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Sustainable synthesis of uridine-5′-monophosphate analogues by immobilized uracil phosphoribosyltransferase from Thermus thermophilus

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dc.contributor.author Arco Arrieta, Jon del
dc.contributor.author Galindo, Javier
dc.contributor.author Clemente Suárez, Vicente Javier
dc.contributor.author Corrales, Amaira
dc.contributor.author Fernández Lucas, Jesús
dc.date.accessioned 2020-11-20T18:02:38Z
dc.date.available 2020-11-20T18:02:38Z
dc.date.issued 2020
dc.identifier.citation Arco, J., Galindo, J., Clemente, V. J., Corrales, A., & Fernández, J. (2020). Sustainable synthesis of uridine-5′-monophosphate analogues by immobilized uracil phosphoribosyltransferase from Thermus thermophilus. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1868(1), 140251. https://doi.org/10.1016/j.bbapap.2019.07.004 spa
dc.identifier.issn 1570-9639
dc.identifier.issn 1878-1454
dc.identifier.uri http://hdl.handle.net/11268/9501
dc.description.abstract Nowadays enzymatic synthesis of nucleic acid derivatives is gaining momentum over traditional chemical synthetic processes. Biotransformations catalyzed by whole cells or enzymes offer an ecofriendly and efficient alternative to the traditional multistep chemical methods, avoiding the use of chemical reagents and organic solvents that are expensive and environmentally harmful. Herein we report for the first time the covalent immobilization a uracil phosphoribosyltransferase (UPRT). In this sense, UPRT from Thermus thermophilus HB8 was immobilized onto glutaraldehyde-activated MagReSyn®Amine magnetic iron oxide porous microparticles (MTtUPRT). According to the catalyst load experiments, MTtUPRT3 was selected as optimal biocatalyst for further studies. MTtUPRT3 was active and stable in a broad range of temperature (70–100 °C) and in the pH interval 6–8, displaying maximum activity at 100 °C and pH 7 (activity 968 IU/gsupport, retained activity 100%). In addition, MTtUPRT3 could be reused up to 8 times in the synthesis of uridine-5′-monophosphate (UMP). Finally, MTtUPRT3 was successfully applied in the sustainable synthesis of different 5-modified uridine-5′-monophosphates at short times. Taking into account these results, MTtUPRT3 would emerge as a valuable biocatalyst for the synthesis of nucleoside monophosphates through an efficient and environmentally friendly methodology. spa
dc.description.sponsorship Sin financiación spa
dc.language.iso eng spa
dc.title Sustainable synthesis of uridine-5′-monophosphate analogues by immobilized uracil phosphoribosyltransferase from Thermus thermophilus spa
dc.type article spa
dc.description.impact 1.037 SJR (2019) Q1, 21/126 Analytical Chemistry, 24/136 Biophysics; Q2, 145/456 Biochemistry, 193/414 Molecular Biology spa
dc.description.impact No data JCR 2019 spa
dc.description.impact No data IDR 2019 spa
dc.identifier.doi 10.1016/j.bbapap.2019.07.004
dc.rights.accessRights closedAccess spa
dc.subject.uem Biología molecular spa
dc.subject.uem Enzimas spa
dc.subject.uem Bioquímica spa
dc.subject.unesco Biología molecular spa
dc.subject.unesco Enzima spa
dc.subject.unesco Bioquímica spa
dc.description.filiation UEM spa
dc.peerreviewed Si spa


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