Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus
- Autores
- Cereijo, Antonela Estefanía; Asención Diez, Matías Damián; Ballicora, Miguel A.; Iglesias, Alberto Alvaro
- Año de publicación
- 2018
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- ADP-glucose pyrophosphorylase from Firmicutes is encoded by two genes (glgC and glgD) leading to a heterotetrameric protein structure, unlike those in other bacterial phyla. The enzymes from two groups of Firmicutes, Bacillales and Lactobacillales, present dissimilar kinetic and regulatory properties. Nevertheless, no ADP-glucose pyrophosphorylase from Clostridiales, the third group in Firmicutes, has been characterized. For this reason, we cloned the glgC and glgD genes from Ruminococcus albus. Different quaternary forms of the enzyme (GlgC, GlgD, and GlgC/GlgD) were purified to homogeneity and their kinetic parameters were analyzed. We observed that GlgD is an inactive monomer when expressed alone but increased the catalytic efficiency of the heterotetramer (GlgC/GlgD) compared to the homotetramer (GlgC). The heterotetramer is regulated by fructose-1,6-bisphosphate, phosphoenolpyruvate, and NAD(P)H. The first characterization of the Bacillales enzyme suggested that heterotetrameric ADP-glucose pyrophosphorylases from Firmicutes were unregulated. Our results, together with data from Lactobacillales, indicate that heterotetrameric Firmicutes enzymes are mostly regulated. Thus, the ADPglucose pyrophosphorylase from Bacillales seems to have distinctive insensitivity to regulation.
Fil: Cereijo, Antonela Estefanía. 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: Asención Diez, Matías Damián. 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: Ballicora, Miguel A.. University of Chicago; Estados Unidos
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 - Materia
-
ADP-GLUCOSE PYROPHOSPHORYLASE
ALLOSTERISM
FRUCTOSE-1,6-BISPHOSPHATE
GLGC
GLGD
GLYCOGEN
GLYCOGEN METABOLISM
PHOSPHOENOLPYRUVATE
PYRUVATE
RUMINOCOCCUS ALBUS - 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:11336/86691
Ver los metadatos del registro completo
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oai_identifier_str |
oai:ri.conicet.gov.ar:11336/86691 |
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3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albusCereijo, Antonela EstefaníaAsención Diez, Matías DamiánBallicora, Miguel A.Iglesias, Alberto AlvaroADP-GLUCOSE PYROPHOSPHORYLASEALLOSTERISMFRUCTOSE-1,6-BISPHOSPHATEGLGCGLGDGLYCOGENGLYCOGEN METABOLISMPHOSPHOENOLPYRUVATEPYRUVATERUMINOCOCCUS ALBUShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1ADP-glucose pyrophosphorylase from Firmicutes is encoded by two genes (glgC and glgD) leading to a heterotetrameric protein structure, unlike those in other bacterial phyla. The enzymes from two groups of Firmicutes, Bacillales and Lactobacillales, present dissimilar kinetic and regulatory properties. Nevertheless, no ADP-glucose pyrophosphorylase from Clostridiales, the third group in Firmicutes, has been characterized. For this reason, we cloned the glgC and glgD genes from Ruminococcus albus. Different quaternary forms of the enzyme (GlgC, GlgD, and GlgC/GlgD) were purified to homogeneity and their kinetic parameters were analyzed. We observed that GlgD is an inactive monomer when expressed alone but increased the catalytic efficiency of the heterotetramer (GlgC/GlgD) compared to the homotetramer (GlgC). The heterotetramer is regulated by fructose-1,6-bisphosphate, phosphoenolpyruvate, and NAD(P)H. The first characterization of the Bacillales enzyme suggested that heterotetrameric ADP-glucose pyrophosphorylases from Firmicutes were unregulated. Our results, together with data from Lactobacillales, indicate that heterotetrameric Firmicutes enzymes are mostly regulated. Thus, the ADPglucose pyrophosphorylase from Bacillales seems to have distinctive insensitivity to regulation.Fil: Cereijo, Antonela Estefanía. 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: Asención Diez, Matías Damián. 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: Ballicora, Miguel A.. University of Chicago; Estados UnidosFil: 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; ArgentinaAmerican Society for Microbiology2018-09info: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/11336/86691Cereijo, Antonela Estefanía; Asención Diez, Matías Damián; Ballicora, Miguel A.; Iglesias, Alberto Alvaro; Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus; American Society for Microbiology; Journal of Bacteriology; 200; 17; 9-20180021-9193CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://jb.asm.org/content/200/17/e00172-18info:eu-repo/semantics/altIdentifier/doi/10.1128/JB.00172-18info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:50:21Zoai:ri.conicet.gov.ar:11336/86691instacron: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 09:50:21.59CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus |
title |
Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus |
spellingShingle |
Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus Cereijo, Antonela Estefanía ADP-GLUCOSE PYROPHOSPHORYLASE ALLOSTERISM FRUCTOSE-1,6-BISPHOSPHATE GLGC GLGD GLYCOGEN GLYCOGEN METABOLISM PHOSPHOENOLPYRUVATE PYRUVATE RUMINOCOCCUS ALBUS |
