Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa

Autores
Ceccoli, Romina Denis; Bianchi, Dario Alejandro; Fink, Michael J.; Mihovilovic, Marko D.; Rial, Daniela Veronica
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Baeyer–Villiger monooxygenases are recognized by their ability and high selectivity as oxidative biocatalysts for the generation of esters or lactones using ketones as starting materials. These enzymes represent valuable tools for biooxidative syntheses since they can catalyze reactions that otherwise involve strong oxidative reagents. In this work, we present a novel enzyme, the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa. This protein is phylogenetically distant from other well-characterized BVMOs. In order to study this new enzyme, we cloned its gene, expressed it in Escherichia coli and characterized the substrate scope of the Baeyer–Villiger monooxygenase from L. biflexa as a whole-cell biocatalyst. For this purpose, we performed the screening of a collection of ketones with variable structures and sizes, namely acyclic ketones, aromatic ketones, cyclic ketones, and fused ketones. As a result, we observed that this biocatalyst readily oxidized linear- and branched- medium-chain ketones, alkyl levulinates and linear ketones with aromatic substituents with excellent regioselectivity. In addition, this enzyme catalyzed the oxidation of 2-substituted cycloketone derivatives but showed an unusual selection against substituents in positions 3 or 4 of the ring.
Fil: Ceccoli, Romina Denis. Consejo Nacional de Investigaciones Científicas y Técnicas Centro Científico Tecnológico - CONICET -Rosario. Instituto de Biologia Molecular y Celular de Rosario; Argentina
Fil: Bianchi, Dario Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina
Fil: Fink, Michael J.. Vienna University of Technology; Austria. Harvard University; Estados Unidos
Fil: Mihovilovic, Marko D.. Vienna University of Technology; Austria
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
Materia
BAEYER–VILLIGER MONOOXYGENASE
BIOCATALYSIS
KETONES
LEPTOSPIRA
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:11336/50315
Acceder
id CONICETDig_758a345380e860c00b261ed69fb05161
oai_identifier_str oai:ri.conicet.gov.ar:11336/50315
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexaCeccoli, Romina DenisBianchi, Dario AlejandroFink, Michael J.Mihovilovic, Marko D.Rial, Daniela VeronicaBAEYER–VILLIGER MONOOXYGENASEBIOCATALYSISKETONESLEPTOSPIRAhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Baeyer–Villiger monooxygenases are recognized by their ability and high selectivity as oxidative biocatalysts for the generation of esters or lactones using ketones as starting materials. These enzymes represent valuable tools for biooxidative syntheses since they can catalyze reactions that otherwise involve strong oxidative reagents. In this work, we present a novel enzyme, the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa. This protein is phylogenetically distant from other well-characterized BVMOs. In order to study this new enzyme, we cloned its gene, expressed it in Escherichia coli and characterized the substrate scope of the Baeyer–Villiger monooxygenase from L. biflexa as a whole-cell biocatalyst. For this purpose, we performed the screening of a collection of ketones with variable structures and sizes, namely acyclic ketones, aromatic ketones, cyclic ketones, and fused ketones. As a result, we observed that this biocatalyst readily oxidized linear- and branched- medium-chain ketones, alkyl levulinates and linear ketones with aromatic substituents with excellent regioselectivity. In addition, this enzyme catalyzed the oxidation of 2-substituted cycloketone derivatives but showed an unusual selection against substituents in positions 3 or 4 of the ring.Fil: Ceccoli, Romina Denis. Consejo Nacional de Investigaciones Científicas y Técnicas Centro Científico Tecnológico - CONICET -Rosario. Instituto de Biologia Molecular y Celular de Rosario; ArgentinaFil: Bianchi, Dario Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; ArgentinaFil: Fink, Michael J.. Vienna University of Technology; Austria. Harvard University; Estados UnidosFil: Mihovilovic, Marko D.. Vienna University of Technology; AustriaFil: Rial, Daniela Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas Centro Científico Tecnológico - CONICET -Rosario. Instituto de Biologia Molecular y Celular de Rosario; ArgentinaSpringer Verlag Berlín2017-12info: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/11336/50315Ceccoli, Romina Denis; Bianchi, Dario Alejandro; Fink, Michael J.; Mihovilovic, Marko D.; Rial, Daniela Veronica; Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa; Springer Verlag Berlín; AMB Express; 7; 1; 12-2017; 1-132191-0855CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1186/s13568-017-0390-5info:eu-repo/semantics/altIdentifier/url/https://amb-express.springeropen.com/articles/10.1186/s13568-017-0390-5info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:50:19Zoai:ri.conicet.gov.ar:11336/50315instacron: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:34982025-09-03 09:50:19.644CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa
title Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa
spellingShingle Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa
Ceccoli, Romina Denis
BAEYER–VILLIGER MONOOXYGENASE
BIOCATALYSIS
KETONES
LEPTOSPIRA
title_short Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa
title_full Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa
title_fullStr Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa
title_full_unstemmed Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa
title_sort Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa
dc.creator.none.fl_str_mv Ceccoli, Romina Denis
Bianchi, Dario Alejandro
Fink, Michael J.
