Reconstructing the evolutionary history of F420-dependent dehydrogenases

Autores
Mascotti, María Laura; Kumar, Hemant; Nguyen, Quoc-Thai; Juri Ayub, Maximiliano; Fraaije, Marco Wilhelmus
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
During the last decade the number of characterized F420-dependent enzymes has significantly increased. Many of these deazaflavoproteins share a TIM-barrel fold and are structurally related to FMN-dependent luciferases and monooxygenases. In this work, we traced the origin and evolutionary history of the F420-dependent enzymes within the luciferase-like superfamily. By a thorough phylogenetic analysis we inferred that the F420-dependent enzymes emerged from a FMN-dependent common ancestor. Furthermore, the data show that during evolution, the family of deazaflavoproteins split into two well-defined groups of enzymes: the F420-dependent dehydrogenases and the F420-dependent reductases. By such event, the dehydrogenases specialized in generating the reduced deazaflavin cofactor, while the reductases employ the reduced F420 for catalysis. Particularly, we focused on investigating the dehydrogenase subfamily and demonstrated that this group diversified into three types of dehydrogenases: the already known F420-dependent glucose-6-phosphate dehydrogenases, the F420-dependent alcohol dehydrogenases, and the sugar-6-phosphate dehydrogenases that were identified in this study. By reconstructing and experimentally characterizing ancestral and extant representatives of F420-dependent dehydrogenases, their biochemical properties were investigated and compared. We propose an evolutionary path for the emergence and diversification of the TIM-barrel fold F420-dependent dehydrogenases subfamily.
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
Fil: Kumar, Hemant. University of Groningen. Faculty of Mathematics and Natural Sciences; Países Bajos
Fil: Nguyen, Quoc-Thai. Scuola Universitaria Superiore IUSS Pavia; Italia. University of Groningen. Faculty of Mathematics and Natural Sciences; Países Bajos. University of Medicine and Pharmacy; Vietnam
Fil: Juri Ayub, Maximiliano. 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
Fil: Fraaije, Marco Wilhelmus. University of Groningen. Faculty of Mathematics and Natural Sciences; Países Bajos
Materia
F420
FGDs
glucose-6-phosphate
dehydrogenases
TIM-barrel
deazaflavins
ancestral sequence reconstruction
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/89010
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/89010
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Reconstructing the evolutionary history of F420-dependent dehydrogenasesMascotti, María LauraKumar, HemantNguyen, Quoc-ThaiJuri Ayub, MaximilianoFraaije, Marco WilhelmusF420FGDsglucose-6-phosphatedehydrogenasesTIM-barreldeazaflavinsancestral sequence reconstructionhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1During the last decade the number of characterized F420-dependent enzymes has significantly increased. Many of these deazaflavoproteins share a TIM-barrel fold and are structurally related to FMN-dependent luciferases and monooxygenases. In this work, we traced the origin and evolutionary history of the F420-dependent enzymes within the luciferase-like superfamily. By a thorough phylogenetic analysis we inferred that the F420-dependent enzymes emerged from a FMN-dependent common ancestor. Furthermore, the data show that during evolution, the family of deazaflavoproteins split into two well-defined groups of enzymes: the F420-dependent dehydrogenases and the F420-dependent reductases. By such event, the dehydrogenases specialized in generating the reduced deazaflavin cofactor, while the reductases employ the reduced F420 for catalysis. Particularly, we focused on investigating the dehydrogenase subfamily and demonstrated that this group diversified into three types of dehydrogenases: the already known F420-dependent glucose-6-phosphate dehydrogenases, the F420-dependent alcohol dehydrogenases, and the sugar-6-phosphate dehydrogenases that were identified in this study. By reconstructing and experimentally characterizing ancestral and extant representatives of F420-dependent dehydrogenases, their biochemical properties were investigated and compared. We propose an evolutionary path for the emergence and diversification of the TIM-barrel fold F420-dependent dehydrogenases subfamily.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; ArgentinaFil: Kumar, Hemant. University of Groningen. Faculty of Mathematics and Natural Sciences; Países BajosFil: Nguyen, Quoc-Thai. Scuola Universitaria Superiore IUSS Pavia; Italia. University of Groningen. Faculty of Mathematics and Natural Sciences; Países Bajos. University of Medicine and Pharmacy; VietnamFil: Juri Ayub, Maximiliano. 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; ArgentinaFil: Fraaije, Marco Wilhelmus. University of Groningen. Faculty of Mathematics and Natural Sciences; Países BajosNature Publishing Group2018-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/89010Mascotti, María Laura; Kumar, Hemant; Nguyen, Quoc-Thai; Juri Ayub, Maximiliano; Fraaije, Marco Wilhelmus; Reconstructing the evolutionary history of F420-dependent dehydrogenases; Nature Publishing Group; Scientific Reports; 8; 1; 12-2018; 1-102045-2322CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41598-018-35590-2info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-018-35590-2info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6279831/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:51:44Zoai:ri.conicet.gov.ar:11336/89010instacron: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 09:51:44.634CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Reconstructing the evolutionary history of F420-dependent dehydrogenases
title Reconstructing the evolutionary history of F420-dependent dehydrogenases
spellingShingle Reconstructing the evolutionary history of F420-dependent dehydrogenases
