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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/13301
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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 Técnicas2025-09-29T10:29:42Zoai: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:34982025-09-29 10:29:43.043CONICET 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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1844614303936675840 |
score |
13.070432 |