On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves

Autores
Iglesias, Alberto Alvaro; Vicario, Lionel; Gomez Casati, Diego Fabian; Sesma, Juliana; Gomez Casati, Maria Eugenia; Bustos, Diego Martin; Podesta, Florencio Esteban
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Structural analogues of D-glyceraldehyde-3-phosphate (D-Ga3P) and NADP+ were studied as potential substrates and inhibitors of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.9; GAPN) from Apium graveolens leaves. Four analogues of NADP+: nicotinamide-hypoxanthine dinucleotide phosphate (NHDP+); 3-acetylpyridine-adenine dinucleotide phosphate (APADP+); 1,N6-etheno-nicotinamide dinucleotide phosphate (oNADP+); and b-nicotinamide adenine dinucleotide 2´:3´-cyclic monophosphate (2?3?NADP+c) were alternative enzyme substrates, with a 2-fold variation in Vmax and 2+/11-fold differences in Km compared to NADP+. These compounds were also able to affect the hysteretic behavior of celery GAPN, in a similar way as the substrate NADP+. The analogues to the nicotinamide moiety: thionicotinamide and 3-aminopyridine, behaved as competitive inhibitors, exhibiting a high-affinity binding to the enzyme. All the analogues of D-Ga3P that were analyzed behaved as competitive inhibitors, except for the L-isomer of the substrate which at relatively high concentrations exhibited a non-competitive effect. Results showed the importance of: (i) the chemical group at carbon-1 of Ga3P; (ii) the presence of a phosphate ester at carbon-3, and (iii) the stereochemical configuration at carbon-2. The particular behavior of L-Ga3P is analyzed by differences in tridimensional structure between bacteria and plant GAPNs.
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Vicario, Lionel. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Sesma, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Gomez Casati, Maria Eugenia. 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
Fil: Bustos, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Podesta, Florencio Esteban. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Materia
Non-phosphorylating
Glyceraldehyde-3-phosphate dehydrogenase
GAPN
Celery
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:11336/85684
Acceder
id CONICETDig_71983c552388a4872bc885e0542567ba
oai_identifier_str oai:ri.conicet.gov.ar:11336/85684
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leavesIglesias, Alberto AlvaroVicario, LionelGomez Casati, Diego FabianSesma, JulianaGomez Casati, Maria EugeniaBustos, Diego MartinPodesta, Florencio EstebanNon-phosphorylatingGlyceraldehyde-3-phosphate dehydrogenaseGAPNCeleryhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Structural analogues of D-glyceraldehyde-3-phosphate (D-Ga3P) and NADP+ were studied as potential substrates and inhibitors of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.9; GAPN) from Apium graveolens leaves. Four analogues of NADP+: nicotinamide-hypoxanthine dinucleotide phosphate (NHDP+); 3-acetylpyridine-adenine dinucleotide phosphate (APADP+); 1,N6-etheno-nicotinamide dinucleotide phosphate (oNADP+); and b-nicotinamide adenine dinucleotide 2´:3´-cyclic monophosphate (2?3?NADP+c) were alternative enzyme substrates, with a 2-fold variation in Vmax and 2+/11-fold differences in Km compared to NADP+. These compounds were also able to affect the hysteretic behavior of celery GAPN, in a similar way as the substrate NADP+. The analogues to the nicotinamide moiety: thionicotinamide and 3-aminopyridine, behaved as competitive inhibitors, exhibiting a high-affinity binding to the enzyme. All the analogues of D-Ga3P that were analyzed behaved as competitive inhibitors, except for the L-isomer of the substrate which at relatively high concentrations exhibited a non-competitive effect. Results showed the importance of: (i) the chemical group at carbon-1 of Ga3P; (ii) the presence of a phosphate ester at carbon-3, and (iii) the stereochemical configuration at carbon-2. The particular behavior of L-Ga3P is analyzed by differences in tridimensional structure between bacteria and plant GAPNs.Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Vicario, Lionel. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaFil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Sesma, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Gomez Casati, Maria Eugenia. 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; ArgentinaFil: Bustos, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Podesta, Florencio Esteban. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaElsevier Ireland2002-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/85684Iglesias, Alberto Alvaro; Vicario, Lionel; Gomez Casati, Diego Fabian; Sesma, Juliana; Gomez Casati, Maria Eugenia; et al.; On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves; Elsevier Ireland; Plant Science; 162; 1-2002; 689-6960168-9452CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://ac.els-cdn.com/S0168945202000158/1-s2.0-S0168945202000158-main.pdf?_tid=86c0da4a-6e95-11e3-86e0-00000aacb360&acdnat=1388107604_d41dd1d981f88a33c2c4d29d09883a51info:eu-repo/semantics/altIdentifier/doi/10.1016/S0168-9452(02)00015-8info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:41:00Zoai:ri.conicet.gov.ar:11336/85684instacron: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 14:41:00.568CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves
title On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves
spellingShingle On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves
Iglesias, Alberto Alvaro
Non-phosphorylating
Glyceraldehyde-3-phosphate dehydrogenase
GAPN
Celery
