Evolution of enzyme functionality in the flavin-containing monooxygenases

Autores
Bailleul, Gautier; Yang, Guang; Nicoll, Callum R.; Mattevi, Andrea; Fraaije, Marco W.; Mascotti, María Laura
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Among the molecular mechanisms of adaptation in biology, enzyme functional diversification is indispensable. By allowing organisms to expand their catalytic repertoires and adopt fundamentally different chemistries, animals can harness or eliminate new-found substances and xenobiotics that they are exposed to in new environments. Here, we explore the flavin-containing monooxygenases (FMOs) that are essential for xenobiotic detoxification. Employing a paleobiochemistry approach in combination with enzymology techniques we disclose the set of historical substitutions responsible for the family’s functional diversification in tetrapods. Remarkably, a few amino acid replacements differentiate an ancestral multi-tasking FMO into a more specialized monooxygenase by modulating the oxygenating flavin intermediate. Our findings substantiate an ongoing premise that enzymatic function hinges on a subset of residues that is not limited to the active site core.
Fil: Bailleul, Gautier. University of Groningen; Países Bajos
Fil: Yang, Guang. University of Groningen; Países Bajos
Fil: Nicoll, Callum R.. Universita degli Studi di Pavia; Italia
Fil: Mattevi, Andrea. Universita degli Studi di Pavia; Italia
Fil: Fraaije, Marco W.. University of Groningen; Países Bajos
Fil: Mascotti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Materia
FUNCTIONAL DIVERGENCE
FLAVIN-CONTAINING MONOOXYGENASES
HISTORICAL BIOCHEMISTRY
ASR
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/227629
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Evolution of enzyme functionality in the flavin-containing monooxygenasesBailleul, GautierYang, GuangNicoll, Callum R.Mattevi, AndreaFraaije, Marco W.Mascotti, María LauraFUNCTIONAL DIVERGENCEFLAVIN-CONTAINING MONOOXYGENASESHISTORICAL BIOCHEMISTRYASRhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Among the molecular mechanisms of adaptation in biology, enzyme functional diversification is indispensable. By allowing organisms to expand their catalytic repertoires and adopt fundamentally different chemistries, animals can harness or eliminate new-found substances and xenobiotics that they are exposed to in new environments. Here, we explore the flavin-containing monooxygenases (FMOs) that are essential for xenobiotic detoxification. Employing a paleobiochemistry approach in combination with enzymology techniques we disclose the set of historical substitutions responsible for the family’s functional diversification in tetrapods. Remarkably, a few amino acid replacements differentiate an ancestral multi-tasking FMO into a more specialized monooxygenase by modulating the oxygenating flavin intermediate. Our findings substantiate an ongoing premise that enzymatic function hinges on a subset of residues that is not limited to the active site core.Fil: Bailleul, Gautier. University of Groningen; Países BajosFil: Yang, Guang. University of Groningen; Países BajosFil: Nicoll, Callum R.. Universita degli Studi di Pavia; ItaliaFil: Mattevi, Andrea. Universita degli Studi di Pavia; ItaliaFil: Fraaije, Marco W.. University of Groningen; Países BajosFil: Mascotti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaSpringer2023-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/227629Bailleul, Gautier; Yang, Guang; Nicoll, Callum R.; Mattevi, Andrea; Fraaije, Marco W.; et al.; Evolution of enzyme functionality in the flavin-containing monooxygenases; Springer; Nature Communications; 14; 1; 2-2023; 1-102041-1723CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41467-023-36756-xinfo:eu-repo/semantics/altIdentifier/doi/10.1038/s41467-023-36756-xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:40:21Zoai:ri.conicet.gov.ar:11336/227629instacron: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 15:40:21.71CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Evolution of enzyme functionality in the flavin-containing monooxygenases
title Evolution of enzyme functionality in the flavin-containing monooxygenases
spellingShingle Evolution of enzyme functionality in the flavin-containing monooxygenases
Bailleul, Gautier
FUNCTIONAL DIVERGENCE
FLAVIN-CONTAINING MONOOXYGENASES
HISTORICAL BIOCHEMISTRY
ASR
title_short Evolution of enzyme functionality in the flavin-containing monooxygenases
title_full Evolution of enzyme functionality in the flavin-containing monooxygenases
title_fullStr Evolution of enzyme functionality in the flavin-containing monooxygenases
title_full_unstemmed Evolution of enzyme functionality in the flavin-containing monooxygenases
title_sort Evolution of enzyme functionality in the flavin-containing monooxygenases
dc.creator.none.fl_str_mv Bailleul, Gautier
Yang, Guang
Nicoll, Callum R.
