyme showed kinetic parameters similar to those reported for orthologous enzymes purified from apple and pear fruits. The activity of recombinant GolDHase was strongly inhibited by Cu2+ and Hg2+, suggesting that it might have cysteine residues critical for functionality. Oxidizing compounds (like diamide, hydrogen peroxide, and oxidized glutathione) inactivated the enzyme, whereas its activity was restored after incubation with reduced glutathione and thioredoxin from Escherichia coli. Recombinant thioredoxin h from peach fruits also recovered the activity of oxidized GolDHase. Our results suggest that peach fruit GolDHase could be redox regulated in vivo and this would be of relevance to determine carbon assimilation and partitioning in plants accumulating sugar alcohols.Fil: Hartman, Matias Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaFil: Figueroa, Carlos Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaFil: Piattoni, Claudia Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaFil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaOxford University Press2014-04info: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/11336/13301Hartman, Matias Daniel; Figueroa, Carlos Maria; Piattoni, Claudia Vanesa; Iglesias, Alberto Alvaro; Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h; Oxford University Press; Plant And Cell Physiology; 55; 6; 4-2014; 1157-11680032-0781enginfo:eu-repo/semantics/altIdentifier/url/http://pcp.oxfordjournals.org/content/early/2014/04/18/pcp.pcu055.longinfo:eu-repo/semantics/altIdentifier/doi/10.1093/pcp/pcu055info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:26:53Zoai:ri.conicet.gov.ar:11336/13301instacron: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:34982025-10-15 15:26:53.59CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h
title Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h
spellingShingle Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h
Hartman, Matias Daniel
Glucitol Dehydrogenase
Glucitol Metabolism
Peach
Prunus Persica
Redox Regulation
Thioredoxin
title_short Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h
title_full Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h
title_fullStr Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h
title_full_unstemmed Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h
title_sort Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h
dc.creator.none.fl_str_mv Hartman, Matias Daniel
Figueroa, Carlos Maria
Piattoni, Claudia Vanesa
Iglesias, Alberto Alvaro
author Hartman, Matias Daniel
author_facet Hartman, Matias Daniel
Figueroa, Carlos Maria
Piattoni, Claudia Vanesa
Iglesias, Alberto Alvaro
author_role author
author2 Figueroa, Carlos Maria
Piattoni, Claudia Vanesa
Iglesias, Alberto Alvaro
author2_role author
author
author
dc.subject.none.fl_str_mv Glucitol Dehydrogenase
Glucitol Metabolism
Peach
Prunus Persica
Redox Regulation
Thioredoxin
topic Glucitol Dehydrogenase
Glucitol Metabolism
Peach
Prunus Persica
Redox Regulation
Thioredoxin
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Glucitol (Gol) is a major photosynthetic product in plants from the Rosaceae family. Herein we report the molecular cloning, heterologous expression, and characterization of Gol dehydrogenase (GolDHase, EC 1.1.1.14) from peach (Prunus persica) fruits. The recombinant enzyme showed kinetic parameters similar to those reported for orthologous enzymes purified from apple and pear fruits. The activity of recombinant GolDHase was strongly inhibited by Cu2+ and Hg2+, suggesting that it might have cysteine residues critical for functionality. Oxidizing compounds (like diamide, hydrogen peroxide, and oxidized glutathione) inactivated the enzyme, whereas its activity was restored after incubation with reduced glutathione and thioredoxin from Escherichia coli. Recombinant thioredoxin h from peach fruits also recovered the activity of oxidized GolDHase. Our results suggest that peach fruit GolDHase could be redox regulated in vivo and this would be of relevance to determine carbon assimilation and partitioning in plants accumulating sugar alcohols.
Fil: Hartman, Matias Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Figueroa, Carlos Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Piattoni, Claudia Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina
description Glucitol (Gol) is a major photosynthetic product in plants from the Rosaceae family. Herein we report the molecular cloning, heterologous expression, and characterization of Gol dehydrogenase (GolDHase, EC 1.1.1.14) from peach (Prunus persica) fruits. The recombinant enzyme showed kinetic parameters similar to those reported for orthologous enzymes purified from apple and pear fruits. The activity of recombinant GolDHase was strongly inhibited by Cu2+ and Hg2+, suggesting that it might have cysteine residues critical for functionality. Oxidizing compounds (like diamide, hydrogen peroxide, and oxidized glutathione) inactivated the enzyme, whereas its activity was restored after incubation with reduced glutathione and thioredoxin from Escherichia coli. Recombinant thioredoxin h from peach fruits also recovered the activity of oxidized GolDHase. Our results suggest that peach fruit GolDHase could be redox regulated in vivo and this would be of relevance to determine carbon assimilation and partitioning in plants accumulating sugar alcohols.
publishDate 2014
dc.date.none.fl_str_mv 2014-04
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/11336/13301
Hartman, Matias Daniel; Figueroa, Carlos Maria; Piattoni, Claudia Vanesa; Iglesias, Alberto Alvaro; Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h; Oxford University Press; Plant And Cell Physiology; 55; 6; 4-2014; 1157-1168
0032-0781
url http://hdl.handle.net/11336/13301
identifier_str_mv Hartman, Matias Daniel; Figueroa, Carlos Maria; Piattoni, Claudia Vanesa; Iglesias, Alberto Alvaro; Glucitol Dehydrogenase from Peach (Prunus persica) Fruits is Regulated by Thioredoxin h; Oxford University Press; Plant And Cell Physiology; 55; 6; 4-2014; 1157-1168
0032-0781
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://pcp.oxfordjournals.org/content/early/2014/04/18/pcp.pcu055.long
info:eu-repo/semantics/altIdentifier/doi/10.1093/pcp/pcu055
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
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 13.22299

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