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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/39169

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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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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