title_short On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves
title_full On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves
title_fullStr On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves
title_full_unstemmed On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves
title_sort On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves
dc.creator.none.fl_str_mv Iglesias, Alberto Alvaro
Vicario, Lionel
Gomez Casati, Diego Fabian
Sesma, Juliana
Gomez Casati, Maria Eugenia
Bustos, Diego Martin
Podesta, Florencio Esteban
author Iglesias, Alberto Alvaro
author_facet Iglesias, Alberto Alvaro
Vicario, Lionel
Gomez Casati, Diego Fabian
Sesma, Juliana
Gomez Casati, Maria Eugenia
Bustos, Diego Martin
Podesta, Florencio Esteban
author_role author
author2 Vicario, Lionel
Gomez Casati, Diego Fabian
Sesma, Juliana
Gomez Casati, Maria Eugenia
Bustos, Diego Martin
Podesta, Florencio Esteban
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Non-phosphorylating
Glyceraldehyde-3-phosphate dehydrogenase
GAPN
Celery
topic Non-phosphorylating
Glyceraldehyde-3-phosphate dehydrogenase
GAPN
Celery
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Structural analogues of D-glyceraldehyde-3-phosphate (D-Ga3P) and NADP+ were studied as potential substrates and inhibitors of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.9; GAPN) from Apium graveolens leaves. Four analogues of NADP+: nicotinamide-hypoxanthine dinucleotide phosphate (NHDP+); 3-acetylpyridine-adenine dinucleotide phosphate (APADP+); 1,N6-etheno-nicotinamide dinucleotide phosphate (oNADP+); and b-nicotinamide adenine dinucleotide 2´:3´-cyclic monophosphate (2?3?NADP+c) were alternative enzyme substrates, with a 2-fold variation in Vmax and 2+/11-fold differences in Km compared to NADP+. These compounds were also able to affect the hysteretic behavior of celery GAPN, in a similar way as the substrate NADP+. The analogues to the nicotinamide moiety: thionicotinamide and 3-aminopyridine, behaved as competitive inhibitors, exhibiting a high-affinity binding to the enzyme. All the analogues of D-Ga3P that were analyzed behaved as competitive inhibitors, except for the L-isomer of the substrate which at relatively high concentrations exhibited a non-competitive effect. Results showed the importance of: (i) the chemical group at carbon-1 of Ga3P; (ii) the presence of a phosphate ester at carbon-3, and (iii) the stereochemical configuration at carbon-2. The particular behavior of L-Ga3P is analyzed by differences in tridimensional structure between bacteria and plant GAPNs.
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Vicario, Lionel. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Sesma, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Gomez Casati, Maria Eugenia. 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
Fil: Bustos, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Podesta, Florencio Esteban. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
description Structural analogues of D-glyceraldehyde-3-phosphate (D-Ga3P) and NADP+ were studied as potential substrates and inhibitors of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.9; GAPN) from Apium graveolens leaves. Four analogues of NADP+: nicotinamide-hypoxanthine dinucleotide phosphate (NHDP+); 3-acetylpyridine-adenine dinucleotide phosphate (APADP+); 1,N6-etheno-nicotinamide dinucleotide phosphate (oNADP+); and b-nicotinamide adenine dinucleotide 2´:3´-cyclic monophosphate (2?3?NADP+c) were alternative enzyme substrates, with a 2-fold variation in Vmax and 2+/11-fold differences in Km compared to NADP+. These compounds were also able to affect the hysteretic behavior of celery GAPN, in a similar way as the substrate NADP+. The analogues to the nicotinamide moiety: thionicotinamide and 3-aminopyridine, behaved as competitive inhibitors, exhibiting a high-affinity binding to the enzyme. All the analogues of D-Ga3P that were analyzed behaved as competitive inhibitors, except for the L-isomer of the substrate which at relatively high concentrations exhibited a non-competitive effect. Results showed the importance of: (i) the chemical group at carbon-1 of Ga3P; (ii) the presence of a phosphate ester at carbon-3, and (iii) the stereochemical configuration at carbon-2. The particular behavior of L-Ga3P is analyzed by differences in tridimensional structure between bacteria and plant GAPNs.
publishDate 2002
dc.date.none.fl_str_mv 2002-01
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/11336/85684
Iglesias, Alberto Alvaro; Vicario, Lionel; Gomez Casati, Diego Fabian; Sesma, Juliana; Gomez Casati, Maria Eugenia; et al.; On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves; Elsevier Ireland; Plant Science; 162; 1-2002; 689-696
0168-9452
CONICET Digital
CONICET
url http://hdl.handle.net/11336/85684
identifier_str_mv Iglesias, Alberto Alvaro; Vicario, Lionel; Gomez Casati, Diego Fabian; Sesma, Juliana; Gomez Casati, Maria Eugenia; et al.; On the interaction of sustrate analogues with non-phosphorylating glyceraldehydes-3-phosphate dehydrogenase from celery leaves; Elsevier Ireland; Plant Science; 162; 1-2002; 689-696
0168-9452
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://ac.els-cdn.com/S0168945202000158/1-s2.0-S0168945202000158-main.pdf?_tid=86c0da4a-6e95-11e3-86e0-00000aacb360&acdnat=1388107604_d41dd1d981f88a33c2c4d29d09883a51
info:eu-repo/semantics/altIdentifier/doi/10.1016/S0168-9452(02)00015-8
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
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Ireland
publisher.none.fl_str_mv Elsevier Ireland
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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