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Kinetic characterization of the oxidation of catecolamines and related compounds by laccase

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dc.contributor.authorTaboada Rodriguez, Amaury
dc.contributor.authorManzano Nicolás, Jesús
dc.contributor.authorTeruel Puche, José Antonio
dc.contributor.authorMarín Iniesta, Fulgencio
dc.contributor.authorGarcía Cánovas, Francisco
dc.contributor.authorGarcía Molina, Francisco
dc.contributor.authorTudela Serrano, José
dc.contributor.authorMuñoz Muñoz, José Luis
dc.contributor.departmentBioquímica y Biología Molecular A
dc.date.accessioned2026-01-15T11:19:18Z
dc.date.available2026-01-15T11:19:18Z
dc.date.copyright© 2020 Elsevier B.V.
dc.date.issued2020-07-25
dc.description.abstractThe pathways of melanization and sclerotization of the cuticle in insects are carried out by the action of laccases on dopamine and related compounds. In this work, the laccase action of Trametes versicolor (TvL) on catecholamines and related compounds has been kinetically characterized. Among them, dopamine, l-dopa, l-epinephrine, l-norepinephrine, dl-isoprenaline, l-isoprenaline, dl-α-methyldopa, l-α-methyldopa and l-dopa methylester. A chronometric method has been used, which is based on measuring the lag period necessary to consume a small amount of ascorbic acid, added to the reaction medium. The use of TvL has allowed docking studies of these molecules to be carried out at the active site of this enzyme. The hydrogen bridge interaction between the hydroxyl oxygen at C-4 with His-458, and with the acid group of Asp-206, would make it possible to transfer the electron to the T1 Cu-(II) copper centre of the enzyme. Furthermore, Phe-265 would facilitate the adaptation of the substrate to the enzyme through Π-Π interactions. To kinetically characterize these compounds, we need to take into consideration that, excluding l-dopa, l-α-methyldopa and dl-α-methyldopa, all compounds are in hydrochloride form. Because of this, first we need to kinetically characterize the inhibition by chloride and, after that, calculate the kinetic parameters KM and VmaxS. From the kinetic data obtained, it appears that the best substrate is dopamine. The presence of an isopropyl group bound to nitrogen (isoprenaline) makes it especially difficult to catalyse. The formation of the ester (l-dopa methyl ester) practically does not affect catalysis. The addition of a methyl group (α-methyl dopa) increases the rate but decreases the affinity for catalysis. l-Epinephrine and l-norepinephrine have an affinity similar to isoprenaline, but faster catalysis, probably due to the greater nucleophilic power of their phenolic hydroxyl.
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dc.identifier.citationInternational Journal of Biological Macromolecules, 2020, Vol. 164, pp. 1256-1266
dc.identifier.doihttps://doi.org/10.1016/j.ijbiomac.2020.07.112
dc.identifier.eissn1879-0003
dc.identifier.issn0141-8130
dc.identifier.urihttp://hdl.handle.net/10201/187090
dc.languageeng
dc.publisherElsevier
dc.relationThis work was partially supported by several grants, FEDER RTC-2017-5964-2 InsectFlour project “Aprovechamiento de subproductos industriales agrícolas para la producción de harinas de insectos para consumo humano y animal”/“Exploitation of industrial agronomic by-products to the production of insect flours for human and animal consumption” from Ministerio de Ciencia, Innovacion y Universidades (Madrid, Spain), 20961/PI/18 project and 20809/PI/18 project from Fundacion Seneca (CARM, Murcia, Spain), SAF2016-77241-R from MINECO (Madrid, Spain) and AEIP-15452 project from University of Murcia (Murcia, Spain). JMN has a research contract from RTC-2017-5964-2 project. JM-M receives internal funding from Northumbria University.
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S0141813020338605
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectKinetic
dc.subjectCatecholamines
dc.subjectKinetic characterization
dc.subjectLaccase
dc.subjectDocking
dc.subject.odsObjetivo 6: Agua y saneamiento
dc.titleKinetic characterization of the oxidation of catecolamines and related compounds by laccase
dc.typeinfo:eu-repo/semantics/article
dc.type.versioninfo:eu-repo/semantics/publishedVersion
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