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Molecular docking studies of ortho-substituted phenols to tyrosinase helps discern if a molecule can be an enzyme substrate

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dc.contributor.authorGarcía-Molina, Pablo
dc.contributor.authorGarcía-Cánovas, Francisco
dc.contributor.authorGarcía-Molina, Francisco
dc.contributor.authorMontenegro Arce, María Fernanda
dc.contributor.authorRodríguez López, José Neptuno
dc.contributor.authorTeruel Puche, José Antonio
dc.contributor.authorTudela Serrano, José
dc.contributor.departmentBioquímica y Biología Molecular Aes
dc.date.accessioned2025-04-28T08:09:51Z
dc.date.available2025-04-28T08:09:51Z
dc.date.created2024-05-20
dc.date.issued2024-06-23
dc.descriptionThis manuscript version is made available under the CC-BY 4.0 license http://creativecommons.org/licenses/by/4.0/. The version of a Published Work that appeared in final form in International Journal of Molecular Sciences. To access the final edited and published work https://doi.org/10.3390/ijms25136891
dc.description.abstractPhenolic compounds with a position ortho to the free phenolic hydroxyl group occupied can be tyrosinase substrates. However, ortho-substituted compounds are usually described as inhibitors. The mechanism of action of tyrosinase on monophenols is complex, and if they are ortho-substituted, it is more complicated. It can be shown that many of these molecules can become substrates of the enzyme in the presence of catalytic o-diphenol, MBTH, or in the presence of hydrogen peroxide. Docking studies can help discern whether a molecule can behave as a substrate or inhibitor of the enzyme. Specifically, phenols such as thymol, carvacrol, guaiacol, eugenol, isoeugenol, and ferulic acid are substrates of tyrosinase, and docking simulations to the active center of the enzyme predict this since the distance of the peroxide oxygen from the oxy-tyrosinase form to the ortho position of the phenolic hydroxyl is adequate for the electrophilic attack reaction that gives rise to hydroxylation occurring.es
dc.formatapplication/pdfes
dc.format.extent14es
dc.identifier.citationInternational Journal of Molecular Sciences 2024, 25, 6891
dc.identifier.doihttps://doi.org/10.3390/ijms25136891
dc.identifier.issn1661-6596
dc.identifier.urihttp://hdl.handle.net/10201/153502
dc.languageenges
dc.publisherMDPIes
dc.relationFundacion Seneca, Region of Murcia, Spain, Project 20809/PI/18es
dc.relation.publisherversionhttps://www.mdpi.com/1422-0067/25/13/6891es
dc.relation.requireshttp://hdl.handle.net/10201/153521
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAtribución 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectTyrosinasees
dc.subjectSubstrateses
dc.subjectInhibitorses
dc.subjectOrtho-substituted phenolses
dc.subjectMolecular dockinges
dc.subject.otherCDU::5 - Ciencias puras y naturales::57 - Biología::577 - Bioquímica. Biología molecular. Biofísicaes
dc.titleMolecular docking studies of ortho-substituted phenols to tyrosinase helps discern if a molecule can be an enzyme substratees
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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