Please use this identifier to cite or link to this item: https://hdl.handle.net/11000/30661
Full metadata record
DC FieldValueLanguage
dc.contributor.authorCuyàs, Elisabet-
dc.contributor.authorVerdura, Sara-
dc.contributor.authorLozano Sánchez, Jesús-
dc.contributor.authorViciano, Ignacio-
dc.contributor.authorLlorach-Pares, Laura-
dc.contributor.authorNonell-Canals, Alfons-
dc.contributor.authorBosch-Barrera, Joaquim-
dc.contributor.authorBrunet, Joan-
dc.contributor.authorsegura Carretero, Antonio-
dc.contributor.authorSanchez-Martinez, Melchor-
dc.contributor.authorEncinar, José Antonio-
dc.contributor.authorMENÉNDEZ MENÉNDEZ, JAVIER ABEL-
dc.contributor.otherDepartamentos de la UMH::Bioquímica y Biología Moleculares_ES
dc.date.accessioned2024-01-26T09:12:37Z-
dc.date.available2024-01-26T09:12:37Z-
dc.date.created2019-03-26-
dc.identifier.citationFood and Chemical Toxicology, 128 (2019) 35–45es_ES
dc.identifier.issn0278-6915-
dc.identifier.urihttps://hdl.handle.net/11000/30661-
dc.description.abstractCatechol-containing polyphenols present in coffee and tea, while serving as excellent substrates for catechol-Omethyltransferase (COMT)-catalyzed O-methylation, can also operate as COMT inhibitors. However, little is known about the relationship between COMT and the characteristic phenolics present in extra virgin olive oil (EVOO). We here selected the EVOO dihydroxy-phenol oleacein for a computational study of COMT-driven methylation using classic molecular docking/molecular dynamics simulations and hybrid quantum mechanical/ molecular mechanics, which were supported by in vitro activity studies using human COMT. Oleacein could be superimposed onto the catechol-binding site of COMT, maintaining the interactions with the atomic positions involved in methyl transfer from the S-adenosyl-L-methionine cofactor. The transition state structure for the meta-methylation in the O5 position of the oleacein benzenediol moiety was predicted to occur preferentially. Enzyme analysis of the conversion ratio of catechol to O-alkylated guaiacol confirmed the inhibitory effect of oleacein on human COMT, which remained unaltered when tested against the protein version encoded by the functional Val158Met polymorphism of the COMT gene. Our study provides a theoretical determination of how EVOO dihydroxy-phenols can be metabolized via COMT. The ability of oleacein to inhibit COMT adds a new dimension to the physiological and therapeutic utility of EVOO secoiridoids.es_ES
dc.formatapplication/pdfes_ES
dc.format.extent11es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.rightsinfo:eu-repo/semantics/closedAccesses_ES
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectextra virgin olive oiles_ES
dc.subjectpolyphenolses_ES
dc.subjectsecoiridoidses_ES
dc.subjectoleaceines_ES
dc.subjectCOMTes_ES
dc.subjectcanceres_ES
dc.subject.classificationBioquímica y Biología Moleculares_ES
dc.subject.otherCDU::5 - Ciencias puras y naturales::57 - Biología::577 - Bioquímica. Biología molecular. Biofísicaes_ES
dc.titleThe extra virgin olive oil phenolic oleacein is a dual substrate-inhibitor of catechol-O-methyltransferasees_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherversionhttps:// doi.org/10.1016/j.fct.2019.03.049es_ES
Appears in Collections:
Artículos Bioquímica y Biología Molecular


no-thumbnailView/Open:

 10.1016_j.fct.2019.03.049 (3).pdf



2,83 MB
Adobe PDF
Share:


Creative Commons ???jsp.display-item.text9???