Deciphering the molecular specificity of phenolic compounds as inhibitors or glycosyl acceptors of β-fructofuranosidase from Xanthophyllomyces dendrorhous

13 pags., 6 figs., 2 tabs. -- Open Access funded by Creative Commons Atribution Licence 4.0

Detalles Bibliográficos
Autores: Ramírez-Escudero, Mercedes, Míguez, Noa, Gimeno-Pérez, María, Ballesteros Olmo, Antonio, Fernández Lobato, María, Plou Gasca, Francisco José, Sanz-Aparicio, J.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2019
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/205007
Acceso en línea:http://hdl.handle.net/10261/205007
Access Level:acceso abierto
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spelling Deciphering the molecular specificity of phenolic compounds as inhibitors or glycosyl acceptors of β-fructofuranosidase from Xanthophyllomyces dendrorhousRamírez-Escudero, MercedesMíguez, NoaGimeno-Pérez, MaríaBallesteros Olmo, AntonioFernández Lobato, MaríaPlou Gasca, Francisco JoséSanz-Aparicio, J.13 pags., 6 figs., 2 tabs. -- Open Access funded by Creative Commons Atribution Licence 4.0Enzymatic glycosylation of polyphenols is a tool to improve their physicochemical properties and bioavailability. On the other hand, glycosidic enzymes can be inhibited by phenolic compounds. In this work, we studied the specificity of various phenolics (hydroquinone, hydroxytyrosol, epigallocatechin gallate, catechol and p-nitrophenol) as fructosyl acceptors or inhibitors of the β-fructofuranosidase from Xanthophyllomyces dendrorhous (pXd-INV). Only hydroquinone and hydroxytyrosol gave rise to the formation of glycosylated products. For the rest, an inhibitory effect on both the hydrolytic (H) and transglycosylation (T) activity of pXd-INV, as well as an increase in the H/T ratio, was observed. To disclose the binding mode of each compound and elucidate the molecular features determining its acceptor or inhibitor behaviour, ternary complexes of the inactive mutant pXd-INV-D80A with fructose and the different polyphenols were analyzed by X-ray crystallography. All the compounds bind by stacking against Trp105 and locate one of their phenolic hydroxyls making a polar linkage to the fructose O2 at 3.6-3.8 Å from the C2, which could enable the ulterior nucleophilic attack leading to transfructosylation. Binding of hydroquinone was further investigated by soaking in absence of fructose, showing a flexible site that likely allows productive motion of the intermediates. Therefore, the acceptor capacity of the different polyphenols seems mediated by their ability to make flexible polar links with the protein, this flexibility being essential for the transfructosylation reaction to proceed. Finally, the binding affinity of the phenolic compounds was explained based on the two sites previously reported for pXd-INV.Tis work was supported by grants from the Spanish Ministry of Economy and Competitiveness (BIO2016- 76601-C3-1-R/2-R/3-R), the Fundación Ramón Areces (XIX Call of Research Grants in Life and Materials Sciences) and the European Union’s Horizon 2020 research and innovation program Blue Growth (Agreement No. 634486, INMARE). M.G.-P. thanks the Spanish Ministry of Education for FPU Grant. We thank the Fundación Ramón Areces by an institutional grant to the Centre of Molecular Biology Severo Ochoa (CBMSO).Springer NatureMinisterio de Economía y Competitividad (España)Fundación Ramón ArecesEuropean CommissionSCOAPConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2020202020192020info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/205007reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2016-76601-C3-1-Rinfo:eu-repo/grantAgreement/EC/H2020/634486info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2016-76601-C3-2-Rinfo:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2016-76601-C3-3-Rhttp://dx.doi.org/10.1038/s41598-019-53948-ySíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2050072026-05-22T06:33:51Z
dc.title.none.fl_str_mv Deciphering the molecular specificity of phenolic compounds as inhibitors or glycosyl acceptors of β-fructofuranosidase from Xanthophyllomyces dendrorhous
title Deciphering the molecular specificity of phenolic compounds as inhibitors or glycosyl acceptors of β-fructofuranosidase from Xanthophyllomyces dendrorhous
spellingShingle Deciphering the molecular specificity of phenolic compounds as inhibitors or glycosyl acceptors of β-fructofuranosidase from Xanthophyllomyces dendrorhous
Ramírez-Escudero, Mercedes
title_short Deciphering the molecular specificity of phenolic compounds as inhibitors or glycosyl acceptors of β-fructofuranosidase from Xanthophyllomyces dendrorhous
title_full Deciphering the molecular specificity of phenolic compounds as inhibitors or glycosyl acceptors of β-fructofuranosidase from Xanthophyllomyces dendrorhous
title_fullStr Deciphering the molecular specificity of phenolic compounds as inhibitors or glycosyl acceptors of β-fructofuranosidase from Xanthophyllomyces dendrorhous
title_full_unstemmed Deciphering the molecular specificity of phenolic compounds as inhibitors or glycosyl acceptors of β-fructofuranosidase from Xanthophyllomyces dendrorhous
title_sort Deciphering the molecular specificity of phenolic compounds as inhibitors or glycosyl acceptors of β-fructofuranosidase from Xanthophyllomyces dendrorhous
dc.creator.none.fl_str_mv Ramírez-Escudero, Mercedes
Míguez, Noa
Gimeno-Pérez, María
Ballesteros Olmo, Antonio
Fernández Lobato, María
Plou Gasca, Francisco José
Sanz-Aparicio, J.
author Ramírez-Escudero, Mercedes
author_facet Ramírez-Escudero, Mercedes
Míguez, Noa
Gimeno-Pérez, María
Ballesteros Olmo, Antonio
Fernández Lobato, María
Plou Gasca, Francisco José
Sanz-Aparicio, J.
author_role author
author2 Míguez, Noa
Gimeno-Pérez, María
Ballesteros Olmo, Antonio
Fernández Lobato, María
Plou Gasca, Francisco José
Sanz-Aparicio, J.
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
Fundación Ramón Areces
European Commission
SCOAP
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description 13 pags., 6 figs., 2 tabs. -- Open Access funded by Creative Commons Atribution Licence 4.0
publishDate 2019
dc.date.none.fl_str_mv 2019
2020
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/205007
url http://hdl.handle.net/10261/205007
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
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info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2016-76601-C3-1-R
info:eu-repo/grantAgreement/EC/H2020/634486
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2016-76601-C3-2-R
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2016-76601-C3-3-R
http://dx.doi.org/10.1038/s41598-019-53948-y
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Springer Nature
publisher.none.fl_str_mv Springer Nature
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
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