Mattevi, Andrea
Fraaije, Marco W.
Mascotti, María Laura
author Bailleul, Gautier
author_facet Bailleul, Gautier
Yang, Guang
Nicoll, Callum R.
Mattevi, Andrea
Fraaije, Marco W.
Mascotti, María Laura
author_role author
author2 Yang, Guang
Nicoll, Callum R.
Mattevi, Andrea
Fraaije, Marco W.
Mascotti, María Laura
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv FUNCTIONAL DIVERGENCE
FLAVIN-CONTAINING MONOOXYGENASES
HISTORICAL BIOCHEMISTRY
ASR
topic FUNCTIONAL DIVERGENCE
FLAVIN-CONTAINING MONOOXYGENASES
HISTORICAL BIOCHEMISTRY
ASR
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Among the molecular mechanisms of adaptation in biology, enzyme functional diversification is indispensable. By allowing organisms to expand their catalytic repertoires and adopt fundamentally different chemistries, animals can harness or eliminate new-found substances and xenobiotics that they are exposed to in new environments. Here, we explore the flavin-containing monooxygenases (FMOs) that are essential for xenobiotic detoxification. Employing a paleobiochemistry approach in combination with enzymology techniques we disclose the set of historical substitutions responsible for the family’s functional diversification in tetrapods. Remarkably, a few amino acid replacements differentiate an ancestral multi-tasking FMO into a more specialized monooxygenase by modulating the oxygenating flavin intermediate. Our findings substantiate an ongoing premise that enzymatic function hinges on a subset of residues that is not limited to the active site core.
Fil: Bailleul, Gautier. University of Groningen; Países Bajos
Fil: Yang, Guang. University of Groningen; Países Bajos
Fil: Nicoll, Callum R.. Universita degli Studi di Pavia; Italia
Fil: Mattevi, Andrea. Universita degli Studi di Pavia; Italia
Fil: Fraaije, Marco W.. University of Groningen; Países Bajos
Fil: Mascotti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
description Among the molecular mechanisms of adaptation in biology, enzyme functional diversification is indispensable. By allowing organisms to expand their catalytic repertoires and adopt fundamentally different chemistries, animals can harness or eliminate new-found substances and xenobiotics that they are exposed to in new environments. Here, we explore the flavin-containing monooxygenases (FMOs) that are essential for xenobiotic detoxification. Employing a paleobiochemistry approach in combination with enzymology techniques we disclose the set of historical substitutions responsible for the family’s functional diversification in tetrapods. Remarkably, a few amino acid replacements differentiate an ancestral multi-tasking FMO into a more specialized monooxygenase by modulating the oxygenating flavin intermediate. Our findings substantiate an ongoing premise that enzymatic function hinges on a subset of residues that is not limited to the active site core.
publishDate 2023
dc.date.none.fl_str_mv 2023-02
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/11336/227629
Bailleul, Gautier; Yang, Guang; Nicoll, Callum R.; Mattevi, Andrea; Fraaije, Marco W.; et al.; Evolution of enzyme functionality in the flavin-containing monooxygenases; Springer; Nature Communications; 14; 1; 2-2023; 1-10
2041-1723
CONICET Digital
CONICET
url http://hdl.handle.net/11336/227629
identifier_str_mv Bailleul, Gautier; Yang, Guang; Nicoll, Callum R.; Mattevi, Andrea; Fraaije, Marco W.; et al.; Evolution of enzyme functionality in the flavin-containing monooxygenases; Springer; Nature Communications; 14; 1; 2-2023; 1-10
2041-1723
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://www.nature.com/articles/s41467-023-36756-x
info:eu-repo/semantics/altIdentifier/doi/10.1038/s41467-023-36756-x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
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 13.22299

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