A Computer Simulation Insight into the Formation of Apocarotenoids: Study of the Carotenoid Oxygenases BCO1 and BCO2 and Their Interaction with Putative Substrates

Carotenoids are isoprenoid pigments, and sources of vitamin A in humans. The first metabolic pathway for their synthesis is mediated by the enzymes β,β-carotene-15,15′-dioxygenase (BCO1) and β,β-carotene-9′,10′-dioxygenase (BCO2), which cleave carotenoids into smaller compounds, called apocarotenoid...

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Autores: Martínez, Anabela, Cantero, Jorge, Meléndez Martínez, Antonio Jesús, Paulino, Margot
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/141877
Acceso en línea:https://hdl.handle.net/11441/141877
https://doi.org/10.3390/molecules27227813
Access Level:acceso abierto
Palabra clave:Carotenoid oxygenases
Ligand interaction
Molecular dynamics
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spelling A Computer Simulation Insight into the Formation of Apocarotenoids: Study of the Carotenoid Oxygenases BCO1 and BCO2 and Their Interaction with Putative SubstratesMartínez, AnabelaCantero, JorgeMeléndez Martínez, Antonio JesúsPaulino, MargotCarotenoid oxygenasesLigand interactionMolecular dynamicsCarotenoids are isoprenoid pigments, and sources of vitamin A in humans. The first metabolic pathway for their synthesis is mediated by the enzymes β,β-carotene-15,15′-dioxygenase (BCO1) and β,β-carotene-9′,10′-dioxygenase (BCO2), which cleave carotenoids into smaller compounds, called apocarotenoids. The objective of this study is to gain insight into the interaction of BCO1 and BCO2 with carotenoids, adding structural diversity and importance in the agro-food and/or health sectors. Homology modeling of BCO1 and BCO2, and the molecular dynamics of complexes with all carotenoids were performed. Interaction energy and structures were analyzed. For both enzymes, the general structure is conserved with a seven beta-sheet structure, and the β-carotene is positioned at an optimal distance from the catalytic center. Fe2+ forms in an octahedral coordination sphere with four perfectly conserved histidine residues. BCO1 finds stability in a structure in which the β-carotene is positioned ready for enzymatic catalysis at the 15–15′ bond, and BCO2 in positioning the bond to be cleaved (C9–C10) close to the active site. In BCO1 the carotenoids interact with only seven residues with aromatic rings, while the interaction of BCO2 is much more varied in terms of the type of interaction, with more residues of different chemical natures.Multidisciplinary Digital Publishing Institute (MDPI)Nutrición y Bromatología, Toxicología y Medicina Legal2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/141877https://doi.org/10.3390/molecules27227813reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésMolecules, 27 (22), 7813.https://doi.org/10.3390/molecules27227813info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1418772026-06-17T12:51:07Z
dc.title.none.fl_str_mv A Computer Simulation Insight into the Formation of Apocarotenoids: Study of the Carotenoid Oxygenases BCO1 and BCO2 and Their Interaction with Putative Substrates
title A Computer Simulation Insight into the Formation of Apocarotenoids: Study of the Carotenoid Oxygenases BCO1 and BCO2 and Their Interaction with Putative Substrates
spellingShingle A Computer Simulation Insight into the Formation of Apocarotenoids: Study of the Carotenoid Oxygenases BCO1 and BCO2 and Their Interaction with Putative Substrates
Martínez, Anabela
Carotenoid oxygenases
Ligand interaction
Molecular dynamics
title_short A Computer Simulation Insight into the Formation of Apocarotenoids: Study of the Carotenoid Oxygenases BCO1 and BCO2 and Their Interaction with Putative Substrates
title_full A Computer Simulation Insight into the Formation of Apocarotenoids: Study of the Carotenoid Oxygenases BCO1 and BCO2 and Their Interaction with Putative Substrates
title_fullStr A Computer Simulation Insight into the Formation of Apocarotenoids: Study of the Carotenoid Oxygenases BCO1 and BCO2 and Their Interaction with Putative Substrates
title_full_unstemmed A Computer Simulation Insight into the Formation of Apocarotenoids: Study of the Carotenoid Oxygenases BCO1 and BCO2 and Their Interaction with Putative Substrates
title_sort A Computer Simulation Insight into the Formation of Apocarotenoids: Study of the Carotenoid Oxygenases BCO1 and BCO2 and Their Interaction with Putative Substrates
dc.creator.none.fl_str_mv Martínez, Anabela
Cantero, Jorge
Meléndez Martínez, Antonio Jesús
Paulino, Margot
author Martínez, Anabela
author_facet Martínez, Anabela
Cantero, Jorge
Meléndez Martínez, Antonio Jesús
Paulino, Margot
author_role author
author2 Cantero, Jorge
Meléndez Martínez, Antonio Jesús
Paulino, Margot
author2_role author
author
author
dc.contributor.none.fl_str_mv Nutrición y Bromatología, Toxicología y Medicina Legal
dc.subject.none.fl_str_mv Carotenoid oxygenases
Ligand interaction
Molecular dynamics
topic Carotenoid oxygenases
Ligand interaction
Molecular dynamics
description Carotenoids are isoprenoid pigments, and sources of vitamin A in humans. The first metabolic pathway for their synthesis is mediated by the enzymes β,β-carotene-15,15′-dioxygenase (BCO1) and β,β-carotene-9′,10′-dioxygenase (BCO2), which cleave carotenoids into smaller compounds, called apocarotenoids. The objective of this study is to gain insight into the interaction of BCO1 and BCO2 with carotenoids, adding structural diversity and importance in the agro-food and/or health sectors. Homology modeling of BCO1 and BCO2, and the molecular dynamics of complexes with all carotenoids were performed. Interaction energy and structures were analyzed. For both enzymes, the general structure is conserved with a seven beta-sheet structure, and the β-carotene is positioned at an optimal distance from the catalytic center. Fe2+ forms in an octahedral coordination sphere with four perfectly conserved histidine residues. BCO1 finds stability in a structure in which the β-carotene is positioned ready for enzymatic catalysis at the 15–15′ bond, and BCO2 in positioning the bond to be cleaved (C9–C10) close to the active site. In BCO1 the carotenoids interact with only seven residues with aromatic rings, while the interaction of BCO2 is much more varied in terms of the type of interaction, with more residues of different chemical natures.
publishDate 2022
dc.date.none.fl_str_mv 2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/141877
https://doi.org/10.3390/molecules27227813
url https://hdl.handle.net/11441/141877
https://doi.org/10.3390/molecules27227813
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Molecules, 27 (22), 7813.
https://doi.org/10.3390/molecules27227813
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute (MDPI)
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute (MDPI)
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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