title_short |
Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus |
title_full |
Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus |
title_fullStr |
Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus |
title_full_unstemmed |
Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus |
title_sort |
Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus |
dc.creator.none.fl_str_mv |
Cereijo, Antonela Estefanía Asención Diez, Matías Damián Ballicora, Miguel A. Iglesias, Alberto Alvaro |
author |
Cereijo, Antonela Estefanía |
author_facet |
Cereijo, Antonela Estefanía Asención Diez, Matías Damián Ballicora, Miguel A. Iglesias, Alberto Alvaro |
author_role |
author |
author2 |
Asención Diez, Matías Damián Ballicora, Miguel A. Iglesias, Alberto Alvaro |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
ADP-GLUCOSE PYROPHOSPHORYLASE ALLOSTERISM FRUCTOSE-1,6-BISPHOSPHATE GLGC GLGD GLYCOGEN GLYCOGEN METABOLISM PHOSPHOENOLPYRUVATE PYRUVATE RUMINOCOCCUS ALBUS |
topic |
ADP-GLUCOSE PYROPHOSPHORYLASE ALLOSTERISM FRUCTOSE-1,6-BISPHOSPHATE GLGC GLGD GLYCOGEN GLYCOGEN METABOLISM PHOSPHOENOLPYRUVATE PYRUVATE RUMINOCOCCUS ALBUS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
ADP-glucose pyrophosphorylase from Firmicutes is encoded by two genes (glgC and glgD) leading to a heterotetrameric protein structure, unlike those in other bacterial phyla. The enzymes from two groups of Firmicutes, Bacillales and Lactobacillales, present dissimilar kinetic and regulatory properties. Nevertheless, no ADP-glucose pyrophosphorylase from Clostridiales, the third group in Firmicutes, has been characterized. For this reason, we cloned the glgC and glgD genes from Ruminococcus albus. Different quaternary forms of the enzyme (GlgC, GlgD, and GlgC/GlgD) were purified to homogeneity and their kinetic parameters were analyzed. We observed that GlgD is an inactive monomer when expressed alone but increased the catalytic efficiency of the heterotetramer (GlgC/GlgD) compared to the homotetramer (GlgC). The heterotetramer is regulated by fructose-1,6-bisphosphate, phosphoenolpyruvate, and NAD(P)H. The first characterization of the Bacillales enzyme suggested that heterotetrameric ADP-glucose pyrophosphorylases from Firmicutes were unregulated. Our results, together with data from Lactobacillales, indicate that heterotetrameric Firmicutes enzymes are mostly regulated. Thus, the ADPglucose pyrophosphorylase from Bacillales seems to have distinctive insensitivity to regulation. Fil: Cereijo, Antonela Estefanía. 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: Asención Diez, Matías Damián. 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: Ballicora, Miguel A.. University of Chicago; Estados Unidos 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 |
description |
ADP-glucose pyrophosphorylase from Firmicutes is encoded by two genes (glgC and glgD) leading to a heterotetrameric protein structure, unlike those in other bacterial phyla. The enzymes from two groups of Firmicutes, Bacillales and Lactobacillales, present dissimilar kinetic and regulatory properties. Nevertheless, no ADP-glucose pyrophosphorylase from Clostridiales, the third group in Firmicutes, has been characterized. For this reason, we cloned the glgC and glgD genes from Ruminococcus albus. Different quaternary forms of the enzyme (GlgC, GlgD, and GlgC/GlgD) were purified to homogeneity and their kinetic parameters were analyzed. We observed that GlgD is an inactive monomer when expressed alone but increased the catalytic efficiency of the heterotetramer (GlgC/GlgD) compared to the homotetramer (GlgC). The heterotetramer is regulated by fructose-1,6-bisphosphate, phosphoenolpyruvate, and NAD(P)H. The first characterization of the Bacillales enzyme suggested that heterotetrameric ADP-glucose pyrophosphorylases from Firmicutes were unregulated. Our results, together with data from Lactobacillales, indicate that heterotetrameric Firmicutes enzymes are mostly regulated. Thus, the ADPglucose pyrophosphorylase from Bacillales seems to have distinctive insensitivity to regulation. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-09 |
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/11336/86691 Cereijo, Antonela Estefanía; Asención Diez, Matías Damián; Ballicora, Miguel A.; Iglesias, Alberto Alvaro; Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus; American Society for Microbiology; Journal of Bacteriology; 200; 17; 9-2018 0021-9193 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/86691 |
identifier_str_mv |
Cereijo, Antonela Estefanía; Asención Diez, Matías Damián; Ballicora, Miguel A.; Iglesias, Alberto Alvaro; Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus; American Society for Microbiology; Journal of Bacteriology; 200; 17; 9-2018 0021-9193 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://jb.asm.org/content/200/17/e00172-18 info:eu-repo/semantics/altIdentifier/doi/10.1128/JB.00172-18 |
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 |
American Society for Microbiology |
publisher.none.fl_str_mv |
American Society for Microbiology |
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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1844613552647700480 |
score |
13.070432 |