Mascotti, María Laura
F420
FGDs
glucose-6-phosphate
dehydrogenases
TIM-barrel
deazaflavins
ancestral sequence reconstruction
title_short Reconstructing the evolutionary history of F420-dependent dehydrogenases
title_full Reconstructing the evolutionary history of F420-dependent dehydrogenases
title_fullStr Reconstructing the evolutionary history of F420-dependent dehydrogenases
title_full_unstemmed Reconstructing the evolutionary history of F420-dependent dehydrogenases
title_sort Reconstructing the evolutionary history of F420-dependent dehydrogenases
dc.creator.none.fl_str_mv Mascotti, María Laura
Kumar, Hemant
Nguyen, Quoc-Thai
Juri Ayub, Maximiliano
Fraaije, Marco Wilhelmus
author Mascotti, María Laura
author_facet Mascotti, María Laura
Kumar, Hemant
Nguyen, Quoc-Thai
Juri Ayub, Maximiliano
Fraaije, Marco Wilhelmus
author_role author
author2 Kumar, Hemant
Nguyen, Quoc-Thai
Juri Ayub, Maximiliano
Fraaije, Marco Wilhelmus
author2_role author
author
author
author
dc.subject.none.fl_str_mv F420
FGDs
glucose-6-phosphate
dehydrogenases
TIM-barrel
deazaflavins
ancestral sequence reconstruction
topic F420
FGDs
glucose-6-phosphate
dehydrogenases
TIM-barrel
deazaflavins
ancestral sequence reconstruction
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 During the last decade the number of characterized F420-dependent enzymes has significantly increased. Many of these deazaflavoproteins share a TIM-barrel fold and are structurally related to FMN-dependent luciferases and monooxygenases. In this work, we traced the origin and evolutionary history of the F420-dependent enzymes within the luciferase-like superfamily. By a thorough phylogenetic analysis we inferred that the F420-dependent enzymes emerged from a FMN-dependent common ancestor. Furthermore, the data show that during evolution, the family of deazaflavoproteins split into two well-defined groups of enzymes: the F420-dependent dehydrogenases and the F420-dependent reductases. By such event, the dehydrogenases specialized in generating the reduced deazaflavin cofactor, while the reductases employ the reduced F420 for catalysis. Particularly, we focused on investigating the dehydrogenase subfamily and demonstrated that this group diversified into three types of dehydrogenases: the already known F420-dependent glucose-6-phosphate dehydrogenases, the F420-dependent alcohol dehydrogenases, and the sugar-6-phosphate dehydrogenases that were identified in this study. By reconstructing and experimentally characterizing ancestral and extant representatives of F420-dependent dehydrogenases, their biochemical properties were investigated and compared. We propose an evolutionary path for the emergence and diversification of the TIM-barrel fold F420-dependent dehydrogenases subfamily.
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
Fil: Kumar, Hemant. University of Groningen. Faculty of Mathematics and Natural Sciences; Países Bajos
Fil: Nguyen, Quoc-Thai. Scuola Universitaria Superiore IUSS Pavia; Italia. University of Groningen. Faculty of Mathematics and Natural Sciences; Países Bajos. University of Medicine and Pharmacy; Vietnam
Fil: Juri Ayub, Maximiliano. 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
Fil: Fraaije, Marco Wilhelmus. University of Groningen. Faculty of Mathematics and Natural Sciences; Países Bajos
description During the last decade the number of characterized F420-dependent enzymes has significantly increased. Many of these deazaflavoproteins share a TIM-barrel fold and are structurally related to FMN-dependent luciferases and monooxygenases. In this work, we traced the origin and evolutionary history of the F420-dependent enzymes within the luciferase-like superfamily. By a thorough phylogenetic analysis we inferred that the F420-dependent enzymes emerged from a FMN-dependent common ancestor. Furthermore, the data show that during evolution, the family of deazaflavoproteins split into two well-defined groups of enzymes: the F420-dependent dehydrogenases and the F420-dependent reductases. By such event, the dehydrogenases specialized in generating the reduced deazaflavin cofactor, while the reductases employ the reduced F420 for catalysis. Particularly, we focused on investigating the dehydrogenase subfamily and demonstrated that this group diversified into three types of dehydrogenases: the already known F420-dependent glucose-6-phosphate dehydrogenases, the F420-dependent alcohol dehydrogenases, and the sugar-6-phosphate dehydrogenases that were identified in this study. By reconstructing and experimentally characterizing ancestral and extant representatives of F420-dependent dehydrogenases, their biochemical properties were investigated and compared. We propose an evolutionary path for the emergence and diversification of the TIM-barrel fold F420-dependent dehydrogenases subfamily.
publishDate 2018
dc.date.none.fl_str_mv 2018-12
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/11336/89010
Mascotti, María Laura; Kumar, Hemant; Nguyen, Quoc-Thai; Juri Ayub, Maximiliano; Fraaije, Marco Wilhelmus; Reconstructing the evolutionary history of F420-dependent dehydrogenases; Nature Publishing Group; Scientific Reports; 8; 1; 12-2018; 1-10
2045-2322
CONICET Digital
CONICET
url http://hdl.handle.net/11336/89010
identifier_str_mv Mascotti, María Laura; Kumar, Hemant; Nguyen, Quoc-Thai; Juri Ayub, Maximiliano; Fraaije, Marco Wilhelmus; Reconstructing the evolutionary history of F420-dependent dehydrogenases; Nature Publishing Group; Scientific Reports; 8; 1; 12-2018; 1-10
2045-2322
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/s41598-018-35590-2
info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-018-35590-2
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6279831/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
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 13.070432

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