Mihovilovic, Marko D.
Rial, Daniela Veronica
author Ceccoli, Romina Denis
author_facet Ceccoli, Romina Denis
Bianchi, Dario Alejandro
Fink, Michael J.
Mihovilovic, Marko D.
Rial, Daniela Veronica
author_role author
author2 Bianchi, Dario Alejandro
Fink, Michael J.
Mihovilovic, Marko D.
Rial, Daniela Veronica
author2_role author
author
author
author
dc.subject.none.fl_str_mv BAEYER–VILLIGER MONOOXYGENASE
BIOCATALYSIS
KETONES
LEPTOSPIRA
topic BAEYER–VILLIGER MONOOXYGENASE
BIOCATALYSIS
KETONES
LEPTOSPIRA
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Baeyer–Villiger monooxygenases are recognized by their ability and high selectivity as oxidative biocatalysts for the generation of esters or lactones using ketones as starting materials. These enzymes represent valuable tools for biooxidative syntheses since they can catalyze reactions that otherwise involve strong oxidative reagents. In this work, we present a novel enzyme, the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa. This protein is phylogenetically distant from other well-characterized BVMOs. In order to study this new enzyme, we cloned its gene, expressed it in Escherichia coli and characterized the substrate scope of the Baeyer–Villiger monooxygenase from L. biflexa as a whole-cell biocatalyst. For this purpose, we performed the screening of a collection of ketones with variable structures and sizes, namely acyclic ketones, aromatic ketones, cyclic ketones, and fused ketones. As a result, we observed that this biocatalyst readily oxidized linear- and branched- medium-chain ketones, alkyl levulinates and linear ketones with aromatic substituents with excellent regioselectivity. In addition, this enzyme catalyzed the oxidation of 2-substituted cycloketone derivatives but showed an unusual selection against substituents in positions 3 or 4 of the ring.
Fil: Ceccoli, Romina Denis. Consejo Nacional de Investigaciones Científicas y Técnicas Centro Científico Tecnológico - CONICET -Rosario. Instituto de Biologia Molecular y Celular de Rosario; Argentina
Fil: Bianchi, Dario Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina
Fil: Fink, Michael J.. Vienna University of Technology; Austria. Harvard University; Estados Unidos
Fil: Mihovilovic, Marko D.. Vienna University of Technology; Austria
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
description Baeyer–Villiger monooxygenases are recognized by their ability and high selectivity as oxidative biocatalysts for the generation of esters or lactones using ketones as starting materials. These enzymes represent valuable tools for biooxidative syntheses since they can catalyze reactions that otherwise involve strong oxidative reagents. In this work, we present a novel enzyme, the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa. This protein is phylogenetically distant from other well-characterized BVMOs. In order to study this new enzyme, we cloned its gene, expressed it in Escherichia coli and characterized the substrate scope of the Baeyer–Villiger monooxygenase from L. biflexa as a whole-cell biocatalyst. For this purpose, we performed the screening of a collection of ketones with variable structures and sizes, namely acyclic ketones, aromatic ketones, cyclic ketones, and fused ketones. As a result, we observed that this biocatalyst readily oxidized linear- and branched- medium-chain ketones, alkyl levulinates and linear ketones with aromatic substituents with excellent regioselectivity. In addition, this enzyme catalyzed the oxidation of 2-substituted cycloketone derivatives but showed an unusual selection against substituents in positions 3 or 4 of the ring.
publishDate 2017
dc.date.none.fl_str_mv 2017-12
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/11336/50315
Ceccoli, Romina Denis; Bianchi, Dario Alejandro; Fink, Michael J.; Mihovilovic, Marko D.; Rial, Daniela Veronica; Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa; Springer Verlag Berlín; AMB Express; 7; 1; 12-2017; 1-13
2191-0855
CONICET Digital
CONICET
url http://hdl.handle.net/11336/50315
identifier_str_mv Ceccoli, Romina Denis; Bianchi, Dario Alejandro; Fink, Michael J.; Mihovilovic, Marko D.; Rial, Daniela Veronica; Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa; Springer Verlag Berlín; AMB Express; 7; 1; 12-2017; 1-13
2191-0855
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1186/s13568-017-0390-5
info:eu-repo/semantics/altIdentifier/url/https://amb-express.springeropen.com/articles/10.1186/s13568-017-0390-5
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 Springer Verlag Berlín
publisher.none.fl_str_mv Springer Verlag Berlín
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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score 13.13397

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