Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches
- Autores
- Fox, Ana Romina; Soto, Gabriela Cynthia; Mozzicafreddo, Matteo; García, Araceli Nora; Cuccioloni, Massimiliano; Angeletti, Mauro; Salerno, Juan Carlos; Ayub, Nicolas Daniel
- Año de publicación
- 2013
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Acetoacetyl-CoA thiolase (EC 2.3.1.9), commonly named thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA and CoA. This enzyme acts in anabolic processes as the first step in the biosynthesis of isoprenoids and polyhydroxybutyrate in eukaryotes and bacteria, respectively. We have recently reported the evolutionary and functional equivalence of these enzymes, suggesting that thiolase II could be the rate limiting enzyme in these pathways and presented evidence indicating that this enzyme modulates the availability of reducing equivalents during abiotic stress adaptation in bacteria and plants. However, these results are not sufficient to clarify why thiolase II was evolutionary selected as a critical enzyme in the production of antioxidant compounds. Regarding this intriguing topic, we propose that thiolase II could sense changes in the acetyl-CoA/CoA ratio induced by the inhibition of the tricarboxylic acid cycle under abiotic stress. Thus, the high level of evolutionary and functional constraint of thiolase II may be due to the connection of this enzyme with an ancient and conserved metabolic route.
Fil: Fox, Ana Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina
Fil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina
Fil: Mozzicafreddo, Matteo. University of Camerino. School of Biosciences and Biotechnology; Italia
Fil: García, Araceli Nora. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina
Fil: Cuccioloni, Massimiliano. University of Camerino. School of Biosciences and Biotechnology; Italia
Fil: Angeletti, Mauro. University of Camerino. School of Biosciences and Biotechnology; Italia
Fil: Salerno, Juan Carlos. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina
Fil: Ayub, Nicolas Daniel. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina - Materia
-
Thiolase Ii
Coa
Acetyl-Coa
Tricarboxyl Acid Cycle
Antioxidant Compounds - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/4037
Ver los metadatos del registro completo
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Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approachesFox, Ana RominaSoto, Gabriela CynthiaMozzicafreddo, MatteoGarcía, Araceli NoraCuccioloni, MassimilianoAngeletti, MauroSalerno, Juan CarlosAyub, Nicolas DanielThiolase IiCoaAcetyl-CoaTricarboxyl Acid CycleAntioxidant Compoundshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Acetoacetyl-CoA thiolase (EC 2.3.1.9), commonly named thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA and CoA. This enzyme acts in anabolic processes as the first step in the biosynthesis of isoprenoids and polyhydroxybutyrate in eukaryotes and bacteria, respectively. We have recently reported the evolutionary and functional equivalence of these enzymes, suggesting that thiolase II could be the rate limiting enzyme in these pathways and presented evidence indicating that this enzyme modulates the availability of reducing equivalents during abiotic stress adaptation in bacteria and plants. However, these results are not sufficient to clarify why thiolase II was evolutionary selected as a critical enzyme in the production of antioxidant compounds. Regarding this intriguing topic, we propose that thiolase II could sense changes in the acetyl-CoA/CoA ratio induced by the inhibition of the tricarboxylic acid cycle under abiotic stress. Thus, the high level of evolutionary and functional constraint of thiolase II may be due to the connection of this enzyme with an ancient and conserved metabolic route.Fil: Fox, Ana Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; ArgentinaFil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; ArgentinaFil: Mozzicafreddo, Matteo. University of Camerino. School of Biosciences and Biotechnology; ItaliaFil: García, Araceli Nora. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; ArgentinaFil: Cuccioloni, Massimiliano. University of Camerino. School of Biosciences and Biotechnology; ItaliaFil: Angeletti, Mauro. University of Camerino. School of Biosciences and Biotechnology; ItaliaFil: Salerno, Juan Carlos. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; ArgentinaFil: Ayub, Nicolas Daniel. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier2013-10-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/4037Fox, Ana Romina; Soto, Gabriela Cynthia; Mozzicafreddo, Matteo; García, Araceli Nora; Cuccioloni, Massimiliano; et al.; Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches; Elsevier; Gene; 533; 1; 11-10-2013; 5-100378-1119enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0378111913013164info:eu-repo/semantics/altIdentifier/doi/10.1016/j.gene.2013.09.096info:eu-repo/semantics/altIdentifier/issn/0378-1119info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:35:48Zoai:ri.conicet.gov.ar:11336/4037instacron: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 15:35:48.436CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches |
title |
Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches |
spellingShingle |
Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches Fox, Ana Romina Thiolase Ii Coa Acetyl-Coa Tricarboxyl Acid Cycle Antioxidant Compounds |
title_short |
Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches |
title_full |
Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches |
title_fullStr |
Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches |
title_full_unstemmed |
Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches |
title_sort |
Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches |
dc.creator.none.fl_str_mv |
Fox, Ana Romina Soto, Gabriela Cynthia Mozzicafreddo, Matteo García, Araceli Nora Cuccioloni, Massimiliano Angeletti, Mauro Salerno, Juan Carlos Ayub, Nicolas Daniel |
author |
Fox, Ana Romina |
author_facet |
Fox, Ana Romina Soto, Gabriela Cynthia Mozzicafreddo, Matteo García, Araceli Nora Cuccioloni, Massimiliano Angeletti, Mauro Salerno, Juan Carlos Ayub, Nicolas Daniel |
author_role |
author |
author2 |
Soto, Gabriela Cynthia Mozzicafreddo, Matteo García, Araceli Nora Cuccioloni, Massimiliano Angeletti, Mauro Salerno, Juan Carlos Ayub, Nicolas Daniel |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
Thiolase Ii Coa Acetyl-Coa Tricarboxyl Acid Cycle Antioxidant Compounds |
topic |
Thiolase Ii Coa Acetyl-Coa Tricarboxyl Acid Cycle Antioxidant Compounds |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Acetoacetyl-CoA thiolase (EC 2.3.1.9), commonly named thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA and CoA. This enzyme acts in anabolic processes as the first step in the biosynthesis of isoprenoids and polyhydroxybutyrate in eukaryotes and bacteria, respectively. We have recently reported the evolutionary and functional equivalence of these enzymes, suggesting that thiolase II could be the rate limiting enzyme in these pathways and presented evidence indicating that this enzyme modulates the availability of reducing equivalents during abiotic stress adaptation in bacteria and plants. However, these results are not sufficient to clarify why thiolase II was evolutionary selected as a critical enzyme in the production of antioxidant compounds. Regarding this intriguing topic, we propose that thiolase II could sense changes in the acetyl-CoA/CoA ratio induced by the inhibition of the tricarboxylic acid cycle under abiotic stress. Thus, the high level of evolutionary and functional constraint of thiolase II may be due to the connection of this enzyme with an ancient and conserved metabolic route. Fil: Fox, Ana Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina Fil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina Fil: Mozzicafreddo, Matteo. University of Camerino. School of Biosciences and Biotechnology; Italia Fil: García, Araceli Nora. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina Fil: Cuccioloni, Massimiliano. University of Camerino. School of Biosciences and Biotechnology; Italia Fil: Angeletti, Mauro. University of Camerino. School of Biosciences and Biotechnology; Italia Fil: Salerno, Juan Carlos. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina Fil: Ayub, Nicolas Daniel. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina |
description |
Acetoacetyl-CoA thiolase (EC 2.3.1.9), commonly named thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA and CoA. This enzyme acts in anabolic processes as the first step in the biosynthesis of isoprenoids and polyhydroxybutyrate in eukaryotes and bacteria, respectively. We have recently reported the evolutionary and functional equivalence of these enzymes, suggesting that thiolase II could be the rate limiting enzyme in these pathways and presented evidence indicating that this enzyme modulates the availability of reducing equivalents during abiotic stress adaptation in bacteria and plants. However, these results are not sufficient to clarify why thiolase II was evolutionary selected as a critical enzyme in the production of antioxidant compounds. Regarding this intriguing topic, we propose that thiolase II could sense changes in the acetyl-CoA/CoA ratio induced by the inhibition of the tricarboxylic acid cycle under abiotic stress. Thus, the high level of evolutionary and functional constraint of thiolase II may be due to the connection of this enzyme with an ancient and conserved metabolic route. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013-10-11 |
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/11336/4037 Fox, Ana Romina; Soto, Gabriela Cynthia; Mozzicafreddo, Matteo; García, Araceli Nora; Cuccioloni, Massimiliano; et al.; Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches; Elsevier; Gene; 533; 1; 11-10-2013; 5-10 0378-1119 |
url |
http://hdl.handle.net/11336/4037 |
identifier_str_mv |
Fox, Ana Romina; Soto, Gabriela Cynthia; Mozzicafreddo, Matteo; García, Araceli Nora; Cuccioloni, Massimiliano; et al.; Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches; Elsevier; Gene; 533; 1; 11-10-2013; 5-10 0378-1119 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0378111913013164 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.gene.2013.09.096 info:eu-repo/semantics/altIdentifier/issn/0378-1119 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.22299 |