1. Universidad Antonio Nariño
  2. Trabajos de grado
  3. Pregrado
  4. Bioquímica
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dc.contributor.advisorMalagon, Edwin-
dc.creatorPaez Pedraza, Leidy Catherine-
dc.date.accessioned2021-02-22T15:25:06Z-
dc.date.available2021-02-22T15:25:06Z-
dc.date.created2020-07-01-
dc.identifier.urihttp://repositorio.uan.edu.co/handle/123456789/1603-
dc.description.abstractThe chemical properties and molecular structure of Canavalia ensiformis urease have been extensively studied. Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea, allowing nitrogen to be available as a nutrient for plants. In agriculture, volatilization nitrogen losses and in medicine gastrointestinal diseases caused by pathogens have made the study of ureases important in several fields of application. The interaction of Jack Bean urease (JBU) with five soluble sulfonated resorcinarenes with different chemical structure was evaluated in terms of activity, interaction mechanism and simulation of molecular coupling. The results of UV-VIS spectroscopy experiments suggest conformational changes in structure that reflect the decrease in enzyme activity by more than 50%, with the strongest strong inhibitor being c-sulfonatoresorcin [4] arene (Na4ESRA), followed by c-propylsulfonaterosorcin [4] arene (Na4PrRA), c ethylsulfonatoresorcin [4] arene (Na4EtRA), c methylsulfonatoresorcin [4] arene (Na4MeRA) and the weakest inhibitor c-methylthioethylsulfonatoresorcin [4] arene (Na4SRA). Docking calculations suggest non-competitive inhibition and show that resorcinarenes bind through hydrophobic interactions to different enzyme domains and that they do not bind to the catalytic sitees_ES
dc.description.tableofcontentsLas propiedades químicas y la estructura molecular de la ureasa de Canavalia ensiformis han sido estudiadas ampliamente. La ureasa es una metaloenzima dependiente de níquel que cataliza la hidrólisis de la urea, permitiendo que el nitrógeno esté disponible como nutriente para las plantas. En la agricultura, las pérdidas de nitrógeno por volatilización y en la medicina las enfermedades gastrointestinales causadas por patógenos han hecho que el estudio de las ureasas sea importante en varios campos de aplicación. La interacción de la ureasa de Jack Bean (JBU) con cinco resorcinarenos sulfonados solubles con diferente estructura química se evaluó en términos de actividad , mecanismo de interacción y simulación de acoplamiento molecular. Los resultados de los experimentos de espectroscopia UV-VIS sugieren cambios conformacionales en la estructura que reflejan la disminucion de la actividad de la enzima en más del 50%, siendo el inhibidor mas fuerte fuerte c-sulfonatoresorcin[4]areno (Na4ESRA), seguido por c-propilsulfonaterosorcin[4]areno (Na4PrRA), c-ethylsulfonatoresorcin[4]areno (Na4EtRA), c-methylsulfonatoresorcin[4]areno (Na4MeRA) y el inhibidor más débil c-metiltioetilsulfonatoresorcin[4]areno (Na4SRA). Los cálculos de acoplamiento sugieren una inhibicion no competitiva y muestran que los resorcinarenos se unen mediante interacciones hidrofóbicas a diferentes dominios de la enzima y que no se unen al sitio catalítico.es_ES
dc.language.isospaes_ES
dc.publisherUniversidad Antonio Nariñoes_ES
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 Estados Unidos de América*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.subjectureasaes_ES
dc.subjectresorcinarenoes_ES
dc.subjectinhibiciónes_ES
dc.subjectNo competitivaes_ES
dc.subjectactividades_ES
dc.subjectenzimáticaes_ES
dc.titleEfecto de una serie de resorcinarenos solubles en la actividad enzimática de ureasa de Jack Bean (canavalia ensiformis)es_ES
dc.publisher.programBioquímicaes_ES
dc.rights.accesRightsrestrictedAccesses_ES
dc.subject.keywordUreasees_ES
dc.subject.keywordresorcinarenees_ES
dc.subject.keywordinhibitiones_ES
dc.subject.keywordnon-competitivees_ES
dc.subject.keywordenzimatices_ES
dc.subject.keywordactivityes_ES
dc.type.spaTrabajo de grado (Pregrado y/o Especialización)es_ES
dc.type.hasVersioninfo:eu-repo/semantics/acceptedVersiones_ES
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dc.description.degreenameBioquímico(a)es_ES
dc.description.degreelevelPregradoes_ES
dc.publisher.facultyFacultad de Cienciases_ES
dc.description.notesPresenciales_ES
dc.publisher.campusBogotá - Circunvalar-
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