Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach
- Autores
- Lozada, Mariana; Rial, Daniela Veronica; Mac Cormack, Walter Patricio; Jansson, Janet K.; Sjöling, Sara; Carroll, JoLynn; Dionisi, Hebe Monica
- Año de publicación
- 2017
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The goal of this work was to identify sequences encoding monooxygenase biocatalysts with novel features by in silico mining an assembled metagenomic dataset of polar and subpolar marine sediments. The targeted enzyme sequences were Baeyer-Villiger and bacterial cytochrome P450 monooxygenases (CYP153). These enzymes have wide-ranging applications, from the synthesis of steroids, antibiotics, mycotoxins and pheromones to the synthesis of monomers for polymerization and anticancer precursors, due to their extraordinary enantio-, regio-, and chemo-selectivity that are valuable features for organic synthesis. Phylogenetic analyses were used to select the most divergent sequences affiliated to these enzyme families among the 264 putative monooxygenases recovered from the ~14 million protein-coding sequences in the assembled metagenome dataset. Three-dimensional structure modeling and docking analysis suggested features useful in biotechnological applications in five metagenomic sequences, such as wide substrate range, novel substrate specificity or regioselectivity. Further analysis revealed structural features associated with psychrophilic enzymes, such as broader substrate accessibility, larger catalytic pockets or low domain interactions, suggesting that they could be applied in biooxidations at room or low temperatures, saving costs inherent to energy consumption. This work allowed the identification of putative enzyme candidates with promising features from metagenomes, providing a suitable starting point for further developments.
Fil: Lozada, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; Argentina
Fil: Rial, Daniela Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas Centro Científico Tecnológico - CONICET -Rosario. Instituto de Biologia Molecular y Celular de Rosario; Argentina
Fil: Mac Cormack, Walter Patricio. Ministerio de Relaciones Exteriores, Comercio Interno y Culto. Dirección Nacional del Antártico. Instituto Antártico Argentino; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina
Fil: Jansson, Janet K.. Pacific Northwest National Laboratory; Estados Unidos
Fil: Sjöling, Sara. Södertörn University; Suecia
Fil: Carroll, JoLynn. Fram-High North Research Centre for Climate and the Environment; Noruega. UiT The Arctic University of Norway; Noruega
Fil: Dionisi, Hebe Monica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; Argentina - Materia
-
BACTERIAL CYTOCHROME P450
BAEYER-VILLIGER MONOOXYGENASES
BIOPROSPECTING BIOCATALYSTS
MOLECULAR MODELING
PHYLOGENETIC ANALYSIS - 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:11336/39169
Ver los metadatos del registro completo
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Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approachLozada, MarianaRial, Daniela VeronicaMac Cormack, Walter PatricioJansson, Janet K.Sjöling, SaraCarroll, JoLynnDionisi, Hebe MonicaBACTERIAL CYTOCHROME P450BAEYER-VILLIGER MONOOXYGENASESBIOPROSPECTING BIOCATALYSTSMOLECULAR MODELINGPHYLOGENETIC ANALYSIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The goal of this work was to identify sequences encoding monooxygenase biocatalysts with novel features by in silico mining an assembled metagenomic dataset of polar and subpolar marine sediments. The targeted enzyme sequences were Baeyer-Villiger and bacterial cytochrome P450 monooxygenases (CYP153). These enzymes have wide-ranging applications, from the synthesis of steroids, antibiotics, mycotoxins and pheromones to the synthesis of monomers for polymerization and anticancer precursors, due to their extraordinary enantio-, regio-, and chemo-selectivity that are valuable features for organic synthesis. Phylogenetic analyses were used to select the most divergent sequences affiliated to these enzyme families among the 264 putative monooxygenases recovered from the ~14 million protein-coding sequences in the assembled metagenome dataset. Three-dimensional structure modeling and docking analysis suggested features useful in biotechnological applications in five metagenomic sequences, such as wide substrate range, novel substrate specificity or regioselectivity. Further analysis revealed structural features associated with psychrophilic enzymes, such as broader substrate accessibility, larger catalytic pockets or low domain interactions, suggesting that they could be applied in biooxidations at room or low temperatures, saving costs inherent to energy consumption. This work allowed the identification of putative enzyme candidates with promising features from metagenomes, providing a suitable starting point for further developments.Fil: Lozada, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; ArgentinaFil: Rial, Daniela Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas Centro Científico Tecnológico - CONICET -Rosario. Instituto de Biologia Molecular y Celular de Rosario; ArgentinaFil: Mac Cormack, Walter Patricio. Ministerio de Relaciones Exteriores, Comercio Interno y Culto. Dirección Nacional del Antártico. Instituto Antártico Argentino; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; ArgentinaFil: Jansson, Janet K.. Pacific Northwest National Laboratory; Estados UnidosFil: Sjöling, Sara. Södertörn University; SueciaFil: Carroll, JoLynn. Fram-High North Research Centre for Climate and the Environment; Noruega. UiT The Arctic University of Norway; NoruegaFil: Dionisi, Hebe Monica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; ArgentinaMolecular Diversity Preservation International2017-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/39169Lozada, Mariana; Rial, Daniela Veronica; Mac Cormack, Walter Patricio; Jansson, Janet K.; Sjöling, Sara; et al.; Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach; Molecular Diversity Preservation International; Marine Drugs; 15; 4; 4-2017; 1-191660-3397CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1660-3397/15/4/114info:eu-repo/semantics/altIdentifier/doi/10.3390/md15040114info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:49:57Zoai:ri.conicet.gov.ar:11336/39169instacron: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 09:49:57.355CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach |
title |
Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach |
spellingShingle |
Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach Lozada, Mariana BACTERIAL CYTOCHROME P450 BAEYER-VILLIGER MONOOXYGENASES BIOPROSPECTING BIOCATALYSTS MOLECULAR MODELING PHYLOGENETIC ANALYSIS |
title_short |
Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach |
title_full |
Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach |
title_fullStr |
Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach |
title_full_unstemmed |
Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach |
title_sort |
Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach |
dc.creator.none.fl_str_mv |
Lozada, Mariana Rial, Daniela Veronica Mac Cormack, Walter Patricio Jansson, Janet K. Sjöling, Sara Carroll, JoLynn Dionisi, Hebe Monica |
author |
Lozada, Mariana |
author_facet |
Lozada, Mariana Rial, Daniela Veronica Mac Cormack, Walter Patricio Jansson, Janet K. Sjöling, Sara Carroll, JoLynn Dionisi, Hebe Monica |
author_role |
author |
author2 |
Rial, Daniela Veronica Mac Cormack, Walter Patricio Jansson, Janet K. Sjöling, Sara Carroll, JoLynn Dionisi, Hebe Monica |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
BACTERIAL CYTOCHROME P450 BAEYER-VILLIGER MONOOXYGENASES BIOPROSPECTING BIOCATALYSTS MOLECULAR MODELING PHYLOGENETIC ANALYSIS |
topic |
BACTERIAL CYTOCHROME P450 BAEYER-VILLIGER MONOOXYGENASES BIOPROSPECTING BIOCATALYSTS MOLECULAR MODELING PHYLOGENETIC ANALYSIS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The goal of this work was to identify sequences encoding monooxygenase biocatalysts with novel features by in silico mining an assembled metagenomic dataset of polar and subpolar marine sediments. The targeted enzyme sequences were Baeyer-Villiger and bacterial cytochrome P450 monooxygenases (CYP153). These enzymes have wide-ranging applications, from the synthesis of steroids, antibiotics, mycotoxins and pheromones to the synthesis of monomers for polymerization and anticancer precursors, due to their extraordinary enantio-, regio-, and chemo-selectivity that are valuable features for organic synthesis. Phylogenetic analyses were used to select the most divergent sequences affiliated to these enzyme families among the 264 putative monooxygenases recovered from the ~14 million protein-coding sequences in the assembled metagenome dataset. Three-dimensional structure modeling and docking analysis suggested features useful in biotechnological applications in five metagenomic sequences, such as wide substrate range, novel substrate specificity or regioselectivity. Further analysis revealed structural features associated with psychrophilic enzymes, such as broader substrate accessibility, larger catalytic pockets or low domain interactions, suggesting that they could be applied in biooxidations at room or low temperatures, saving costs inherent to energy consumption. This work allowed the identification of putative enzyme candidates with promising features from metagenomes, providing a suitable starting point for further developments. Fil: Lozada, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; Argentina Fil: Rial, Daniela Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas Centro Científico Tecnológico - CONICET -Rosario. Instituto de Biologia Molecular y Celular de Rosario; Argentina Fil: Mac Cormack, Walter Patricio. Ministerio de Relaciones Exteriores, Comercio Interno y Culto. Dirección Nacional del Antártico. Instituto Antártico Argentino; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Jansson, Janet K.. Pacific Northwest National Laboratory; Estados Unidos Fil: Sjöling, Sara. Södertörn University; Suecia Fil: Carroll, JoLynn. Fram-High North Research Centre for Climate and the Environment; Noruega. UiT The Arctic University of Norway; Noruega Fil: Dionisi, Hebe Monica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; Argentina |
description |
The goal of this work was to identify sequences encoding monooxygenase biocatalysts with novel features by in silico mining an assembled metagenomic dataset of polar and subpolar marine sediments. The targeted enzyme sequences were Baeyer-Villiger and bacterial cytochrome P450 monooxygenases (CYP153). These enzymes have wide-ranging applications, from the synthesis of steroids, antibiotics, mycotoxins and pheromones to the synthesis of monomers for polymerization and anticancer precursors, due to their extraordinary enantio-, regio-, and chemo-selectivity that are valuable features for organic synthesis. Phylogenetic analyses were used to select the most divergent sequences affiliated to these enzyme families among the 264 putative monooxygenases recovered from the ~14 million protein-coding sequences in the assembled metagenome dataset. Three-dimensional structure modeling and docking analysis suggested features useful in biotechnological applications in five metagenomic sequences, such as wide substrate range, novel substrate specificity or regioselectivity. Further analysis revealed structural features associated with psychrophilic enzymes, such as broader substrate accessibility, larger catalytic pockets or low domain interactions, suggesting that they could be applied in biooxidations at room or low temperatures, saving costs inherent to energy consumption. This work allowed the identification of putative enzyme candidates with promising features from metagenomes, providing a suitable starting point for further developments. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-04 |
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/11336/39169 Lozada, Mariana; Rial, Daniela Veronica; Mac Cormack, Walter Patricio; Jansson, Janet K.; Sjöling, Sara; et al.; Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach; Molecular Diversity Preservation International; Marine Drugs; 15; 4; 4-2017; 1-19 1660-3397 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/39169 |
identifier_str_mv |
Lozada, Mariana; Rial, Daniela Veronica; Mac Cormack, Walter Patricio; Jansson, Janet K.; Sjöling, Sara; et al.; Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach; Molecular Diversity Preservation International; Marine Drugs; 15; 4; 4-2017; 1-19 1660-3397 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://www.mdpi.com/1660-3397/15/4/114 info:eu-repo/semantics/altIdentifier/doi/10.3390/md15040114 |
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 |
dc.publisher.none.fl_str_mv |
Molecular Diversity Preservation International |
publisher.none.fl_str_mv |
Molecular Diversity Preservation International |
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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1844613542772211712 |
score |
13.070432 |